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Human Metabolome Database Version 2.5

 

Showing metabocard for Alpha-Linolenic acid (HMDB01388)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-22 09:39:13
Accession Number HMDB01388
Secondary Accession Numbers Not Available
Common Name Alpha-Linolenic acid
Description Alpha-linolenic acid (ALA) is a polyunsaturated fatty acid (PUFA). It is a member of the group of essential fatty acids called omega-3 fatty acids. Alpha-linolenic acid, in particular, is not synthesized by mammals and therefore is an essential dietary requirement for all mammals. Certain nuts (English walnuts) and vegetable oils (canola, soybean, flaxseed/linseed, olive) are particularly rich in alpha-linolenic acid (ALA). Omega-3 fatty acids get their name based on the location of one of their first double bond. In all omega-3 fatty acids, the first double bond is located between the third and fourth carbon atom counting from the methyl end of the fatty acid (n-3). Although humans and other mammals can synthesize saturated and some monounsaturated fatty acids from carbon groups in carbohydrates and proteins, they lack the enzymes necessary to insert a cis double bond at the n-6 or the n-3 position of a fatty acid. Omega-3 fatty acids like a-linolenic acid are important structural components of cell membranes. When incorporated into phospholipids, they affect cell membrane properties such as fluidity, flexibility, permeability and the activity of membrane bound enzymes. Omega-3 fatty acids can modulate the expression of a number of genes, including those involved with fatty acid metabolism and inflammation. Alpha linolenic acid and other omega 3 fatty acids may regulate gene expression by interacting with specific transcription factors, including peroxisome proliferator activated receptors (PPARs) and liver X receptors (LXRs).
Synonyms
  1. (9,12,15)-linolenate
  2. (9,12,15)-linolenic acid
  3. (9Z,12Z,15Z)-Octadecatrienoate
  4. (9Z,12Z,15Z)-Octadecatrienoic acid
  5. (Z,Z,Z)-9,12,15-Octadecatrienoate
  6. (Z,Z,Z)-9,12,15-Octadecatrienoic acid
  7. 9,12,15-Octadecatrienoate
  8. 9,12,15-Octadecatrienoic acid
  9. 9-cis,12-cis,15-cis-octadecatrienoate
  10. 9-cis,12-cis,15-cis-octadecatrienoic acid
  11. Industrene 120
  12. Linolenate
  13. Linolenic acid
  14. a-Linolenate
  15. all-cis-9,12,15-Octadecatrienoate
  16. all-cis-9,12,15-Octadecatrienoic acid
  17. alpha-Linolenate
  18. cis,cis,cis-9,12,15-Octadecatrienoate
  19. cis,cis,cis-9,12,15-Octadecatrienoic acid
  20. cis-9,12,15-octadecatrienoate
  21. cis-9,12,15-octadecatrienoic acid
  22. a-Linolenic acid
  23. alpha-Linolenic acid
Chemical IUPAC Name (9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
Chemical Formula C18H30O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Long chain fatty acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • alkene
Biofunction
  • Essential fatty acid
Application
—
Source
  • Exogenous
Average Molecular Weight 278.430
Monoisotopic Molecular Weight 278.224579
Isomeric SMILES CCC=C/CC=C/CC=C/CCCCCCCC(O)=O
Canonical SMILES CCC=CCC=CCC=CCCCCCCCC(O)=O
KEGG Compound ID C06427 Link Image
BioCyc ID LINOLENIC_ACID Link Image
BiGG ID 48237 Link Image
Wikipedia Link Linolenic acid Link Image
NuGOwiki Link HMDB01388 Link Image
Metagene Link HMDB01388 Link Image
METLIN ID 6208 Link Image
PubChem Compound 860 Link Image
PubChem Substance 11362510 Link Image
ChEBI ID 27432 Link Image
CAS Registry Number 463-40-1
InChI Identifier InChI=1/C18H30O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(19)20/h3-4,6-7,9-10H,2,5,8,11-17H2,1H3,(H,19,20)/b4-3-,7-6-,10-9-
Synthesis Reference Li, Guihua; Qian, Xiangming; Jiang, Yanchao; Ma, Shushi. Preparation of a-linolenic acid from linseed oil. Zhengzhou Gongcheng Xueyuan Xuebao (2004), 25(3), 13-15.
Melting Point (Experimental) -16.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.000124 mg/mL [MEYLAN,WM et al. (1996)]; 2.66e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity 6.46 [SANGSTER (1993)] Source: PhysProp
Predicted LogP/Hydrophobicity 6.62 [Predicted by ALOGPS]; 5.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Epidermis —
Fibroblasts —
Intestine —
Muscle —
Nervous Tissues —
Placenta —
Platelet —
Prostate —
Concentrations (Normal)
Biofluid Blood
Value 1.1 +/- 0.8 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.975 +/- 1.223 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nikolaos Psychogios, David D. Hau, Jun Peng, An Chi Guo, Rupasri Mandal, Souhaila Bouatra, Igor Sinelnikov, Ramanarayan Krishnamurthy, Roman Eisner, Bijaya Gautam, Nelson Young, Jinaguo Xia, Craig Knox, Ying Wei Dong, Paul Huang, Janet McManus, Theresa Pedersen, Fiona Bamforth, Russ Greiner, Bruce McManus, John Newman, David S. Wishart, The Human Serum Metabolome, PLoS ONE (Submitted).
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 17.5 +/- 7.6 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 16.8 +/- 7.3 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 18.5 +/- 7.9 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Urine
Value 0.73 +/- 0.54 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Kim KM, Jung BH, Lho DS, Chung WY, Paeng KJ, Chung BC: Alteration of urinary profiles of endogenous steroids and polyunsaturated fatty acids in thyroid cancer. Cancer Lett. 2003 Dec 30;202(2):173-9. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 21.2 +/- 7.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypertension
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 20.5 +/- 7.5 uM
Age Adult:>18 yrs old
Sex Male
Condition Essential hypertension
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Blood
Value 22.7 +/- 6.2 uM
Age Adult:>18 yrs old
Sex Female
Condition Essential hypertension
Comments Not Available
References
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Biofluid Urine
Value 0.49 +/- 0.46 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Condition Thyroid cancer
Comments Not Available
References
  • Kim KM, Jung BH, Lho DS, Chung WY, Paeng KJ, Chung BC: Alteration of urinary profiles of endogenous steroids and polyunsaturated fatty acids in thyroid cancer. Cancer Lett. 2003 Dec 30;202(2):173-9. [PubMed Link Image]
Associated Disorders
Condition References
Essential hypertension
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Hypertension
  • Wang S, Ma A, Song S, Quan Q, Zhao X, Zheng X: Fasting serum free fatty acid composition, waist/hip ratio and insulin activity in essential hypertensive patients. Hypertens Res. 2008 Apr;31(4):623-32. [PubMed Link Image]
Thyroid cancer
  • Kim KM, Jung BH, Lho DS, Chung WY, Paeng KJ, Chung BC: Alteration of urinary profiles of endogenous steroids and polyunsaturated fatty acids in thyroid cancer. Cancer Lett. 2003 Dec 30;202(2):173-9. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Alpha Linolenic Acid and Linoleic Acid Metabolism SMP00018 Link Image map00592 Link Image
General References
  1. Christensen JH, Fabrin K, Borup K, Barber N, Poulsen J: Prostate tissue and leukocyte levels of n-3 polyunsaturated fatty acids in men with benign prostate hyperplasia or prostate cancer. BJU Int. 2006 Feb;97(2):270-3. [PubMed Link Image]
  2. Attar-Bashi NM, Frauman AG, Sinclair AJ: Alpha-linolenic acid and the risk of prostate cancer. What is the evidence? J Urol. 2004 Apr;171(4):1402-7. [PubMed Link Image]
  3. Rastogi SK, Singh J: Effect of chemical penetration enhancer and iontophoresis on the in vitro percutaneous absorption enhancement of insulin through porcine epidermis. Pharm Dev Technol. 2005;10(1):97-104. [PubMed Link Image]
  4. Allman MA, Pena MM, Pang D: Supplementation with flaxseed oil versus sunflowerseed oil in healthy young men consuming a low fat diet: effects on platelet composition and function. Eur J Clin Nutr. 1995 Mar;49(3):169-78. [PubMed Link Image]
  5. Fokkema MR, Brouwer DA, Hasperhoven MB, Martini IA, Muskiet FA: Short-term supplementation of low-dose gamma-linolenic acid (GLA), alpha-linolenic acid (ALA), or GLA plus ALA does not augment LCP omega 3 status of Dutch vegans to an appreciable extent. Prostaglandins Leukot Essent Fatty Acids. 2000 Nov;63(5):287-92. [PubMed Link Image]
  6. Becker CC, Lund P, Holmer G, Jensen H, Sandstrom B: Effects of butter oil blends with increased concentrations of stearic, oleic and linolenic acid on blood lipids in young adults. Eur J Clin Nutr. 1999 Jul;53(7):535-41. [PubMed Link Image]
  7. Jones DB, Scaretto L, Carter R, Mann JI: Glucose, insulin and platelet fatty acids following myocardial infarction: an association with infarct size. Diabete Metab. 1987 Jul-Aug;13(4):463-6. [PubMed Link Image]
  8. Crastes de Paulet A, Babin F, Billeaud C, Bougle D, Sarda P, Mendy F: [Biological effects on premature neonates of a milk formula enriched with alpha-linolenic acid: a multicenter study] Bull Acad Natl Med. 1994 Feb;178(2):267-73; discussion 273-8. [PubMed Link Image]
  9. Richieri GV, Ogata RT, Kleinfeld AM: Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB. J Biol Chem. 1994 Sep 30;269(39):23918-30. [PubMed Link Image]
  10. Li D, Sinclair A, Wilson A, Nakkote S, Kelly F, Abedin L, Mann N, Turner A: Effect of dietary alpha-linolenic acid on thrombotic risk factors in vegetarian men. Am J Clin Nutr. 1999 May;69(5):872-82. [PubMed Link Image]
  11. Bhatia KS, Singh J: Effect of linolenic acid/ethanol or limonene/ethanol and iontophoresis on the in vitro percutaneous absorption of LHRH and ultrastructure of human epidermis. Int J Pharm. 1999 Apr 15;180(2):235-50. [PubMed Link Image]
  12. Baylin A, Kabagambe EK, Ascherio A, Spiegelman D, Campos H: Adipose tissue alpha-linolenic acid and nonfatal acute myocardial infarction in Costa Rica. Circulation. 2003 Apr 1;107(12):1586-91. Epub 2003 Mar 10. [PubMed Link Image]
  13. Williard DE, Nwankwo JO, Kaduce TL, Harmon SD, Irons M, Moser HW, Raymond GV, Spector AA: Identification of a fatty acid delta6-desaturase deficiency in human skin fibroblasts. J Lipid Res. 2001 Apr;42(4):501-8. [PubMed Link Image]
  14. Campbell FM, Gordon MJ, Dutta-Roy AK: Preferential uptake of long chain polyunsaturated fatty acids by isolated human placental membranes. Mol Cell Biochem. 1996 Feb 9;155(1):77-83. [PubMed Link Image]
  15. Cunnane SC, Hamadeh MJ, Liede AC, Thompson LU, Wolever TM, Jenkins DJ: Nutritional attributes of traditional flaxseed in healthy young adults. Am J Clin Nutr. 1995 Jan;61(1):62-8. [PubMed Link Image]
  16. Bajaj M, Suraamornkul S, Romanelli A, Cline GW, Mandarino LJ, Shulman GI, DeFronzo RA: Effect of a sustained reduction in plasma free fatty acid concentration on intramuscular long-chain fatty Acyl-CoAs and insulin action in type 2 diabetic patients. Diabetes. 2005 Nov;54(11):3148-53. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. Calcium-dependent phospholipase A2 precursor
  2. Group IIF secretory phospholipase A2 precursor
  3. Cytosolic phospholipase A2
  4. Phospholipase A2 precursor
  5. Group XIIB secretory phospholipase A2-like protein precursor
  6. Group 10 secretory phospholipase A2 precursor
  7. Group IIE secretory phospholipase A2 precursor
  8. Group IID secretory phospholipase A2 precursor
  9. Group 3 secretory phospholipase A2 precursor
  10. Bile acid CoA:amino acid N-acyltransferase
  11. Cytosolic acyl coenzyme A thioester hydrolase
  12. Acyl-coenzyme A thioesterase 2
  13. Acyl-coenzyme A thioesterase 8
  14. CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
  15. Delta-6 fatty acid desaturase
  16. Cytosolic phospholipase A2 beta
  17. Acyl-CoA thioesterase 4
  18. 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)
  19. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5287
Enzyme 1 Name Calcium-dependent phospholipase A2 precursor
Enzyme 1 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. PLA2-10
  3. Group V phospholipase A2
Enzyme 1 Gene Name PLA2G5
Enzyme 1 Protein Sequence >Calcium-dependent phospholipase A2 precursor 
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 1 Number of Residues 138
Enzyme 1 Molecular Weight 15674
Enzyme 1 Theoretical pI 8.48
Enzyme 1 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 1 General Function Not Available
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-20
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 460915 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >417 bp 
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 1 GenBank Gene ID U03090 Link Image
Enzyme 1 GeneCard ID PLA2G5 Link Image
Enzyme 1 GenAtlas ID PLA2G5 Link Image
Enzyme 1 HGNC ID HGNC:9038 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p36-p34
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5288
Enzyme 2 Name Group IIF secretory phospholipase A2 precursor
Enzyme 2 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIF
  2. GIIF sPLA2
  3. sPLA(2-IIF
Enzyme 2 Gene Name PLA2G2F
Enzyme 2 Protein Sequence >Group IIF secretory phospholipase A2 precursor 
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 2 Number of Residues 168
Enzyme 2 Molecular Weight 18658
Enzyme 2 Theoretical pI 4.94
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. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Enzyme 2 Pathways
Enzyme 2 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12276060 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >507 bp 
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 2 GenBank Gene ID AF306566 Link Image
Enzyme 2 GeneCard ID PLA2G2F Link Image
Enzyme 2 GenAtlas ID PLA2G2F Link Image
Enzyme 2 HGNC ID HGNC:30040 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p35
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5289
Enzyme 3 Name Cytosolic phospholipase A2
Enzyme 3 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA[Includes: Phospholipase A2
  3. Phosphatidylcholine 2- acylhydrolase
  4. Lysophospholipase
Enzyme 3 Gene Name PLA2G4A
Enzyme 3 Protein Sequence >Cytosolic phospholipase A2 
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 3 Number of Residues 749
Enzyme 3 Molecular Weight 85212
Enzyme 3 Theoretical pI 5.03
Enzyme 3 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 3 General Function Not Available
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 190007 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 3 PDB ID 1CJY Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID M72393 Link Image
Enzyme 3 GeneCard ID PLA2G4A Link Image
Enzyme 3 GenAtlas ID PLA2G4A Link Image
Enzyme 3 HGNC ID HGNC:9035 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q25
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed Link Image]
  2. Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed Link Image]
  3. Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed Link Image]
  4. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  5. Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed Link Image]
  6. Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5290
Enzyme 4 Name Phospholipase A2 precursor
Enzyme 4 Synonyms
  1. Phosphatidylcholine 2- acylhydrolase
  2. Group IB phospholipase A2
Enzyme 4 Gene Name PLA2G1B
Enzyme 4 Protein Sequence >Phospholipase A2 precursor 
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 4 Number of Residues 148
Enzyme 4 Molecular Weight 16360
Enzyme 4 Theoretical pI 7.91
Enzyme 4 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 4 General Function Not Available
Enzyme 4 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 4 Pathways
Enzyme 4 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 387025 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >447 bp 
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 4 GenBank Gene ID M21056 Link Image
Enzyme 4 GeneCard ID PLA2G1B Link Image
Enzyme 4 GenAtlas ID PLA2G1B Link Image
Enzyme 4 HGNC ID HGNC:9030 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12q23-q24.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed Link Image]
  2. Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed Link Image]
  3. Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5291
Enzyme 5 Name Group XIIB secretory phospholipase A2-like protein precursor
Enzyme 5 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. GXIIB
Enzyme 5 Gene Name PLA2G12B
Enzyme 5 Protein Sequence >Group XIIB secretory phospholipase A2-like protein precursor 
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 5 Number of Residues 195
Enzyme 5 Molecular Weight 21659
Enzyme 5 Theoretical pI 5.81
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
  • extracellular region
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not known; does not seem to have catalytic activity
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-19
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 13560707 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9BX93 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PG12B_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >585 bp 
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCCTGTGATTCCCTG
GTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGTCAG
CGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 5 GenBank Gene ID AF349540 Link Image
Enzyme 5 GeneCard ID PLA2G12B Link Image
Enzyme 5 GenAtlas ID PLA2G12B Link Image
Enzyme 5 HGNC ID HGNC:18555 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q22.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5292
Enzyme 6 Name Group 10 secretory phospholipase A2 precursor
Enzyme 6 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 6 Gene Name PLA2G10
Enzyme 6 Protein Sequence >Group 10 secretory phospholipase A2 precursor 
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 6 Number of Residues 155
Enzyme 6 Molecular Weight 17132
Enzyme 6 Theoretical pI 6.46
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 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 6 Pathways
Enzyme 6 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-21
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2289237 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >498 bp 
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 6 GenBank Gene ID U95301 Link Image
Enzyme 6 GeneCard ID PLA2G10 Link Image
Enzyme 6 GenAtlas ID PLA2G10 Link Image
Enzyme 6 HGNC ID HGNC:9029 Link Image
Enzyme 6 Chromosome Location 16
Enzyme 6 Locus 16p13.1-p12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5294
Enzyme 7 Name Group IIE secretory phospholipase A2 precursor
Enzyme 7 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIE
  2. GIIE sPLA2
  3. sPLA(2-IIE
Enzyme 7 Gene Name PLA2G2E
Enzyme 7 Protein Sequence >Group IIE secretory phospholipase A2 precursor 
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 7 Number of Residues 142
Enzyme 7 Molecular Weight 15989
Enzyme 7 Theoretical pI 8.28
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 preference for arachidonic-containing phospholipids
Enzyme 7 Pathways
Enzyme 7 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-19
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 7108923 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >429 bp 
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 7 GenBank Gene ID AF189279 Link Image
Enzyme 7 GeneCard ID PLA2G2E Link Image
Enzyme 7 GenAtlas ID PLA2G2E Link Image
Enzyme 7 HGNC ID HGNC:13414 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p36.13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5302
Enzyme 8 Name Group IID secretory phospholipase A2 precursor
Enzyme 8 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIID
  2. GIID sPLA2
  3. PLA2IID
  4. sPLA(2-IID
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 8 Gene Name PLA2G2D
Enzyme 8 Protein Sequence >Group IID secretory phospholipase A2 precursor 
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 8 Number of Residues 145
Enzyme 8 Molecular Weight 16546
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. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined
Enzyme 8 Pathways
Enzyme 8 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-20
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 5771420 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >438 bp 
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 8 GenBank Gene ID AF112982 Link Image
Enzyme 8 GeneCard ID PLA2G2D Link Image
Enzyme 8 GenAtlas ID PLA2G2D Link Image
Enzyme 8 HGNC ID HGNC:9033 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p36.12
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed Link Image]
  2. Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5783
Enzyme 9 Name Group 3 secretory phospholipase A2 precursor
Enzyme 9 Synonyms
  1. Group III secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GIII
  3. GIII sPLA2
Enzyme 9 Gene Name PLA2G3
Enzyme 9 Protein Sequence >Group 3 secretory phospholipase A2 precursor 
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
Enzyme 9 Number of Residues 509
Enzyme 9 Molecular Weight 57152
Enzyme 9 Theoretical pI 9.23
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid catabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 9 General Function Not Available
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 7274380 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9NZ20 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PA2G3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID AF220490 Link Image
Enzyme 9 GeneCard ID PLA2G3 Link Image
Enzyme 9 GenAtlas ID PLA2G3 Link Image
Enzyme 9 HGNC ID HGNC:17934 Link Image
Enzyme 9 Chromosome Location 22
Enzyme 9 Locus 22q11.2-q13.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5821
Enzyme 10 Name Bile acid CoA:amino acid N-acyltransferase
Enzyme 10 Synonyms
  1. BAT
  2. BACAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 10 Gene Name BAAT
Enzyme 10 Protein Sequence >Bile acid CoA:amino acid N-acyltransferase 
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 10 Number of Residues 418
Enzyme 10 Molecular Weight 46300
Enzyme 10 Theoretical pI 7.00
Enzyme 10 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
Enzyme 10 Pathways
Enzyme 10 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 532505 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1257 bp 
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
Enzyme 10 GenBank Gene ID L34081 Link Image
Enzyme 10 GeneCard ID BAAT Link Image
Enzyme 10 GenAtlas ID BAAT Link Image
Enzyme 10 HGNC ID HGNC:932 Link Image
Enzyme 10 Chromosome Location 9
Enzyme 10 Locus 9q22.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed Link Image]
  2. Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6335
Enzyme 11 Name Cytosolic acyl coenzyme A thioester hydrolase
Enzyme 11 Synonyms
  1. Long chain acyl-CoA thioester hydrolase
  2. CTE-II
  3. CTE-IIa
  4. Brain acyl-CoA hydrolase
  5. Acyl-CoA thioesterase 7
Enzyme 11 Gene Name ACOT7
Enzyme 11 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase 
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
Enzyme 11 Number of Residues 380
Enzyme 11 Molecular Weight 41797
Enzyme 11 Theoretical pI 8.66
Enzyme 11 GO Classification
Function
  • catalytic activity
Process
—
Component
—
Enzyme 11 General Function Lipid transport and metabolism
Enzyme 11 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-19
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 2780414 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O00154 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name BACH_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1017 bp 
ATGTCGGGCCCAGACGTCGAGACGCCGTCCGCCATCCAGATCTGCCGGATCATGCGGCCA
GATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATCGAGGAG
GCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGTGTGGCC
GCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAGGTGGCG
CATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTCAACGTG
ATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTGTGGTAT
GTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTGTATTCC
CGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAGCGCATG
GAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCGAACACT
GTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACCCTGCAC
GGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATCGTGGCT
GCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTTCATGAC
AAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGCAATAAG
TCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAGAAGCGC
TACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGGTCGCTG
CCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAAGGCAAA
GGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCCTAG
Enzyme 11 GenBank Gene ID D88894 Link Image
Enzyme 11 GeneCard ID ACOT7 Link Image
Enzyme 11 GenAtlas ID ACOT7 Link Image
Enzyme 11 HGNC ID HGNC:24157 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p36.31-p36.11
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6336
Enzyme 12 Name Acyl-coenzyme A thioesterase 2
Enzyme 12 Synonyms
  1. Acyl-CoA thioesterase 2
  2. Peroxisomal acyl-coenzyme A thioester hydrolase 2a
  3. Peroxisomal long-chain acyl-coA thioesterase 2
  4. ZAP128
  5. CTE-Ia
Enzyme 12 Gene Name ACOT2
Enzyme 12 Protein Sequence >Acyl-coenzyme A thioesterase 2 
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGREGTIP
SKV
Enzyme 12 Number of Residues 483
Enzyme 12 Molecular Weight 53257
Enzyme 12 Theoretical pI 8.93
Enzyme 12 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 887376 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P49753 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >937 bp 
CCCCCGGGCTGCAGGAATTCCTGAATTCAAAATGGCCTCATCTCCTGCTGTCCTTCGAGC
GTCCCGGCTGTACCAATGGAGCCTGAAGAGTTCGGCGCAGTTCCTGGGGTCTCCACAGCT
GAGGCAGAACCTGGGCCCTTTCCTGGGATTGTGGACATGTTCGGGAACTGGAGGTGGCCT
GCTGGAGTATCGGGCTAGTCTGCTGGCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTA
TTATAACTATGAAGACCTCCCCAAGACCATGGAGACGCTCCATCTGGAGTACTTTGAAGA
AGCCATGAACTACTTGCTCAGTCATCCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGG
AATTTCCAAAGGGGGTGAGCTCTGCCTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGC
TGCTGTCGTCATCAACGGCTCTGTGGCCAATGTTGGGGGAACCTTACACTACAAGGGCGA
GACCCTGCCCCCTGTGGGCGTCAACAGAAATCGCATCAAGGTGACCAAAGATGGCTATGC
AGACATTGTGGATGTCCTGAACAGCCCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCC
TGTGGAAAGGGCAGAGAGCACCTTCCTGTTCCTGGTAGGTCAGGATGACCACAACTGGAA
GAGTGAGTTCTATGCTAATGAGGCCTGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCC
CCAGATCATCTGTTACCCAGAGACAGGGCACTATATTGAGCCTCCTTACTTCCCCCTGTG
TCGGGCTTCCCTGCATGCCTTGGTGGGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGC
TCATGCCATGGCTCAGGTGGATGCTTGGAAACAACTCCAGACTTTCTTCCACAAACACTT
GGGTGGCCACGAGGGGACAATCCCATCAAAAGTGTAA
Enzyme 12 GenBank Gene ID L40401 Link Image
Enzyme 12 GeneCard ID ACOT2 Link Image
Enzyme 12 GenAtlas ID ACOT2 Link Image
Enzyme 12 HGNC ID HGNC:18431 Link Image
Enzyme 12 Chromosome Location 14
Enzyme 12 Locus 14q24.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed Link Image]
  2. Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6338
Enzyme 13 Name Acyl-coenzyme A thioesterase 8
Enzyme 13 Synonyms
  1. Choloyl-coenzyme A thioesterase
  2. Acyl-CoA thioesterase 8
  3. Peroxisomal acyl-coenzyme A thioester hydrolase 1
  4. PTE-1
  5. Peroxisomal long-chain acyl-coA thioesterase 1
  6. HIV-Nef-associated acyl coA thioesterase
  7. Thioesterase II
  8. hTE
  9. hACTEIII
  10. hACTE-III
  11. PTE-2
Enzyme 13 Gene Name ACOT8
Enzyme 13 Protein Sequence >Acyl-coenzyme A thioesterase 8 
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
Enzyme 13 Number of Residues 319
Enzyme 13 Molecular Weight 35915
Enzyme 13 Theoretical pI 7.60
Enzyme 13 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolism
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 2318125 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O14734 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ACOT8_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >960 bp 
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
Enzyme 13 GenBank Gene ID AF014404 Link Image
Enzyme 13 GeneCard ID ACOT8 Link Image
Enzyme 13 GenAtlas ID ACOT8 Link Image
Enzyme 13 HGNC ID HGNC:15919 Link Image
Enzyme 13 Chromosome Location 20
Enzyme 13 Locus 20q13.12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed Link Image]
  2. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed Link Image]
  3. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8755
Enzyme 14 Name CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 Protein Sequence >CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2 
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 14 Number of Residues 189
Enzyme 14 Molecular Weight 21067
Enzyme 14 Theoretical pI 7.27
Enzyme 14 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways
Enzyme 14 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-22
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 22761446 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q542Y6 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q542Y6_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >570 bp 
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
Enzyme 14 GenBank Gene ID AK075389 Link Image
Enzyme 14 GeneCard ID Not Available
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID HGNC:18554 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs Not Available
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8800
Enzyme 15 Name Delta-6 fatty acid desaturase
Enzyme 15 Synonyms
  1. CDNA FLJ90458 fis, clone NT2RP3001738, highly similar to Fatty acid desaturase 2
  2. Fatty acid desaturase 2
Enzyme 15 Gene Name FADS2
Enzyme 15 Protein Sequence >Delta-6 fatty acid desaturase 
MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVI
GHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTA
EDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQH
DYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFV
LGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAV
SYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQL
TATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLL
RALLDIIRSLKKSGKLWLDAYLHK
Enzyme 15 Number of Residues 444
Enzyme 15 Molecular Weight 52260
Enzyme 15 Theoretical pI 9.18
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid desaturation
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 15 General Function Lipid transport and metabolism
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals Not Available
Enzyme 15 Transmembrane Regions
  • 132-154
  • 158-180
  • 266-288
  • 303-325
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 4406528 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O95864 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name O95864_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1335 bp 
ATGGGGAAGGGAGGGAACCAGGGCGAGGGGGCCGCCGAGCGCGAGGTGTCGGTGCCCACC
TTCAGCTGGGAGGAGATTCAGAAGCATAACCTGCGCACCGACAGGTGGCTGGTCATTGAC
CGCAAGGTTTACAACATCACCAAATGGTCCATCCAGCACCCGGGGGGCCAGCGGGTCATC
GGGCACTACGCTGGAGAAGATGCAACGGATGCCTTCCGCGCCTTCCACCCTGACCTGGAA
TTCGTGGGCAAGTTCTTGAAACCCCTGCTGATTGGTGAACTGGCCCCGGAGGAGCCCAGC
CAGGACCACGGCAAGAACTCAAAGATCACTGAGGACTTCCGGGCCCTGAGGAAGACGGCT
GAGGACATGAACCTGTTCAAGACCAACCACGTGTTCTTCCTCCTCCTCCTGGCCCACATC
ATCGCCCTGGAGAGCATTGCATGGTTCACTGTCTTTTACTTTGGCAATGGCTGGATTCCT
ACCCTCATCACGGCCTTTGTCCTTGCTACCTCTCAGGCCCAAGCTGGATGGCTGCAACAT
GATTATGGCCACCTGTCTGTCTACAGAAAACCCAAGTGGAACCACCTTGTCCACAAATTC
GTCATTGGCCACTTAAAGGGTGCCTCTGCCAACTGGTGGAATCATCGCCACTTCCAGCAC
CACGCCAAGCCTAACATCTTCCACAAGGATCCCGATGTGAACATGCTGCACGTGTTTGTT
CTGGGCGAATGGCAGCCCATCGAGTACGGCAAGAAGAAGCTGAAATACCTGCCCTACAAT
CACCAGCACGAATACTTCTTCCTGATTGGGCCGCCGCTGCTCATCCCCATGTATTTCCAG
TACCAGATTATCATGACCATGATCGTCCATAAGAACTGGGTGGACCTGGCCTGGGCCGTC
AGCTACTACATCCGGTTCTTCATCACCTACATCCCTTTCTACGGCATCCTGGGAGCCCTC
CTTTTCCTCAACTTCATCAGGTTCCTGGAGAGCCACTGGTTTGTGTGGGTCACACAGATG
AATCACATCGTCATGGAGATTGACCAGGAGGCCTACCGTGACTGGTTCAGTAGCCAGCTG
ACAGCCACCTGCAACGTGGAGCAGTCCTTCTTCAACGACTGGTTCAGTGGACACCTTAAC
TTCCAGATTGAGCACCACCTCTTCCCCACCATGCCCCGGCACAACTTACACAAGATCGCC
CCGCTGGTGAAGTCTCTATGTGCCAAGCATGGCATTGAATACCAGGAGAAGCCGCTACTG
AGGGCCCTGCTGGACATCATCAGGTCCCTGAAGAAGTCTGGGAAGCTGTGGCTGGACGCC
TACCTTCACAAATGA
Enzyme 15 GenBank Gene ID AF126799 Link Image
Enzyme 15 GeneCard ID FADS2 Link Image
Enzyme 15 GenAtlas ID FADS2 Link Image
Enzyme 15 HGNC ID HGNC:3575 Link Image
Enzyme 15 Chromosome Location 11
Enzyme 15 Locus 11q12-q13.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Cho HP, Nakamura MT, Clarke SD: Cloning, expression, and nutritional regulation of the mammalian Delta-6 desaturase. J Biol Chem. 1999 Jan 1;274(1):471-7. [PubMed Link Image]
  2. Marquardt A, Stohr H, White K, Weber BH: cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family. Genomics. 2000 Jun 1;66(2):175-83. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 14866
Enzyme 16 Name Cytosolic phospholipase A2 beta
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name PLA2G4B
Enzyme 16 Protein Sequence >MEKAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVWNQSFHFRIHR 
QLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEGRLEVEFRLQS
LADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGPQEASVGTGTF
RFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMRVELKKEAGLR
ELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIMATGGGIRAMT
SLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTELLKTQVTKNK
LGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLSDQREALSHGQ
NPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEFFMGQLMKRLP
ESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPLLKIEEPPSTA
GRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGLPNQLTPSEPH
LCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQEQGIPFPPISP
SPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEAAAGEVNLSSS
DSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRPH
Enzyme 16 Number of Residues 781
Enzyme 16 Molecular Weight 88066
Enzyme 16 Theoretical pI 5.85
Enzyme 16 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 16 General Function Not Available
Enzyme 16 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 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 3811347 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P0C869 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PA24B_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 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 16 GenBank Gene ID AF065215 Link Image
Enzyme 16 GeneCard ID P0C869 Link Image
Enzyme 16 GenAtlas ID PLA2G4B Link Image
Enzyme 16 HGNC ID HGNC:9036 Link Image
Enzyme 16 Chromosome Location 15
Enzyme 16 Locus 15q11.2-q21.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed Link Image]
  2. Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15234
Enzyme 17 Name Acyl-CoA thioesterase 4
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name ACOT4
Enzyme 17 Protein Sequence >Acyl-CoA thioesterase 4 
MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADACGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L
Enzyme 17 Number of Residues 421
Enzyme 17 Molecular Weight 46274
Enzyme 17 Theoretical pI 7.95
Enzyme 17 GO Classification
Function
  • CoA hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 60551129 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q5BKT6 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q5BKT6_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1266 bp 
ATGTCAGCAACGCTGATCCTGGAGCCCCCAGGCCGCTGCTGCTGGAACGAGCCGGTGCGC
ATTGCCGTGCGCGGCCTGGCCCCGGAGCAGCGGGTTACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTCTTCCGGGCCCACGCGCGCTACTGCGCCGACGCCTGCGGCGAGCTG
GACCTGGAGCGCGCACCCGCGCTGGGCGGCAGCTTCGCGGGACTCGAGCCCATGGGGCTG
CTCTGGGCCCTGGAACCCGAGAAGCCTTTTTGGCGCTTCCTGAAGCGGGACGTACAGATT
CCTTTTGTCGTGGAGTTGGAGGTGCTGGACGGCCACGACCCCGAGCCTGGACGGCTGCTG
TGCCAGGCGCAGCACGAGCGCCACTTCCTCCCGCCAGGGGTGCGGCGCCAGTCGGTGCGA
GCGGGCCGGGTGCGCGCCACGCTCTTCCTGCCGCCAGGACCTGGACCCTTCCCAGGGATC
ATTGACATCTTTGGTATTGGAGGGGGCCTCTTGGAATATCGAGCCAGCCTCCTTGCTGGC
CATGGCTTTGCCACGTTGGCTCTAGCTTATTATAACTTTGAAGATCTCCCCAATAACATG
GACAACATATCCCTGGAGTACTTCGAAGAAGCCGTATGCTACATGCTTCAACATCCCCAG
GTAAAAGGCCCAGGCATTGGGCTTTTGGGCATTTCTCTAGGAGCTGATATTTGTCTCTCA
ATGGCCTCATTCTTGAAGAATGTCTCAGCCACAGTTTCCATCAATGGATCTGGGATCAGT
GGGAACACAGCCATCAACTATAAGCACAGTAGCATTCCACCATTGGGCTATGACCTGAGG
AGAATCAAGGTAGCTTTCTCAGGCCTCGTGGACATCGTGGATATAAGGAATGCTCTCGTA
GGAGGGTACAAGAACCCCAGCATGATTCCAATAGAGAAGGCCCAGGGGCCCATCCTGCTC
ATTGTTGGTCAGGATGACCATAACTGGAGAAGTGAGTTGTATGCCCAAACAGTCTCTGAA
CGGTTACAGGCCCATGGAAAGGAAAAACCCCAGATCATCTGTTACCCTGGGACTGGGCAT
TACATCGAGCCTCCTTACTTCCCCCTGTGCCCAGCTTCCCTTCACAGATTACTGAACAAA
CATGTTATATGGGGTGGGGAGCCCAGGGCTCATTCTAAGGCCCAGGAAGATGCCTGGAAG
CAAATTCTAGCCTTCTTCTGCAAACACCTGGGAGGTACCCAGAAAACAGCTGTCCCTAAA
TTGTAA
Enzyme 17 GenBank Gene ID BC090945 Link Image
Enzyme 17 GeneCard ID Q5BKT6 Link Image
Enzyme 17 GenAtlas ID ACOT4 Link Image
Enzyme 17 HGNC ID HGNC:19748 Link Image
Enzyme 17 Chromosome Location 14
Enzyme 17 Locus 14q24.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15299
Enzyme 18 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 18 Synonyms Not Available
Enzyme 18 Gene Name PLA2G2A
Enzyme 18 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 18 Number of Residues 144
Enzyme 18 Molecular Weight 16083
Enzyme 18 Theoretical pI 9.51
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158256040 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K5I7 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K5I7_HUMAN Link Image
Enzyme 18 PDB ID 1DB4 Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >435 bp 
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 18 GenBank Gene ID AK291302 Link Image
Enzyme 18 GeneCard ID A8K5I7 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16561
Enzyme 19 Name Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name PLA2G6
Enzyme 19 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 19 Number of Residues 752
Enzyme 19 Molecular Weight 84094
Enzyme 19 Theoretical pI 7.24
Enzyme 19 GO Classification
Function
—
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
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Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID B0QYE8 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B0QYE8_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AL022322 Link Image
Enzyme 19 GeneCard ID B0QYE8 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 22
Enzyme 19 Locus 22q13.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available