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Human Metabolome Database Version 2.5

 

Showing metabocard for LysoPC(16:0) (HMDB10382)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-16 14:19:56
Update Date 2009-10-22 15:35:39
Accession Number HMDB10382
Secondary Accession Numbers Not Available
Common Name LysoPC(16:0)
Description LysoPC(16:0) is a lysophospholipid (LyP). It is a monoglycerophospholipid in which a phosphorylcholine moiety occupies a glycerol substitution site. Lysophosphatidylcholines can have different combinations of fatty acids of varying lengths and saturation attached at the C-1 (sn-1) position. Fatty acids containing 16, 18 and 20 carbons are the most common. LysoPC(16:0), in particular, consists of one chain of palmitic acid at the C-1 position. The palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats. Lysophosphatidylcholine is found in small amounts in most tissues. It is formed by hydrolysis of phosphatidylcholine by the enzyme phospholipase A2, as part of the de-acylation/re-acylation cycle that controls its overall molecular species composition. It can also be formed inadvertently during extraction of lipids from tissues if the phospholipase is activated by careless handling. In blood plasma significant amounts of lysophosphatidylcholine are formed by a specific enzyme system, lecithin:cholesterol acyltransferase (LCAT), which is secreted from the liver. The enzyme catalyzes the transfer of the fatty acids of position sn-2 of phosphatidylcholine to the free cholesterol in plasma, with formation of cholesterol esters and lysophosphatidylcholine. Lysophospholipids have a role in lipid signaling by acting on lysophospholipid receptors (LPL-R). LPL-R's are members of the G protein-coupled receptor family of integral membrane proteins.
Synonyms
  1. LysoPC(16:0/0:0)
  2. Lysophosphatidylcholine(16:0/0:0)
  3. LPC(16:0)
  4. LPC(16:0/0:0)
  5. LyPC(16:0)
  6. LyPC(16:0/0:0)
  7. Lysophosphatidylcholine(16:0)
  8. LysoPC(16:0)
  9. 1-palmitoyl-glycero-3-phosphocholine
  10. 1-palmitoyl-lysophosphatidylcholine
Chemical IUPAC Name 1-hexadecanoyl-glycero-3-phosphocholine
Chemical Formula C24H50NO7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Lysophosphatidylcholines
Family
  • Mammalian Metabolite
Species
  • cation
  • anion
  • secondary alcohol
  • quaternary ammonium salt
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
Source
  • Endogenous
Average Molecular Weight 495.630
Monoisotopic Molecular Weight 495.332489
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OCC[N+](C)(C)C
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C
KEGG Compound ID C04230 Link Image
BioCyc ID PHOSPHATIDYLCHOLINE Link Image
BiGG ID Not Available
Wikipedia Link Lecithin Link Image
NuGOwiki Link HMDB10382 Link Image
Metagene Link HMDB10382 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C24H50NO7P/c1-5-6-7-8-9-10-11-12-13-14-15-16-17-18-24(27)30-21-23(26)22-32-33(28,29)31-20-19-25(2,3)4/h23,26H,5-22H2,1-4H3/t23-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.68e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.83 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
Biofluid Location
  • Blood
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 106.598 +/- 16.732 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments quantified by Lipomics Technologies, Inc.
References
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Acyl-protein thioesterase 1
  2. Calcium-dependent phospholipase A2 precursor
  3. Group IIF secretory phospholipase A2 precursor
  4. Cytosolic phospholipase A2
  5. Phospholipase A2 precursor
  6. Group XIIB secretory phospholipase A2-like protein precursor
  7. Group 10 secretory phospholipase A2 precursor
  8. Group IIE secretory phospholipase A2 precursor
  9. Acyl-protein thioesterase 2
  10. Phosphatidylcholine-sterol acyltransferase precursor
  11. Eosinophil lysophospholipase
  12. Group IID secretory phospholipase A2 precursor
  13. Platelet-activating factor acetylhydrolase precursor
  14. Platelet-activating factor acetylhydrolase IB subunit gamma
  15. Platelet-activating factor acetylhydrolase IB subunit beta
  16. Group 3 secretory phospholipase A2 precursor
  17. Platelet-activating factor acetylhydrolase 2, cytoplasmic
  18. CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
  19. Membrane-bound O-acyltransferase domain-containing protein 5
  20. 1-acylglycerophosphocholine O-acyltransferase 1
  21. Acyltransferase-like 1
  22. Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
  23. Phospholipase B1
  24. Cytosolic phospholipase A2 beta
  25. cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
  26. cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
  27. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5285
Enzyme 1 Name Acyl-protein thioesterase 1
Enzyme 1 Synonyms
  1. Lysophospholipase 1
  2. Lysophospholipase I
Enzyme 1 Gene Name LYPLA1
Enzyme 1 Protein Sequence >Acyl-protein thioesterase 1
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRP
VTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQ
GGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLM
FGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
Enzyme 1 Number of Residues 230
Enzyme 1 Molecular Weight 24670
Enzyme 1 Theoretical pI 6.77
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Also has low lysophospholipase activity
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 3415123 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O75608 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LYPA1_HUMAN Link Image
Enzyme 1 PDB ID 1FJ2 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >693 bp
ATGTGCGGCAATAACATGTCAACCCCGCTGCCCGCCATCGTGCCCGCCGCCCGGAAGGCC
ACCGCTGCGGTGATTTTCCTGCATGGATTGGGAGATACTGGGCACGGATGGGCAGAAGCC
TTTGCAGGTATCAGAAGTTCACATATCAAATATATCTGCCCGCATGCGCCTGTTAGGCCT
GTTACATTAAATATGAACGTGGCTATGCCTTCATGGTTTGATATTATTGGGCTTTCACCA
GATTCACAGGAGGATGAATCTGGGATTAAACAGGCAGCAGAAAATATAAAAGCTTTGATT
GATCAAGAAGTGAAGAATGGCATTCCTTCTAACAGAATTATTTTGGGAGGGTTTTCTCAG
GGAGGAGCTTTATCTTTATATACTGCCCTTACCACACAGCAGAAACTGGCAGGTGTCACT
GCACTCAGTTGCTGGCTTCCACTTCGGGCTTCCTTTCCACAGGGTCCTATCGGTGGTGCT
AATAGAGATATTTCTATTCTCCAGTGCCACGGGGATTGTGACCCTTTGGTTCCCCTGATG
TTTGGTTCTCTTACGGTGGAAAAACTAAAAACATTGGTGAATCCAGCCAATGTGACCTTT
AAAACCTATGAAGGTATGATGCACAGTTCGTGTCAACAGGAAATGATGGATGTCAAGCAA
TTCATTGATAAACTCCTACCTCCAATTGATTGA
Enzyme 1 GenBank Gene ID AF081281 Link Image
Enzyme 1 GeneCard ID LYPLA1 Link Image
Enzyme 1 GenAtlas ID LYPLA1 Link Image
Enzyme 1 HGNC ID HGNC:6737 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS: Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure. 2000 Nov 15;8(11):1137-46. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5287
Enzyme 2 Name Calcium-dependent phospholipase A2 precursor
Enzyme 2 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. PLA2-10
  3. Group V phospholipase A2
Enzyme 2 Gene Name PLA2G5
Enzyme 2 Protein Sequence >Calcium-dependent phospholipase A2 precursor
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 2 Number of Residues 138
Enzyme 2 Molecular Weight 15674
Enzyme 2 Theoretical pI 8.48
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle
Enzyme 2 Pathways
Enzyme 2 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 460915 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 2 GenBank Gene ID U03090 Link Image
Enzyme 2 GeneCard ID PLA2G5 Link Image
Enzyme 2 GenAtlas ID PLA2G5 Link Image
Enzyme 2 HGNC ID HGNC:9038 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36-p34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5288
Enzyme 3 Name Group IIF secretory phospholipase A2 precursor
Enzyme 3 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIF
  2. GIIF sPLA2
  3. sPLA(2-IIF
Enzyme 3 Gene Name PLA2G2F
Enzyme 3 Protein Sequence >Group IIF secretory phospholipase A2 precursor
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 3 Number of Residues 168
Enzyme 3 Molecular Weight 18658
Enzyme 3 Theoretical pI 4.94
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Enzyme 3 Pathways
Enzyme 3 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12276060 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 3 GenBank Gene ID AF306566 Link Image
Enzyme 3 GeneCard ID PLA2G2F Link Image
Enzyme 3 GenAtlas ID PLA2G2F Link Image
Enzyme 3 HGNC ID HGNC:30040 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5289
Enzyme 4 Name Cytosolic phospholipase A2
Enzyme 4 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA[Includes: Phospholipase A2
  3. Phosphatidylcholine 2- acylhydrolase
  4. Lysophospholipase
Enzyme 4 Gene Name PLA2G4A
Enzyme 4 Protein Sequence >Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 4 Number of Residues 749
Enzyme 4 Molecular Weight 85212
Enzyme 4 Theoretical pI 5.03
Enzyme 4 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid catabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 190007 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 4 PDB ID 1CJY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
Enzyme 4 GenBank Gene ID M72393 Link Image
Enzyme 4 GeneCard ID PLA2G4A Link Image
Enzyme 4 GenAtlas ID PLA2G4A Link Image
Enzyme 4 HGNC ID HGNC:9035 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q25
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed Link Image]
  2. Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed Link Image]
  3. Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed Link Image]
  4. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  5. Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed Link Image]
  6. Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5290
Enzyme 5 Name Phospholipase A2 precursor
Enzyme 5 Synonyms
  1. Phosphatidylcholine 2- acylhydrolase
  2. Group IB phospholipase A2
Enzyme 5 Gene Name PLA2G1B
Enzyme 5 Protein Sequence >Phospholipase A2 precursor
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 5 Number of Residues 148
Enzyme 5 Molecular Weight 16360
Enzyme 5 Theoretical pI 7.91
Enzyme 5 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 387025 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 5 GenBank Gene ID M21056 Link Image
Enzyme 5 GeneCard ID PLA2G1B Link Image
Enzyme 5 GenAtlas ID PLA2G1B Link Image
Enzyme 5 HGNC ID HGNC:9030 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12q23-q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed Link Image]
  2. Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed Link Image]
  3. Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5291
Enzyme 6 Name Group XIIB secretory phospholipase A2-like protein precursor
Enzyme 6 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. GXIIB
Enzyme 6 Gene Name PLA2G12B
Enzyme 6 Protein Sequence >Group XIIB secretory phospholipase A2-like protein precursor
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 6 Number of Residues 195
Enzyme 6 Molecular Weight 21659
Enzyme 6 Theoretical pI 5.81
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not known; does not seem to have catalytic activity
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-19
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 13560707 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BX93 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PG12B_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >585 bp
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCCTGTGATTCCCTG
GTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGTCAG
CGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 6 GenBank Gene ID AF349540 Link Image
Enzyme 6 GeneCard ID PLA2G12B Link Image
Enzyme 6 GenAtlas ID PLA2G12B Link Image
Enzyme 6 HGNC ID HGNC:18555 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q22.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5292
Enzyme 7 Name Group 10 secretory phospholipase A2 precursor
Enzyme 7 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 7 Gene Name PLA2G10
Enzyme 7 Protein Sequence >Group 10 secretory phospholipase A2 precursor
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 7 Number of Residues 155
Enzyme 7 Molecular Weight 17132
Enzyme 7 Theoretical pI 6.46
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine
Enzyme 7 Pathways
Enzyme 7 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-21
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 2289237 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 7 GenBank Gene ID U95301 Link Image
Enzyme 7 GeneCard ID PLA2G10 Link Image
Enzyme 7 GenAtlas ID PLA2G10 Link Image
Enzyme 7 HGNC ID HGNC:9029 Link Image
Enzyme 7 Chromosome Location 16
Enzyme 7 Locus 16p13.1-p12
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5294
Enzyme 8 Name Group IIE secretory phospholipase A2 precursor
Enzyme 8 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIE
  2. GIIE sPLA2
  3. sPLA(2-IIE
Enzyme 8 Gene Name PLA2G2E
Enzyme 8 Protein Sequence >Group IIE secretory phospholipase A2 precursor
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 8 Number of Residues 142
Enzyme 8 Molecular Weight 15989
Enzyme 8 Theoretical pI 8.28
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids
Enzyme 8 Pathways
Enzyme 8 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7108923 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 8 GenBank Gene ID AF189279 Link Image
Enzyme 8 GeneCard ID PLA2G2E Link Image
Enzyme 8 GenAtlas ID PLA2G2E Link Image
Enzyme 8 HGNC ID HGNC:13414 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p36.13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5295
Enzyme 9 Name Acyl-protein thioesterase 2
Enzyme 9 Synonyms
  1. Lysophospholipase II
  2. LPL- I
Enzyme 9 Gene Name LYPLA2
Enzyme 9 Protein Sequence >Acyl-protein thioesterase 2
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
Enzyme 9 Number of Residues 231
Enzyme 9 Molecular Weight 24737
Enzyme 9 Theoretical pI 7.25
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3859560 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O95372 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name LYPA2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >696 bp
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
Enzyme 9 GenBank Gene ID AF098668 Link Image
Enzyme 9 GeneCard ID LYPLA2 Link Image
Enzyme 9 GenAtlas ID LYPLA2 Link Image
Enzyme 9 HGNC ID HGNC:6738 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p36.12-p35.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5298
Enzyme 10 Name Phosphatidylcholine-sterol acyltransferase precursor
Enzyme 10 Synonyms
  1. Lecithin-cholesterol acyltransferase
  2. Phospholipid-cholesterol acyltransferase
Enzyme 10 Gene Name LCAT
Enzyme 10 Protein Sequence >Phosphatidylcholine-sterol acyltransferase precursor
MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQL
EAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGV
QIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEY
YRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGS
IKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGR
DFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDP
VGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLG
AYRQGPPASPTASPEPPPPE
Enzyme 10 Number of Residues 440
Enzyme 10 Molecular Weight 49578
Enzyme 10 Theoretical pI 6.04
Enzyme 10 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Central enzyme in the extracellular metabolism of plasma lipoproteins. Among other substrates it esterifies the free cholesterol transported in plasma lipoproteins
Enzyme 10 Pathways
Enzyme 10 Reactions
  • phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-24
Enzyme 10 Transmembrane Regions
  • 199-216
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 307117 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P04180 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name LCAT_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1323 bp
ATGGGGCCGCCCGGCTCCCCATGGCAGTGGGTGACGCTGCTGCTGGGGCTGCTGCTCCCT
CCTGCCGCCCCCTTCTGGCTCCTCAATGTGCTCTTCCCCCCGCACACCACGCCCAAGGCT
GAGCTCAGTAACCACACACGGCCCGTCATCCTCGTGCCCGGCTGCCTGGGGAATCAGCTA
GAAGCCAAGCTGGACAAACCAGATGTGGTGAACTGGATGTGCTACCGCAAGACAGAGGAC
TTCTTCACCATCTGGCTGGATCTCAACATGTTCCTACCCCTTGGGGTAGACTGCTGGATC
GATAACACCAGGGTTGTCTACAACCGGAGCTCTGGGCTCGTGTCCAACGCCCCTGGTGTC
CAGATCCGCGTCCCTGGCTTTGGCAAGACCTACTCTGTGGAGTACCTGGACAGCAGCAAG
CTGGCAGGGTACCTGCACACACTGGTGCAGAACCTGGTCAACAATGGCTACGTGCGGGAC
GAGACTGTGCGCGCCGCCCCCTATGACTGGCGGCTGGAGCCCGGCCAGCAGGAGGAGTAC
TACCGCAAGCTCGCAGGGCTGGTGGAGGAGATGCACGCTGCCTATGGGAAGCCTGTCTTC
CTCATTGGCCACAGCCTCGGCTGTCTACACTTGCTCTATTTCCTGCTGCGCCAGCCCCAG
GCCTGGAAGGACCGCTTTATTGATGGCTTCATCTCTCTTGGGGCTCCCTGGGGTGGCTCC
ATCAAGCCCATGCTGGTCTTGGCCTCAGGTGACAACCAGGGCATCCCCATCATGTCCAGC
ATCAAGCTGAAAGAGGAGCAGCGCATAACCACCACCTCCCCCTGGATGTTTCCCTCTCGC
ATGGCGTGGCCTGAGGACCACGTGTTCATTTCCACACCCAGCTTCAACTACACAGGCCGT
GACTTCCAACGCTTCTTTGCAGACCTGCACTTTGAGGAAGGCTGGTACATGTGGCTGCAG
TCACGTGACCTCCTGGCAGGACTCCCAGCACCTGGTGTGGAAGTATACTGTCTTTACGGC
GTGGGCCTGCCCACGCCCCGCACCTACATCTACGACCACGGCTTCCCCTACACGGACCCT
GTGGGTGTGCTCTATGAGGATGGTGATGACACGGTGGCGACCCGCAGCACCGAGCTCTGT
GGCCTGTGGCAGGGCCGCCAGCCACAGCCTGTGCACCTGCTGCCCCTGCACGGGATACAG
CATCTCAACATGGTCTTCAGCAACCTGACCCTGGAGCACATCAATGCCATCCTGCTGGGT
GCCTACCGCCAGGGTCCCCCTGCATCCCCGACTGCCAGCCCAGAGCCCCCGCCTCCTGAA
TAA
Enzyme 10 GenBank Gene ID M12625 Link Image
Enzyme 10 GeneCard ID LCAT Link Image
Enzyme 10 GenAtlas ID LCAT Link Image
Enzyme 10 HGNC ID HGNC:6522 Link Image
Enzyme 10 Chromosome Location 16
Enzyme 10 Locus 16q22.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R: Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2335-9. [PubMed Link Image]
  2. McLean J, Wion K, Drayna D, Fielding C, Lawn R: Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression. Nucleic Acids Res. 1986 Dec 9;14(23):9397-406. [PubMed Link Image]
  3. Tata F, Chaves ME, Markham AF, Scrace GD, Waterfield MD, McIntyre N, Williamson R, Humphries SE: The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase. Biochim Biophys Acta. 1987 Nov 20;910(2):142-8. [PubMed Link Image]
  4. Rogne S, Skretting G, Larsen F, Myklebost O, Mevag B, Carlson LA, Holmquist L, Gjone E, Prydz H: The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease. Biochem Biophys Res Commun. 1987 Oct 14;148(1):161-9. [PubMed Link Image]
  5. Yang CY, Manoogian D, Pao Q, Lee FS, Knapp RD, Gotto AM Jr, Pownall HJ: Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme. J Biol Chem. 1987 Mar 5;262(7):3086-91. [PubMed Link Image]
  6. Schindler PA, Settineri CA, Collet X, Fielding CJ, Burlingame AL: Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. Protein Sci. 1995 Apr;4(4):791-803. [PubMed Link Image]
  7. Skretting G, Prydz H: An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease. Biochem Biophys Res Commun. 1992 Jan 31;182(2):583-7. [PubMed Link Image]
  8. Klein HG, Lohse P, Pritchard PH, Bojanovski D, Schmidt H, Brewer HB Jr: Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123----Ile) and lecithin-cholesterol acyltransferase (Thr347----Met). J Clin Invest. 1992 Feb;89(2):499-506. [PubMed Link Image]
  9. Taramelli R, Pontoglio M, Candiani G, Ottolenghi S, Dieplinger H, Catapano A, Albers J, Vergani C, McLean J: Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. Hum Genet. 1990 Jul;85(2):195-9. [PubMed Link Image]
  10. Gotoda T, Yamada N, Murase T, Sakuma M, Murayama N, Shimano H, Kozaki K, Albers JJ, Yazaki Y, Akanuma Y: Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency. Lancet. 1991 Sep 28;338(8770):778-81. [PubMed Link Image]
  11. Skretting G, Blomhoff JP, Solheim J, Prydz H: The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families. FEBS Lett. 1992 Sep 14;309(3):307-10. [PubMed Link Image]
  12. Maeda E, Naka Y, Matozaki T, Sakuma M, Akanuma Y, Yoshino G, Kasuga M: Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene. Biochem Biophys Res Commun. 1991 Jul 31;178(2):460-6. [PubMed Link Image]
  13. Funke H, von Eckardstein A, Pritchard PH, Hornby AE, Wiebusch H, Motti C, Hayden MR, Dachet C, Jacotot B, Gerdes U, et al.: Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease. J Clin Invest. 1993 Feb;91(2):677-83. [PubMed Link Image]
  14. Hill JS, O K, Wang X, Pritchard PH: Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism. Biochim Biophys Acta. 1993 Jun 19;1181(3):321-3. [PubMed Link Image]
  15. Steyrer E, Haubenwallner S, Horl G, Giessauf W, Kostner GM, Zechner R: A single G to A nucleotide transition in exon IV of the lecithin: cholesterol acyltransferase (LCAT) gene results in an Arg140 to His substitution and causes LCAT-deficiency. Hum Genet. 1995 Jul;96(1):105-9. [PubMed Link Image]
  16. Wiebusch H, Cullen P, Owen JS, Collins D, Sharp PS, Funke H, Assmann G: Deficiency of lecithin:cholesterol acyltransferase due to compound heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT gene. Hum Mol Genet. 1995 Jan;4(1):143-5. [PubMed Link Image]
  17. Owen JS, Wiebusch H, Cullen P, Watts GF, Lima VL, Funke H, Assmann G: Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene. Hum Mutat. 1996;8(1):79-82. [PubMed Link Image]
  18. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5299
Enzyme 11 Name Eosinophil lysophospholipase
Enzyme 11 Synonyms
  1. Charcot-Leyden crystal protein
  2. Lysolecithin acylhydrolase
  3. CLC
  4. Galectin-10
Enzyme 11 Gene Name CLC
Enzyme 11 Protein Sequence >Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
Enzyme 11 Number of Residues 142
Enzyme 11 Molecular Weight 16481
Enzyme 11 Theoretical pI 7.50
Enzyme 11 GO Classification
Function
  • binding
  • carbohydrate binding
  • sugar binding
Process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function May have both lysophospholipase and carbohydrate-binding activities
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 187274 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q05315 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name LPPL_HUMAN Link Image
Enzyme 11 PDB ID 1QKQ Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
Enzyme 11 GenBank Gene ID L01664 Link Image
Enzyme 11 GeneCard ID CLC Link Image
Enzyme 11 GenAtlas ID CLC Link Image
Enzyme 11 HGNC ID HGNC:2014 Link Image
Enzyme 11 Chromosome Location 19
Enzyme 11 Locus 19q13.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed Link Image]
  2. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed Link Image]
  3. Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed Link Image]
  4. Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed Link Image]
  5. Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5302
Enzyme 12 Name Group IID secretory phospholipase A2 precursor
Enzyme 12 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIID
  2. GIID sPLA2
  3. PLA2IID
  4. sPLA(2-IID
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 12 Gene Name PLA2G2D
Enzyme 12 Protein Sequence >Group IID secretory phospholipase A2 precursor
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 12 Number of Residues 145
Enzyme 12 Molecular Weight 16546
Enzyme 12 Theoretical pI 8.28
Enzyme 12 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-20
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 5771420 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 12 GenBank Gene ID AF112982 Link Image
Enzyme 12 GeneCard ID PLA2G2D Link Image
Enzyme 12 GenAtlas ID PLA2G2D Link Image
Enzyme 12 HGNC ID HGNC:9033 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p36.12
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed Link Image]
  2. Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5771
Enzyme 13 Name Platelet-activating factor acetylhydrolase precursor
Enzyme 13 Synonyms
  1. PAF acetylhydrolase
  2. PAF 2-acylhydrolase
  3. LDL-associated phospholipase A2
  4. LDL-PLA(2
  5. 2-acetyl-1-alkylglycerophosphocholine esterase
  6. 1-alkyl-2-acetylglycerophosphocholine esterase
Enzyme 13 Gene Name PLA2G7
Enzyme 13 Protein Sequence >Platelet-activating factor acetylhydrolase precursor
MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGN
GPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNI
LRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR
DRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDID
HGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMF
PLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFA
TGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGT
NINTTNQHIMLQNSSGIEKYN
Enzyme 13 Number of Residues 441
Enzyme 13 Molecular Weight 50078
Enzyme 13 Theoretical pI 7.61
Enzyme 13 GO Classification
Function
  • 1-alkyl-2-acetylglycerophosphocholine esterase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • 2-acetyl-1-alkylglycerophosphocholine esterase complex
  • protein complex
  • unlocalized protein complex
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids
Enzyme 13 Pathways
Enzyme 13 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-21
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 780133 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q13093 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PAFA_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1326 bp
ATGGTGCCACCCAAATTGCATGTGCTTTTCTGCCTCTGCGGCTGCCTGGCTGTGGTTTAT
CCTTTTGACTGGCAATACATAAATCCTGTTGCCCATATGAAATCATCAGCATGGGTCAAC
AAAATACAAGTACTGATGGCTGCTGCAAGCTTTGGCCAAACTAAAATCCCCCGGGGAAAT
GGGCCTTATTCCGTTGGTTGTACAGACTTAATGTTTGATCACACTAATAAGGGCACCTTC
TTGCGTTTATATTATCCATCCCAAGATAATGATCGCCTTGACACCCTTTGGATCCCAAAT
AAAGAATATTTTTGGGGTCTTAGCAAATTTCTTGGAACACACTGGCTTATGGGCAACATT
TTGAGGTTACTCTTTGGTTCAATGACAACTCCTGCAAACTGGAATTCCCCTCTGAGGCCT
GGTGAAAAATATCCACTTGTTGTTTTTTCTCATGGTCTTGGGGCATTCAGGACACTTTAT
TCTGCTATTGGCATTGACCTGGCATCTCATGGGTTTATAGTTGCTGCTGTAGAACACAGA
GATAGATCTGCATCTGCAACTTACTATTTCAAGGACCAATCTGCTGCAGAAATAGGGGAC
AAGTCTTGGCTCTACCTTAGAACCCTGAAACAAGAGGAGGAGACACATATACGAAATGAG
CAGGTACGGCAAAGAGCAAAAGAATGTTCCCAAGCTCTCAGTCTGATTCTTGACATTGAT
CATGGAAAGCCAGTGAAGAATGCATTAGATTTAAAGTTTGATATGGAACAACTGAAGGAC
TCTATTGATAGGGAAAAAATAGCAGTAATTGGACATTCTTTTGGTGGAGCAACGGTTATT
CAGACTCTTAGTGAAGATCAGAGATTCAGATGTGGTATTGCCCTGGATGCATGGATGTTT
CCACTGGGTGATGAAGTATATTCCAGAATTCCTCAGCCCCTCTTTTTTATCAACTCTGAA
TATTTCCAATATCCTGCTAATATCATAAAAATGAAAAAATGCTACTCACCTGATAAAGAA
AGAAAGATGATTACAATCAGGGGTTCAGTCCACCAGAATTTTGCTGACTTCACTTTTGCA
ACTGGCAAAATAATTGGACACATGCTCAAATTAAAGGGAGACATAGATTCAAATGTAGCT
ATTGATCTTAGCAACAAAGCTTCATTAGCATTCTTACAAAAGCATTTAGGACTTCATAAA
GATTTTGATCAGTGGGACTGCTTGATTGAAGGAGATGATGAGAATCTTATTCCAGGGACC
AACATTAACACAACCAATCAACACATCATGTTACAGAACTCTTCAGGAATAGAGAAATAC
AATTAG
Enzyme 13 GenBank Gene ID U20157 Link Image
Enzyme 13 GeneCard ID PLA2G7 Link Image
Enzyme 13 GenAtlas ID PLA2G7 Link Image
Enzyme 13 HGNC ID HGNC:9040 Link Image
Enzyme 13 Chromosome Location 6
Enzyme 13 Locus 6p21.2-p12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Tjoelker LW, Wilder C, Eberhardt C, Stafforini DM, Dietsch G, Schimpf B, Hooper S, Le Trong H, Cousens LS, Zimmerman GA, et al.: Anti-inflammatory properties of a platelet-activating factor acetylhydrolase. Nature. 1995 Apr 6;374(6522):549-53. [PubMed Link Image]
  2. Tew DG, Southan C, Rice SQ, Lawrence MP, Li H, Boyd HF, Moores K, Gloger IS, Macphee CH: Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins. Arterioscler Thromb Vasc Biol. 1996 Apr;16(4):591-9. [PubMed Link Image]
  3. Tjoelker LW, Eberhardt C, Unger J, Trong HL, Zimmerman GA, McIntyre TM, Stafforini DM, Prescott SM, Gray PW: Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad. J Biol Chem. 1995 Oct 27;270(43):25481-7. [PubMed Link Image]
  4. Stafforini DM, Satoh K, Atkinson DL, Tjoelker LW, Eberhardt C, Yoshida H, Imaizumi T, Takamatsu S, Zimmerman GA, McIntyre TM, Gray PW, Prescott SM: Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase. J Clin Invest. 1996 Jun 15;97(12):2784-91. [PubMed Link Image]
  5. Yamada Y, Yokota M: Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation. Biochem Biophys Res Commun. 1997 Jul 30;236(3):772-5. [PubMed Link Image]
  6. Hiramoto M, Yoshida H, Imaizumi T, Yoshimizu N, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke. Stroke. 1997 Dec;28(12):2417-20. [PubMed Link Image]
  7. Yamada Y, Ichihara S, Fujimura T, Yokota M: Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men. Metabolism. 1998 Feb;47(2):177-81. [PubMed Link Image]
  8. Yoshida H, Imaizumi T, Fujimoto K, Itaya H, Hiramoto M, Yoshimizu N, Fukushi K, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension. Thromb Haemost. 1998 Sep;80(3):372-5. [PubMed Link Image]
  9. Kruse S, Mao XQ, Heinzmann A, Blattmann S, Roberts MH, Braun S, Gao PS, Forster J, Kuehr J, Hopkin JM, Shirakawa T, Deichmann KA: The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma. Am J Hum Genet. 2000 May;66(5):1522-30. Epub 2000 Mar 24. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5777
Enzyme 14 Name Platelet-activating factor acetylhydrolase IB subunit gamma
Enzyme 14 Synonyms
  1. PAF acetylhydrolase 29 kDa subunit
  2. PAF-AH 29 kDa subunit
  3. PAF-AH subunit gamma
  4. PAFAH subunit gamma
Enzyme 14 Gene Name PAFAH1B3
Enzyme 14 Protein Sequence >Platelet-activating factor acetylhydrolase IB subunit gamma
MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRE
LFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAI
VQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVH
SDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP
Enzyme 14 Number of Residues 231
Enzyme 14 Molecular Weight 25735
Enzyme 14 Theoretical pI 6.84
Enzyme 14 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain
Enzyme 14 Pathways
Enzyme 14 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 1122219 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q15102 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PA1B3_HUMAN Link Image
Enzyme 14 PDB ID 1FXW Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >696 bp
ATGAGTGGAGAGGAGAACCCAGCCAGCAAGCCCACGCCGGTGCAGGACGTACAGGGCGAC
GGGCGCTGGATGTCCCTGCACCATCGGTTCGTGGCTGACAGCAAAGATAAGGAACCCGAA
GTCGTCTTCATCGGGGACTCCTTGGTCCAGCTCATGCACCAGTGCGAGATCTGGCGCGAG
CTCTTCTCTCCTCTGCATGCACTTAACTTTGGCATTGGTGGTGACGGCACACAGCATGTA
CTGTGGCGGCTGGAGAATGGGGAGCTGGAACACATCCGGCCCAAGATTGTGGTGGTCTGG
GTGGGCACCAACAACCACGGACACACAGCAGAGCAGGTGACTGGTGGCATCAAGGCCATT
GTGCAACTGGTGAATGAGCGACAGCCCCAGGCCCGGGTTGTGGTGCTGGGCCTGCTTCCG
CGAGGCCAACATCCCAACCCACTTCGGGAGAAGAACCGACAGGTGAACGAGCTGGTACGG
GCGGCACTGGCTGGCCACCCTCGGGCCCACTTCCTAGATGCCGACCCTGGCTTTGTGCAC
TCAGATGGCACCATCAGCCATCATGACATGTATGATTACCTGCATCTGAGCCGCCTGGGC
TACACACCTGTTTGCCGGGCTCTGCACTCCCTGCTTCTGCGTCTGCTGGCCCAAGACCAG
GGCCAAGGTGCTCCCCTGCTGGAGCCCGCACCCTAA
Enzyme 14 GenBank Gene ID D63391 Link Image
Enzyme 14 GeneCard ID PAFAH1B3 Link Image
Enzyme 14 GenAtlas ID PAFAH1B3 Link Image
Enzyme 14 HGNC ID HGNC:8576 Link Image
Enzyme 14 Chromosome Location 19
Enzyme 14 Locus 19q13.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: cDNA cloning of human cytosolic platelet-activating factor acetylhydrolase gamma-subunit and its mRNA expression in human tissues. Biochem Biophys Res Commun. 1995 Sep 5;214(1):180-7. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5780
Enzyme 15 Name Platelet-activating factor acetylhydrolase IB subunit beta
Enzyme 15 Synonyms
  1. PAF acetylhydrolase 30 kDa subunit
  2. PAF-AH 30 kDa subunit
  3. PAF-AH subunit beta
  4. PAFAH subunit beta
Enzyme 15 Gene Name PAFAH1B2
Enzyme 15 Protein Sequence >Platelet-activating factor acetylhydrolase IB subunit beta
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWR
ELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEA
IVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFV
HSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
Enzyme 15 Number of Residues 229
Enzyme 15 Molecular Weight 25570
Enzyme 15 Theoretical pI 5.80
Enzyme 15 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 15 General Function Amino acid transport and metabolism
Enzyme 15 Specific Function Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit
Enzyme 15 Pathways
Enzyme 15 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 2081614 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P68402 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PA1B2_HUMAN Link Image
Enzyme 15 PDB ID 1FXW Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >690 bp
ATGAGCCAAGGAGACTCAAACCCAGCAGCTATTCCGCATGCAGCAGAAGATATTCAAGGA
GATGACCGATGGATGTCTCAGCACAACAGATTTGTTTTGGACTGTAAAGACAAAGAGCCT
GATGTACTGTTCGTGGGAGACTCCATGGTGCAGTTAATGCAGCAATATGAGATATGGCGA
GAGCTTTTTTCCCCACTTCATGCACTGAATTTTGGAATTGGGGGAGATACAACAAGACAT
GTTTTGTGGAGACTAAAGAATGGAGAACTGGAGAATATTAAGCCTAAGGTCATTGTTGTC
TGGGTAGGAACAAATAACCACGAAAATACAGCAGAAGAAGTAGCAGGTGGGATCGAGGCC
ATTGTACAACTTATCAACACAAGGCAGCCACAGGCCAAAATCATTGTATTGGGTTTGTTA
CCTCGAGGTGAGAAACCCAATCCTTTGAGGCAAAAGAACGCCAAGGTGAACCAACTCCTC
AAGGTTTCGCTGCCGAAGCTTGCCAACGTGCAGCTCCTGGATACCGACGGGGGTTTTGTG
CACTCGGACGGTGCCATCTCCTGCCACGACATGTTTGATTTTCTGCATCTGACAGGAGGG
GGCTATGCAAAGATCTGCAAACCCCTGCATGAACTGATCATGCAGTTGTTGGAGGAAACA
CCTGAGGAGAAACAAACCACCATTGCCTGA
Enzyme 15 GenBank Gene ID D63390 Link Image
Enzyme 15 GeneCard ID PAFAH1B2 Link Image
Enzyme 15 GenAtlas ID PAFAH1B2 Link Image
Enzyme 15 HGNC ID HGNC:8575 Link Image
Enzyme 15 Chromosome Location 11
Enzyme 15 Locus 11q23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: Differential tissue distribution of the beta- and gamma-subunits of human cytosolic platelet-activating factor acetylhydrolase (isoform I). Biochem Biophys Res Commun. 1997 Apr 7;233(1):10-3. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5783
Enzyme 16 Name Group 3 secretory phospholipase A2 precursor
Enzyme 16 Synonyms
  1. Group III secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GIII
  3. GIII sPLA2
Enzyme 16 Gene Name PLA2G3
Enzyme 16 Protein Sequence >Group 3 secretory phospholipase A2 precursor
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
Enzyme 16 Number of Residues 509
Enzyme 16 Molecular Weight 57152
Enzyme 16 Theoretical pI 9.23
Enzyme 16 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid catabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine
Enzyme 16 Pathways
Enzyme 16 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-19
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 7274380 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NZ20 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PA2G3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1530 bp
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGGCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
Enzyme 16 GenBank Gene ID AF220490 Link Image
Enzyme 16 GeneCard ID PLA2G3 Link Image
Enzyme 16 GenAtlas ID PLA2G3 Link Image
Enzyme 16 HGNC ID HGNC:17934 Link Image
Enzyme 16 Chromosome Location 22
Enzyme 16 Locus 22q11.2-q13.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5785
Enzyme 17 Name Platelet-activating factor acetylhydrolase 2, cytoplasmic
Enzyme 17 Synonyms
  1. Serine-dependent phospholipase A2
  2. HSD-PLA2
Enzyme 17 Gene Name PAFAH2
Enzyme 17 Protein Sequence >Platelet-activating factor acetylhydrolase 2, cytoplasmic
MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCT
GLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAF
CMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHV
RNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGA
TAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQ
HEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKH
LDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL
Enzyme 17 Number of Residues 392
Enzyme 17 Molecular Weight 44036
Enzyme 17 Theoretical pI 6.89
Enzyme 17 GO Classification
Function
  • 1-alkyl-2-acetylglycerophosphocholine esterase activity
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • 2-acetyl-1-alkylglycerophosphocholine esterase complex
  • protein complex
  • unlocalized protein complex
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme
Enzyme 17 Pathways
Enzyme 17 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 1765864 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q99487 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PAFA2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1179 bp
ATGGGGGTCAACCAGTCTGTGGGCTTTCCACCTGTCACAGGACCCCACCTCGTAGGCTGT
GGGGATGTGATGGAGGGTCAGAATCTCCAGGGGAGCTTCTTTCGACTCTTCTACCCCTGC
CAAAAGGCAGAGGAGACCATGGAGCAGCCCCTGTGGATTCCCCGCTATGAGTACTGCACT
GGCCTGGCCGAGTACCTGCAGTTTAATAAGCGCTGCGGGGGCTTGCTGTTCAACCTGGCG
GTGGGATCTTGTCGCCTGCCTGTTAGCTGGAATGGCCCCTTTAAGACAAAGGACTCTGGA
TACCCCTTGATCATCTTCTCCCATGGCCTAGGAGCCTTCAGGACTTTGTATTCAGCCTTC
TGCATGGAGCTGGCCTCACGTGGCTTTGTGGTTGCTGTGCCAGAGCACAGGGACCGGTCA
GCGGCAACCACCTATTTCTGCAAGCAGGCCCCAGAAGAGAACCAGCCCACCAATGAATCG
CTGCAGGAGGAATGGATCCCTTTCCGTCGAGTTGAGGAAGGGGAGAAGGAATTTCATGTT
CGGAATCCCCAGGTGCATCAGCGGGTAAGCGAGTGTTTACGGGTGTTGAAGATCCTGCAA
GAGGTCACTGCTGGGCAGACTGTCTTCAACATCTTGCCTGGTGGCTTGGATCTGATGACT
TTGAAGGGCAACATTGACATGAGCCGTGTGGCTGTGATGGGACATTCATTTGGAGGGGCC
ACAGCTATTCTGGCTTTGGCCAAGGAGACCCAATTTCGGTGTGCGGTGGCTCTGGATGCT
TGGATGTTTCCTCTGGAACGTGACTTTTACCCCAAGGCCCGAGGACCTGTGTTCTTTATC
AATACTGAGAAATTCCAGACAATGGAGAGTGTCAATTTGATGAAGAAGATATGTGCCCAG
CATGAACAGTCTAGGATCATAACCGTTCTTGGTTCTGTTCATCGGAGTCAAACTGACTTT
GCTTTTGTGACTGGCAACTTGATTGGTAAATTCTTCTCCACTGAAACCCGTGGGAGCCTG
GACCCCTATGAAGGGCAGGAGGTTATGGTACGGGCCATGTTGGCCTTCCTGCAGAAGCAC
CTCGACCTGAAAGAAGACTATAATCAATGGAACAACCTTATTGAAGGCATTGGACCGTCG
CTCACCCCAGGGGCCCCCCACCATCTGTCCAGCCTGTAG
Enzyme 17 GenBank Gene ID D87845 Link Image
Enzyme 17 GeneCard ID PAFAH2 Link Image
Enzyme 17 GenAtlas ID PAFAH2 Link Image
Enzyme 17 HGNC ID HGNC:8579 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1p34.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Hattori K, Adachi H, Matsuzawa A, Yamamoto K, Tsujimoto M, Aoki J, Hattori M, Arai H, Inoue K: cDNA cloning and expression of intracellular platelet-activating factor (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase. J Biol Chem. 1996 Dec 20;271(51):33032-8. [PubMed Link Image]
  2. Rice SQ, Southan C, Boyd HF, Terrett JA, MacPhee CH, Moores K, Gloger IS, Tew DG: Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor. Biochem J. 1998 Mar 15;330 ( Pt 3):1309-15. [PubMed Link Image]
  3. Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM: Platelet-activating factor acetylhydrolases. J Biol Chem. 1997 Jul 18;272(29):17895-8. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8755
Enzyme 18 Name CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name Not Available
Enzyme 18 Protein Sequence >CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 18 Number of Residues 189
Enzyme 18 Molecular Weight 21067
Enzyme 18 Theoretical pI 7.27
Enzyme 18 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways
Enzyme 18 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-22
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 22761446 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q542Y6 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q542Y6_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
Enzyme 18 GenBank Gene ID AK075389 Link Image
Enzyme 18 GeneCard ID Not Available
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID HGNC:18554 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs Not Available
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 12907
Enzyme 19 Name Membrane-bound O-acyltransferase domain-containing protein 5
Enzyme 19 Synonyms
  1. O-acyltransferase domain-containing protein 5
Enzyme 19 Gene Name MBOAT5
Enzyme 19 Protein Sequence >Membrane-bound O-acyltransferase domain-containing protein 5
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRH
YLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCF
QMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRG
VPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFY
LVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGL
GFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKE
LSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFY
YLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRK
EKLKKME
Enzyme 19 Number of Residues 487
Enzyme 19 Molecular Weight 56036
Enzyme 19 Theoretical pI 8.87
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 44-64 84-104 111-131 180-200 227-247 285-305 364-384 422-442 453-473
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID Q6P1A2 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name MBOA5_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AC006512 Link Image
Enzyme 19 GeneCard ID Q6P1A2 Link Image
Enzyme 19 GenAtlas ID MBOAT5 Link Image
Enzyme 19 HGNC ID HGNC:30244 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 12909
Enzyme 20 Name 1-acylglycerophosphocholine O-acyltransferase 1
Enzyme 20 Synonyms
  1. Lung- type acyl-CoA:lysophosphatidylcholine acyltransferase 1
  2. Acyltransferase-like 2
  3. Phosphonoformate immuno-associated protein 3
Enzyme 20 Gene Name AYTL2
Enzyme 20 Protein Sequence >1-acylglycerophosphocholine O-acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Enzyme 20 Number of Residues 534
Enzyme 20 Molecular Weight 59152
Enzyme 20 Theoretical pI 5.82
Enzyme 20 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Acetyltransferase which mediates the convertion of 1- acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Has a calcium-independent activity. Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1- palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant thereby playing a pivotal role in respiratory physiology
Enzyme 20 Pathways
Enzyme 20 Reactions
  • acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318] ALL_REAC R01318
  • (other) R04480
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 58-78
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 100811832 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q8NF37 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PCAT1_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AB244719 Link Image
Enzyme 20 GeneCard ID Q8NF37 Link Image
Enzyme 20 GenAtlas ID LPCAT1 Link Image
Enzyme 20 HGNC ID HGNC:25718 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 12910
Enzyme 21 Name Acyltransferase-like 1
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name AYTL1
Enzyme 21 Protein Sequence >Acyltransferase-like 1
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
Enzyme 21 Number of Residues 544
Enzyme 21 Molecular Weight 60208
Enzyme 21 Theoretical pI 6.51
Enzyme 21 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Probable acetyltransferase
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 58-78
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 34364994 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q7L5N7 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name AYTL1_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID BX641069 Link Image
Enzyme 21 GeneCard ID Q7L5N7 Link Image
Enzyme 21 GenAtlas ID LPCAT2 Link Image
Enzyme 21 HGNC ID HGNC:26032 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 12921
Enzyme 22 Name Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
Enzyme 22 Synonyms
  1. human
  2. HCG23215, isoform CRA_b
Enzyme 22 Gene Name Not Available
Enzyme 22 Protein Sequence >Full-length cDNA clone CS0DM001YM08 of Fetal liver of Homo sapiens
MAGPSPPLRAGVGRRLLGVAHPDLRPCLCGELQVEGGPGPVPGMLRTCYVRSPWRRGPSS
ARGEQSGSGHLEQEEVQSGSLLFRLLLFLSRSPASRNQRILYTVLECQPLFDSSDMTIAE
WVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSD
GRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADI
TINRELVRKVDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGN
GPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGFDMTSEAALA
KLSYVLGQPGLSLDVRKELLTKDLRGEMTPPSVEERRPSLQGNTLGGGVSWLLSLSGSQE
ADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAA
Enzyme 22 Number of Residues 469
Enzyme 22 Molecular Weight 50186
Enzyme 22 Theoretical pI 6.83
Enzyme 22 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Amino acid transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 28193178 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q86U10 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q86U10_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID BX247999 Link Image
Enzyme 22 GeneCard ID Q86U10 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs Not Available
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12922
Enzyme 23 Name Phospholipase B1
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name PLB1
Enzyme 23 Protein Sequence >Phospholipase B1
MEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKLEVREGAEIRCPD
KDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQYRGLSWSVGGDE
NIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDLPVQARRLVDLMK
NDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDILHAEVPRAFVNL
VTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEFNKKFQEKTHQLI
ESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKSHSRAASALWNNM
LEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDRAPSALHPTSVHA
LRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYRESKPGFLSDSWVSKSNRK
CTRKAPNP
Enzyme 23 Number of Residues 488
Enzyme 23 Molecular Weight 54342
Enzyme 23 Theoretical pI 7.29
Enzyme 23 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 40674028 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q6P1J6 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name Q6P1J6_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID BC065041 Link Image
Enzyme 23 GeneCard ID Q6P1J6 Link Image
Enzyme 23 GenAtlas ID PLB1 Link Image
Enzyme 23 HGNC ID HGNC:30041 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 14866
Enzyme 24 Name Cytosolic phospholipase A2 beta
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name PLA2G4B
Enzyme 24 Protein Sequence >MEKAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVWNQSFHFRIHR
QLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEGRLEVEFRLQS
LADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGPQEASVGTGTF
RFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMRVELKKEAGLR
ELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIMATGGGIRAMT
SLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTELLKTQVTKNK
LGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLSDQREALSHGQ
NPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEFFMGQLMKRLP
ESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPLLKIEEPPSTA
GRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGLPNQLTPSEPH
LCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQEQGIPFPPISP
SPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEAAAGEVNLSSS
DSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRPH
Enzyme 24 Number of Residues 781
Enzyme 24 Molecular Weight 88066
Enzyme 24 Theoretical pI 5.85
Enzyme 24 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid catabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 3811347 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P0C869 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PA24B_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3039 bp
ATGGCGGAGGCGGCTTTGGAAGCCGTGCGGAGCGAGTTACGAGAATTCCCGGCCGCTGCA
AGGGAGCTCTGCGTGCCTCTTGCTGTGCCCTACCTGGACAAACCCCCAACTCCGCTCCAC
TTCTACCGGGACTGGGTCTGCCCCAACAGGCCGTGCATTATCCGCAACGCTCTGCAGCAC
TGGCCGGCCCTCCAGAAGTGGTCCCTCCCCTATTTCAGAGCCACAGTGGGCTCCACAGAG
GTGAGTGTGGCCGTGACCCCAGATGGTTACGCGGATGCCGTGAGAGGGGATCGCTTCATG
ATGCCAGCTGAGCGCCGCCTGCCCCTGAGCTTCGTGCTGGATGTGCTGGAGGGCCGGGCC
CAGCACCCTGGAGTCCTCTATGTGCAGAAGCAGTGCTCCAACCTGCCCAGCGAGCTGCCC
CAGCTGCTGCCTGATCTGGAATCCCATGTGCCCTGGGCCTCCGAAGCCCTGGGAAAGATG
CCCGATGCTGTGAACTTCTGGCTGGGGGAGGCGGCTGCAGTGACTTCTTTGCACAAGGAC
CACTATGAGAACCTCTACTGCGTGGTCTCAGGAGAGAAGCATTTCCTGTTCCATCCGCCC
AGCGACCGGCCCTTCATCCCCTATGAGCTGTACACGCCGGCAACCTACCAGCTAACTGAA
GAGGGCACCTTTAAGGTGGTGGATGAAGAGGCCATGGAGAAGGCAGAGGTGTCCAGGACC
TGCCTGCTCACGGTTCGTGTCCTGCAGGCCCATCGCCTACCCTCTAAGGACCTAGTGACC
CCCTCTGACTGCTACGTGACTCTCTGGCTGCCCACGGCCTGCAGCCACAGGCTCCAGACA
CGCACGGTCAAGAACAGCAGTAGCCCTGTCTGGAACCAGAGCTTTCACTTCAGGATCCAC
AGGCAGCTCAAGAATGTCATGGAACTGAAAGTCTTTGACCAGGACCTGGTGACCGGAGAT
GACCCTGTGTTGTCAGTACTGTTTGATGCGGGGACTCTGCGGGCTGGGGAGTTCCGGCGC
GAGAGCTTCTCACTGAGCCCTCAGGGTGAGGGGCGCCTGGAAGTTGAATTTCGCCTGCAG
AGTCTGGCTGACCGTGGCGAGTGGCTCGTCAGCAATGGCGTTCTGGTGGCCCGGGAGCTC
TCCTGCTTGCACGTTCAACTGGAGGAGACAGGAGACCAGAAGTCCTCAGAGCACAGAGTT
CAGCTTGTGGTTCCTGGGTCCTGTGAGGGTCCGCAGGAGGCCTCTGTGGGCACTGGCACC
TTCCGCTTCCACTGCCCAGCCTGCTGGGAGCAGGAGCTGAGTATTCGCCTGCAGGATGCC
CCCGAGGAGCAACTAAAGGCGCCACTGAGTGCCCTGCCCTCTGGTCAAGTGGTGAGGCTT
GTCTTCCCCACGTCCCAGGAGCCCCTGATGAGAGTGGAGCTGAAAAAAGAAGCAGGACTG
AGGGAGCTGGCCGTGCGACTGGGCTTCGGGCCCTGTGCAGAGGAGCAGGCCTTCCTGAGC
AGGAGGAAGCAGGTGGTGGCCGCGGCCTTGAGGCAGGCCCTGCAGCTGGATGGAGACCTG
CAGGAGGATGAGATCCCAGTGGTAGCTATTATGGCCACTGGTGGTGGGATCCGGGCAATG
ACTTCCCTGTATGGGCAGCTGGCTGGCCTGAAGGAGCTGGGCCTCTTGGATTGCGTCTCC
TACATCACCGGGGCCTCGGGCTCCACCTGGGCCTTGGCCAACCTTTATGAGGACCCAGAG
TGGTCTCAGAAGGACCTGGCAGGGCCCACTGAGTTGCTGAAGACCCAGGTGACCAAGAAC
AAGCTGGGTGTGCTGGCCCCCAGCCAGCTGCAGCGGTACCGGCAGGAGCTGGCCGAGCGT
GCCCGCTTGGGCTACCCAAGCTGCTTCACCAACCTGTGGGCCCTCATCAACGAGGCGCTG
CTGCATGATGAGCCCCATGATCACAAGCTCTCAGATCAACGGGAGGCCCTGAGTCATGGC
CAGAACCCTCTGCCCATCTACTGTGCCCTCAACACCAAAGGGCAGAGCCTGACCACTTTT
GAATTTGGGGAGTGGTGCGAGTTCTCTCCCTACGAGGTCGGCTTCCCCAAGTACGGGGCC
TTCATCCCCTCTGAGCTCTTTGGCTCCGAGTTCTTTATGGGGCAGCTGATGAAGAGGCTT
CCTGAGTCCCGCATCTGCTTCTTAGAAGGTATCTGGAGCAACCTGTATGCAGCCAACCTC
CAGGACAGCTTATACTGGGCCTCAGAGCCCAGCCAGTTCTGGGACCGCTGGGTCAGGAAC
CAGGCCAACCTGGACAAGGAGCAGGTCCCCCTTCTGAAGATAGAAGAACCACCCTCAACA
GCCGGCAGRATAGCTGAGTTTTTCACCGATCTTCTGACGTGGCGTCCACTGGCCCAGGCC
ACACATAATTTCCTGCGTGGCCTCCATTTCCACAAAGACTACTTTCAGCATCCTCACTTC
TCCACATGGAAAGCTACCACTCTGGATGGGCTCCCCAACCAGCTGACACCCTCGGAGCCC
CACCTGTGCCTGCTGGATGTTGGCTACCTCATCAATACCAGCTGCCTGCCCCTCCTGCAG
CCCACTCGGGACGTGGACCTCATCCTGTCATTGGACTACAACCTCCACGGAGCCTTCCAG
CAGTTGCAGCTCCTGGGCCGGTTCTGCCAGGAGCAGGGGATCCCGTTCCCACCCATCTCG
CCCAGCCCCGAAGAGCAGCTCCAGCCTCGGGAGTGCCACACCTTCTCCGACCCCACCTGC
CCCGGAGCCCCTGCGGTGCTGCACTTTCCTCTGGTCAGCGACTCCTTCCGGGAGTACTCG
GCCCCTGGGGTCCGGCGGACACCCGAGGAGGCGGCAGCTGGGGAGGTGAACCTGTCTTCA
TCGGACTCTCCCTACCACTACACGAAGGTGACCTACAGCCAGGAGGACGTGGACAAGCTG
CTGCACCTGACACATTACAATGTCTGCAACAACCAGGAGCAGCTGCTGGAGGCTCTGCGC
CAGGCAGTGCAGCGGAGGCGGCAGCGCAGGCCCCACTGA
Enzyme 24 GenBank Gene ID AF065215 Link Image
Enzyme 24 GeneCard ID P0C869 Link Image
Enzyme 24 GenAtlas ID PLA2G4B Link Image
Enzyme 24 HGNC ID HGNC:9036 Link Image
Enzyme 24 Chromosome Location 15
Enzyme 24 Locus 15q11.2-q21.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed Link Image]
  2. Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15299
Enzyme 25 Name cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name PLA2G2A
Enzyme 25 Protein Sequence >cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
Enzyme 25 Number of Residues 144
Enzyme 25 Molecular Weight 16083
Enzyme 25 Theoretical pI 9.51
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function Not Available
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 158256040 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID A8K5I7 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name A8K5I7_HUMAN Link Image
Enzyme 25 PDB ID 1DB4 Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 25 GenBank Gene ID AK291302 Link Image
Enzyme 25 GeneCard ID A8K5I7 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16479
Enzyme 26 Name cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
Enzyme 26 Synonyms
  1. SubName: Lysophospholipase 3 (Lysosomal phospholipase A2), isoform CRA_a
Enzyme 26 Gene Name LYPLA3
Enzyme 26 Protein Sequence >cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Enzyme 26 Number of Residues 412
Enzyme 26 Molecular Weight 46658
Enzyme 26 Theoretical pI 6.72
Enzyme 26 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein Not Available
Enzyme 26 UniProtKB/Swiss-Prot ID B3KMF3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name B3KMF3_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AK001705 Link Image
Enzyme 26 GeneCard ID B3KMF3 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location 16
Enzyme 26 Locus 16q22.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16561
Enzyme 27 Name Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name PLA2G6
Enzyme 27 Protein Sequence >Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEK
RTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSM
AYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPA
ELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGG
LLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNP
WELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVS
DTVLVNALWETEVYIYEHREEFQKLIQLLLSP
Enzyme 27 Number of Residues 752
Enzyme 27 Molecular Weight 84094
Enzyme 27 Theoretical pI 7.24
Enzyme 27 GO Classification
Function
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID B0QYE8 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name B0QYE8_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AL022322 Link Image
Enzyme 27 GeneCard ID B0QYE8 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location 22
Enzyme 27 Locus 22q13.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available