| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:57:41 |
| Accession Number |
HMDB00114 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Glycerylphosphorylethanolamine |
| Description |
A membrane breakdown product resulting from the cleavage of the lipid group from glycerophosphoethanlomine fatty acids (i.e. phosphatidylethanolamine). It acts as a growth stimulant for hepatocytes. |
| Synonyms |
- 2-aminoethyl ester 1-Glycerophosphoric acid
- GPEA
- Glycerol 3-phosphoethanolamine
- Glycerol 3-phosphorylethanolamine
- Glycerophosphoethanolamine
- Glycerophosphorylethanolamine
- Glyceryl-3-phosphorylethanolamine
- Glycerylphosphorylethanolamine
- a-Glycerophosphorylethanolamine
- alpha-Glycerophosphorylethanolamine
|
| Chemical IUPAC Name |
2-aminoethyl 2,3-dihydroxypropyl hydrogen phosphate |
| Chemical Formula |
C5H14NO6P |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
- Miscellaneous alcohol phosphates
|
| Family |
|
| Species |
- primary alcohol
- secondary alcohol
- 1,2-diol
- phosphoric acid amide
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
215.141 |
| Monoisotopic Molecular Weight |
215.055878 |
| Isomeric SMILES |
OCCN(CC(O)CO)P(O)(O)=O |
| Canonical SMILES |
OCCN(CC(O)CO)P(O)(O)=O |
| KEGG Compound ID |
C01233  |
| BioCyc ID |
Not Available |
| BiGG ID |
Not Available |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB00114  |
| Metagene Link |
HMDB00114  |
| METLIN ID |
5151  |
| PubChem Compound |
123874  |
| PubChem Substance |
700620  |
| ChEBI ID |
Not Available |
| CAS Registry Number |
1190-00-7 |
| InChI Identifier |
InChI=1/C5H14NO6P/c7-2-1-6(13(10,11)12)3-5(9)4-8/h5,7-9H,1-4H2,(H2,10,11,12) |
| Synthesis Reference |
Tronconi, Giovanni. Process for the chromatographic isolation of 1-(a)-glycerylphosphorylcholine and of L-(a)-glycerylphosphorylethanolamine. PCT Int. Appl. (1990), 18 pp. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
29.2 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-2 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-1.90 [Predicted by ALOGPS]; -3.4 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
Not Available |
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Not Available |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
|
| Biofluid Location |
Not Available |
| Tissue Location |
| Tissue |
References |
| Brain |
— |
| Liver |
— |
|
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Kish SJ, Robitaille Y, Ball M, Gilbert J, Deck JH, Chang LJ, Schut L: Glycerophosphoethanolamine concentration is elevated in brain of patients with dominantly inherited olivopontocerebellar atrophy. Neurosci Lett. 1990 Dec 11;120(2):209-11. [PubMed
]
- Perry TL, Hansen S, Gandham SS: Postmortem changes of amino compounds in human and rat brain. J Neurochem. 1981 Feb;36(2):406-10. [PubMed
]
- Nitsch RM, Blusztajn JK, Pittas AG, Slack BE, Growdon JH, Wurtman RJ: Evidence for a membrane defect in Alzheimer disease brain. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1671-5. [PubMed
]
- Jensen JE, Drost DJ, Menon RS, Williamson PC: In vivo brain (31)P-MRS: measuring the phospholipid resonances at 4 Tesla from small voxels. NMR Biomed. 2002 Aug;15(5):338-47. [PubMed
]
- Nelson C, Moffat B, Jacobsen N, Henzel WJ, Stults JT, King KL, McMurtrey A, Vandlen R, Spencer SA: Glycerophosphorylethanolamine (GPEA) identified as an hepatocyte growth stimulator in liver extracts. Exp Cell Res. 1996 Nov 25;229(1):20-6. [PubMed
]
- Fallbrook A, Turenne SD, Mamalias N, Kish SJ, Ross BM: Phosphatidylcholine and phosphatidylethanolamine metabolites may regulate brain phospholipid catabolism via inhibition of lysophospholipase activity. Brain Res. 1999 Jul 10;834(1-2):207-10. [PubMed
]
|
| Metabolic Enzymes |
- Acyl-protein thioesterase 1
- Cytosolic phospholipase A2
- Acyl-protein thioesterase 2
- Eosinophil lysophospholipase
- Glycerophosphodiester phosphodiesterase 1
- MHC class I antigen
- cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
|
|
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 |
5289 |
| Enzyme 2 Name |
Cytosolic phospholipase A2 |
| Enzyme 2 Synonyms |
- cPLA2
- Phospholipase A2 group IVA[Includes: Phospholipase A2
- Phosphatidylcholine 2- acylhydrolase
- Lysophospholipase
|
| Enzyme 2 Gene Name |
PLA2G4A |
| Enzyme 2 Protein Sequence |
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
|
| Enzyme 2 Number of Residues |
749 |
| Enzyme 2 Molecular Weight |
85212 |
| Enzyme 2 Theoretical pI |
5.03 |
| Enzyme 2 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 2 General Function |
Not Available |
| Enzyme 2 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 2 Pathways |
|
| Enzyme 2 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
190007  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P47712  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN  |
| Enzyme 2 PDB ID |
1CJY  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
M72393  |
| Enzyme 2 GeneCard ID |
PLA2G4A  |
| Enzyme 2 GenAtlas ID |
PLA2G4A  |
| Enzyme 2 HGNC ID |
HGNC:9035  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1q25 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5295 |
| Enzyme 3 Name |
Acyl-protein thioesterase 2 |
| Enzyme 3 Synonyms |
- Lysophospholipase II
- LPL- I
|
| Enzyme 3 Gene Name |
LYPLA2 |
| Enzyme 3 Protein Sequence |
>Acyl-protein thioesterase 2
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
|
| Enzyme 3 Number of Residues |
231 |
| Enzyme 3 Molecular Weight |
24737 |
| Enzyme 3 Theoretical pI |
7.25 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 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 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
3859560  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O95372  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
LYPA2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>696 bp
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
|
| Enzyme 3 GenBank Gene ID |
AF098668  |
| Enzyme 3 GeneCard ID |
LYPLA2  |
| Enzyme 3 GenAtlas ID |
LYPLA2  |
| Enzyme 3 HGNC ID |
HGNC:6738  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p36.12-p35.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5299 |
| Enzyme 4 Name |
Eosinophil lysophospholipase |
| Enzyme 4 Synonyms |
- Charcot-Leyden crystal protein
- Lysolecithin acylhydrolase
- CLC
- Galectin-10
|
| Enzyme 4 Gene Name |
CLC |
| Enzyme 4 Protein Sequence |
>Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
|
| Enzyme 4 Number of Residues |
142 |
| Enzyme 4 Molecular Weight |
16481 |
| Enzyme 4 Theoretical pI |
7.50 |
| Enzyme 4 GO Classification |
| Function |
- binding
- carbohydrate binding
- sugar binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
May have both lysophospholipase and carbohydrate-binding activities |
| 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 |
187274  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q05315  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
LPPL_HUMAN  |
| Enzyme 4 PDB ID |
1QKQ  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
|
| Enzyme 4 GenBank Gene ID |
L01664  |
| Enzyme 4 GeneCard ID |
CLC  |
| Enzyme 4 GenAtlas ID |
CLC  |
| Enzyme 4 HGNC ID |
HGNC:2014  |
| Enzyme 4 Chromosome Location |
19 |
| Enzyme 4 Locus |
19q13.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
13050 |
| Enzyme 5 Name |
Glycerophosphodiester phosphodiesterase 1 |
| Enzyme 5 Synonyms |
- Membrane interacting protein of RGS16
- RGS16-interacting membrane protein
|
| Enzyme 5 Gene Name |
GDE1 |
| Enzyme 5 Protein Sequence |
>Glycerophosphodiester phosphodiesterase 1
MWLWEDQGGLLGPFSFLLLVLLLVTRSPVNACLLTGSLFVLLRVFSFEPVPSCRALQVLK
PRDRISAIAHRGGSHDAPENTLAAIRQAAKNGATGVELDIEFTSDGIPVLMHDNTVDRTT
DGTGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLNHNLTIFFDVKGHAH
KATEALKKMYMEFPQLYNNSVVCSFLPEVIYKMRQTDRDVITALTHRPWSLSHTGDGKPR
YDTFWKHFIFVMMDILLDWSMHNILWYLCGISAFLMQKDFVSPAYLKKWSAKGIQVVGWT
VNTFDEKSYYESHLGSSYITDSMVEDCEPHF
|
| Enzyme 5 Number of Residues |
331 |
| Enzyme 5 Molecular Weight |
37719 |
| Enzyme 5 Theoretical pI |
6.70 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- glycerophosphodiester phosphodiesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glycerol metabolism
- metabolism
- physiological process
- polyol metabolism
|
| Component |
| — |
|
| Enzyme 5 General Function |
Energy production and conversion |
| Enzyme 5 Specific Function |
Has glycerophosphoinositol phosphodiesterase activity. Has little or no activity towards glycerophosphocholine. GDE1 activity can be modulated by G-protein signaling pathways |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = myo-inositol + sn-glycerol 3-phosphate [RN:R01193] ALL_REAC R01193
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
7637877  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9NZC3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GDE1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AF212862  |
| Enzyme 5 GeneCard ID |
Q9NZC3  |
| Enzyme 5 GenAtlas ID |
GDE1  |
| Enzyme 5 HGNC ID |
HGNC:29644  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Zheng B, Chen D, Farquhar MG: MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3999-4004. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
13051 |
| Enzyme 6 Name |
MHC class I antigen |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
HLA-B |
| Enzyme 6 Protein Sequence |
>MHC class I antigen
SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWD
RNTQIYKAQAQTDRESLRNLRGYYNQSEAGSHTLQRMYGCDVGPDGRLLRGHDQSAYDGK
DYIALNEDLSSWTAADTAAQITQRKWEAAREAEQWRAYLEGLCVEWLRRYLENGKETLQR
A
|
| Enzyme 6 Number of Residues |
181 |
| Enzyme 6 Molecular Weight |
21059 |
| Enzyme 6 Theoretical pI |
5.13 |
| Enzyme 6 GO Classification |
| Function |
- MHC class I receptor activity
- receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- antigen presentation
- defense response
- immune response
- response to biotic stimulus
- response to stimulus
|
| Component |
- MHC class I protein complex
- MHC protein complex
- protein complex
|
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
1526966  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q95372  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q95372_HUMAN  |
| Enzyme 6 PDB ID |
1XR9  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
U67749  |
| Enzyme 6 GeneCard ID |
Q95372  |
| Enzyme 6 GenAtlas ID |
HLA-B  |
| Enzyme 6 HGNC ID |
HGNC:4932  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Hurley CK, Steiner N, Kosman C, Mitton W, Koester R, Bei M, Bush J, McCormack J, Hahn A, Henson V, Hoyer R, Wade JA, Hartzman RJ, Ng J: Novel HLA-A and HLA-B alleles. Tissue Antigens. 1998 Jul;52(1):84-7. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
16479 |
| Enzyme 7 Name |
cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-) |
| Enzyme 7 Synonyms |
- SubName: Lysophospholipase 3 (Lysosomal phospholipase A2), isoform CRA_a
|
| Enzyme 7 Gene Name |
LYPLA3 |
| Enzyme 7 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 7 Number of Residues |
412 |
| Enzyme 7 Molecular Weight |
46658 |
| Enzyme 7 Theoretical pI |
6.72 |
| Enzyme 7 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 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
B3KMF3  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
B3KMF3_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
AK001705  |
| Enzyme 7 GeneCard ID |
B3KMF3  |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
16 |
| Enzyme 7 Locus |
16q22.1 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |