|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5285 |
| Enzyme 1 Name |
Acyl-protein thioesterase 1 |
| Enzyme 1 Synonyms |
- Lysophospholipase 1
- 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
3415123  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O75608  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
LYPA1_HUMAN  |
| Enzyme 1 PDB ID |
1FJ2  |
| 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  |
| Enzyme 1 GeneCard ID |
LYPLA1  |
| Enzyme 1 GenAtlas ID |
LYPLA1  |
| Enzyme 1 HGNC ID |
HGNC:6737  |
| Enzyme 1 Chromosome Location |
8 |
| Enzyme 1 Locus |
8q11.23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5287 |
| Enzyme 2 Name |
Calcium-dependent phospholipase A2 precursor |
| Enzyme 2 Synonyms |
- Phosphatidylcholine 2-acylhydrolase
- PLA2-10
- 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 |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
460915  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P39877  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PA2G5_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
PLA2G5  |
| Enzyme 2 GenAtlas ID |
PLA2G5  |
| Enzyme 2 HGNC ID |
HGNC:9038  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36-p34 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
|
| 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 |
- Phosphatidylcholine 2-acylhydrolase GIIF
- GIIF sPLA2
- 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 |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
12276060  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9BZM2  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PA2GF_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
PLA2G2F  |
| Enzyme 3 GenAtlas ID |
PLA2G2F  |
| Enzyme 3 HGNC ID |
HGNC:30040  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p35 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5289 |
| Enzyme 4 Name |
Cytosolic phospholipase A2 |
| Enzyme 4 Synonyms |
- cPLA2
- Phospholipase A2 group IVA[Includes: Phospholipase A2
- Phosphatidylcholine 2- acylhydrolase
- 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 |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
190007  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P47712  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN  |
| Enzyme 4 PDB ID |
1CJY  |
| 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  |
| Enzyme 4 GeneCard ID |
PLA2G4A  |
| Enzyme 4 GenAtlas ID |
PLA2G4A  |
| Enzyme 4 HGNC ID |
HGNC:9035  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1q25 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5290 |
| Enzyme 5 Name |
Phospholipase A2 precursor |
| Enzyme 5 Synonyms |
- Phosphatidylcholine 2- acylhydrolase
- 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 |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
387025  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P04054  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PA21B_HUMAN  |
| 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  |
| Enzyme 5 GeneCard ID |
PLA2G1B  |
| Enzyme 5 GenAtlas ID |
PLA2G1B  |
| Enzyme 5 HGNC ID |
HGNC:9030  |
| Enzyme 5 Chromosome Location |
12 |
| Enzyme 5 Locus |
12q23-q24.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
- Group XIII secretory phospholipase A2-like protein
- GXIII sPLA2-like
- 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 |
|
|
| 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 |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
13560707  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9BX93  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PG12B_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
PLA2G12B  |
| Enzyme 6 GenAtlas ID |
PLA2G12B  |
| Enzyme 6 HGNC ID |
HGNC:18555  |
| Enzyme 6 Chromosome Location |
10 |
| Enzyme 6 Locus |
10q22.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
|
| 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 |
- Group X secretory phospholipase A2
- Phosphatidylcholine 2-acylhydrolase GX
- GX sPLA2
- 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 |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
2289237  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O15496  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PA2GX_HUMAN  |
| 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  |
| Enzyme 7 GeneCard ID |
PLA2G10  |
| Enzyme 7 GenAtlas ID |
PLA2G10  |
| Enzyme 7 HGNC ID |
HGNC:9029  |
| Enzyme 7 Chromosome Location |
16 |
| Enzyme 7 Locus |
16p13.1-p12 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
|
| 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 |
- Phosphatidylcholine 2-acylhydrolase GIIE
- GIIE sPLA2
- 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 |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
7108923  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9NZK7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PA2GE_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
PLA2G2E  |
| Enzyme 8 GenAtlas ID |
PLA2G2E  |
| Enzyme 8 HGNC ID |
HGNC:13414  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p36.13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5295 |
| Enzyme 9 Name |
Acyl-protein thioesterase 2 |
| Enzyme 9 Synonyms |
- Lysophospholipase II
- 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 |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
3859560  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O95372  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
LYPA2_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
LYPLA2  |
| Enzyme 9 GenAtlas ID |
LYPLA2  |
| Enzyme 9 HGNC ID |
HGNC:6738  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.12-p35.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| 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 |
- Lecithin-cholesterol acyltransferase
- 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
307117  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P04180  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
LCAT_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
LCAT  |
| Enzyme 10 GenAtlas ID |
LCAT  |
| Enzyme 10 HGNC ID |
HGNC:6522  |
| Enzyme 10 Chromosome Location |
16 |
| Enzyme 10 Locus |
16q22.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5299 |
| Enzyme 11 Name |
Eosinophil lysophospholipase |
| Enzyme 11 Synonyms |
- Charcot-Leyden crystal protein
- Lysolecithin acylhydrolase
- CLC
- 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 |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
187274  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q05315  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
LPPL_HUMAN  |
| Enzyme 11 PDB ID |
1QKQ  |
| 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  |
| Enzyme 11 GeneCard ID |
CLC  |
| Enzyme 11 GenAtlas ID |
CLC  |
| Enzyme 11 HGNC ID |
HGNC:2014  |
| Enzyme 11 Chromosome Location |
19 |
| Enzyme 11 Locus |
19q13.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- Phosphatidylcholine 2-acylhydrolase GIID
- GIID sPLA2
- PLA2IID
- sPLA(2-IID
- 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 |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
5771420  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UNK4  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PA2GD_HUMAN  |
| 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  |
| Enzyme 12 GeneCard ID |
PLA2G2D  |
| Enzyme 12 GenAtlas ID |
PLA2G2D  |
| Enzyme 12 HGNC ID |
HGNC:9033  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
1p36.12 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5771 |
| Enzyme 13 Name |
Platelet-activating factor acetylhydrolase precursor |
| Enzyme 13 Synonyms |
- PAF acetylhydrolase
- PAF 2-acylhydrolase
- LDL-associated phospholipase A2
- LDL-PLA(2
- 2-acetyl-1-alkylglycerophosphocholine esterase
- 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 |
|
| Enzyme 13 Transmembrane Regions |
Not Available |
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
780133  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q13093  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PAFA_HUMAN  |
| 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  |
| Enzyme 13 GeneCard ID |
PLA2G7  |
| Enzyme 13 GenAtlas ID |
PLA2G7  |
| Enzyme 13 HGNC ID |
HGNC:9040  |
| Enzyme 13 Chromosome Location |
6 |
| Enzyme 13 Locus |
6p21.2-p12 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| 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 |
- PAF acetylhydrolase 29 kDa subunit
- PAF-AH 29 kDa subunit
- PAF-AH subunit gamma
- 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 |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
1122219  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q15102  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PA1B3_HUMAN  |
| Enzyme 14 PDB ID |
1FXW  |
| 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  |
| Enzyme 14 GeneCard ID |
PAFAH1B3  |
| Enzyme 14 GenAtlas ID |
PAFAH1B3  |
| Enzyme 14 HGNC ID |
HGNC:8576  |
| Enzyme 14 Chromosome Location |
19 |
| Enzyme 14 Locus |
19q13.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
|
| 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 |
- PAF acetylhydrolase 30 kDa subunit
- PAF-AH 30 kDa subunit
- PAF-AH subunit beta
- 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 |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
2081614  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P68402  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PA1B2_HUMAN  |
| Enzyme 15 PDB ID |
1FXW  |
| 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  |
| Enzyme 15 GeneCard ID |
PAFAH1B2  |
| Enzyme 15 GenAtlas ID |
PAFAH1B2  |
| Enzyme 15 HGNC ID |
HGNC:8575  |
| Enzyme 15 Chromosome Location |
11 |
| Enzyme 15 Locus |
11q23 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
|
| 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 |
- Group III secretory phospholipase A2
- Phosphatidylcholine 2-acylhydrolase GIII
- 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 |
|
|
| 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 |
|
| Enzyme 16 Transmembrane Regions |
Not Available |
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
7274380  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9NZ20  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PA2G3_HUMAN  |
| 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  |
| Enzyme 16 GeneCard ID |
PLA2G3  |
| Enzyme 16 GenAtlas ID |
PLA2G3  |
| Enzyme 16 HGNC ID |
HGNC:17934  |
| Enzyme 16 Chromosome Location |
22 |
| Enzyme 16 Locus |
22q11.2-q13.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- 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
]
|
| 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 |
- Serine-dependent phospholipase A2
- 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 |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
1765864  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q99487  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PAFA2_HUMAN  |
| 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  |
| Enzyme 17 GeneCard ID |
PAFAH2  |
| Enzyme 17 GenAtlas ID |
PAFAH2  |
| Enzyme 17 HGNC ID |
HGNC:8579  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1p34.3 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- 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
]
- 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
]
- Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM: Platelet-activating factor acetylhydrolases. J Biol Chem. 1997 Jul 18;272(29):17895-8. [PubMed
]
|
| 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 |
|
|
| 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 |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
22761446  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q542Y6  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
Q542Y6_HUMAN  |
| 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  |
| Enzyme 18 GeneCard ID |
Not Available |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
HGNC:18554  |
| 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 |
- 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 |
|
| 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  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
MBOA5_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AC006512  |
| Enzyme 19 GeneCard ID |
Q6P1A2  |
| Enzyme 19 GenAtlas ID |
MBOAT5  |
| Enzyme 19 HGNC ID |
HGNC:30244  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- 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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
12909 |
| Enzyme 20 Name |
1-acylglycerophosphocholine O-acyltransferase 1 |
| Enzyme 20 Synonyms |
- Lung- type acyl-CoA:lysophosphatidylcholine acyltransferase 1
- Acyltransferase-like 2
- 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 |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
100811832  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q8NF37  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PCAT1_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AB244719  |
| Enzyme 20 GeneCard ID |
Q8NF37  |
| Enzyme 20 GenAtlas ID |
LPCAT1  |
| Enzyme 20 HGNC ID |
HGNC:25718  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- 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
]
|
| 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 |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
34364994  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q7L5N7  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
AYTL1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
BX641069  |
| Enzyme 21 GeneCard ID |
Q7L5N7  |
| Enzyme 21 GenAtlas ID |
LPCAT2  |
| Enzyme 21 HGNC ID |
HGNC:26032  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| 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 |
- human
- 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 |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
28193178  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q86U10  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
Q86U10_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
BX247999  |
| Enzyme 22 GeneCard ID |
Q86U10  |
| 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 |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
40674028  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q6P1J6  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
Q6P1J6_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
Not Available |
| Enzyme 23 GenBank Gene ID |
BC065041  |
| Enzyme 23 GeneCard ID |
Q6P1J6  |
| Enzyme 23 GenAtlas ID |
PLB1  |
| Enzyme 23 HGNC ID |
HGNC:30041  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- 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
]
|
| 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 |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
3811347  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P0C869  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PA24B_HUMAN  |
| 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  |
| Enzyme 24 GeneCard ID |
P0C869  |
| Enzyme 24 GenAtlas ID |
PLA2G4B  |
| Enzyme 24 HGNC ID |
HGNC:9036  |
| Enzyme 24 Chromosome Location |
15 |
| Enzyme 24 Locus |
15q11.2-q21.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
158256040  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
A8K5I7  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
A8K5I7_HUMAN  |
| Enzyme 25 PDB ID |
1DB4  |
| 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  |
| Enzyme 25 GeneCard ID |
A8K5I7  |
| 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  |
| 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 |
- 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 |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
Not Available |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
B3KMF3  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
B3KMF3_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AK001705  |
| Enzyme 26 GeneCard ID |
B3KMF3  |
| 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  |
| 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 |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
B0QYE8  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
B0QYE8_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AL022322  |
| Enzyme 27 GeneCard ID |
B0QYE8  |
| 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  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |