Reviewed,
UniProtKB/Swiss-Prot Q9NZ20 (PA2G3_HUMAN)
Last modified
June 16, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Group 3 secretory phospholipase A2 EC=3.1.1.4 Alternative name(s): Group III secretory phospholipase A2 Short name=GIII sPLA2 Phosphatidylcholine 2-acylhydrolase GIII sPLA2-III | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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 (PC). Preferential cleavage: 1-palmitoyl-2-linoleoyl-phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1-palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE. Ref.4 |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion per subunit. |
| Enzyme regulation | Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan. |
| Subcellular location | |
| Tissue specificity | Expressed in kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in brain, colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation. Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level). Ref.5 |
| Induction | By IL1B and TNF in microvascular endothelial cells (at protein level). Ref.5 |
| Post-translational modification | N-glycosylation does not affect the catalytical activity, but is required for proper secretion. A nonglycosylated form was observed in several cell types. Ref.5 In several cell types, the N- and C-termini are cleaved off. |
| Sequence similarities | Belongs to the phospholipase A2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Cell membrane Membrane Secreted |
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | extracellular space Ref.1 Traceable author statement. Source: ProtInc plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipase A2 activity Ref.1Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 509 | 490 | Group 3 secretory phospholipase A2 | PRO_0000022992 | |||||||
Regions | |||||||||||
| Region | 150 – 291 | 142 | Phospholipase A2-like | ||||||||
Sites | |||||||||||
| Active site | 184 | 1 | |||||||||
| Active site | 214 | 1 | By similarity | ||||||||
| Metal binding | 158 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 160 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 162 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 185 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 326 | 1 | Phosphothreonine Ref.6 | ||||||||
| Modified residue | 327 | 1 | Phosphothreonine Ref.6 | ||||||||
| Modified residue | 335 | 1 | Phosphoserine Ref.6 | ||||||||
| Glycosylation | 167 | 1 | N-linked (GlcNAc...) Ref.5 | ||||||||
| Glycosylation | 280 | 1 | N-linked (GlcNAc...) Ref.5 | ||||||||
| Glycosylation | 325 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 396 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 439 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 159 ↔ 181 | By similarity | |||||||||
| Disulfide bond | 180 ↔ 220 | By similarity | |||||||||
| Disulfide bond | 187 ↔ 213 | By similarity | |||||||||
| Disulfide bond | 211 ↔ 244 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 70 | 1 | A → S: dbSNP rs2232176. | VAR_024555 | |||||||
| Natural variant | 116 | 1 | E → Q: dbSNP rs2074734. | VAR_024556 | |||||||
| Natural variant | 157 | 1 | L → V: dbSNP rs2074735. | VAR_020288 | |||||||
| Natural variant | 307 | 1 | H → Y: dbSNP rs2232180. | VAR_056581 | |||||||
| Natural variant | 322 | 1 | S → R: dbSNP rs2072193. | VAR_024557 | |||||||
| Natural variant | 378 | 1 | R → Q: dbSNP rs2232183. | VAR_034366 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 167 | 1 | N → S: Loss of glycosylation. Ref.5 | ||||||||
| Mutagenesis | 184 | 1 | H → Q: Loss of PGE2 synthesis. Ref.4 Ref.5 | ||||||||
| Mutagenesis | 280 | 1 | N → S: Loss of glycosylation. Ref.5 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Novel human secreted phospholipase A2 with homology to the group III bee venom enzyme." Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G. J. Biol. Chem. 275:7492-7496(2000) [PubMed: 10713052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. |
| [2] | "The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. Wright H.Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [4] | "Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII)." Murakami M., Masuda S., Shimbara S., Bezzine S., Lazdunski M., Lambeau G., Gelb M.H., Matsukura S., Kokubu F., Adachi M., Kudo I. J. Biol. Chem. 278:10657-10667(2003) [PubMed: 12522102] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-184. |
| [5] | "Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2)." Murakami M., Masuda S., Shimbara S., Ishikawa Y., Ishii T., Kudo I. J. Biol. Chem. 280:24987-24998(2005) [PubMed: 15863501] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION AT ASN-167 AND ASN-280, MUTAGENESIS OF ASN-167; HIS-184 AND ASN-280. |
| [6] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326; THR-327 AND SER-335, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF220490 mRNA. Translation: AAF44746.1. AC005005 Genomic DNA. Translation: AAD15617.1. BC025316 mRNA. Translation: AAH25316.1. | |
| IPI | IPI00024578. |
| RefSeq | NP_056530.2. |
| UniGene | Hs.149623 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1POC based on UniProtKB P00630. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q9NZ20. |
Proteomic databases | |
| PRIDE | Q9NZ20. |
Genome annotation databases | |
| Ensembl | ENSG00000100078. Homo sapiens. [Contig view] |
| GeneID | 50487. |
| KEGG | hsa:50487. |
Organism-specific databases | |
| GeneCards | GC22M029855. |
| H-InvDB | HIX0016386. |
| HGNC | HGNC:17934. PLA2G3. |
| HPA | HPA018314. |
| MIM | 611651. gene. |
| PharmGKB | PA38267. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q9NZ20. |
| HOVERGEN | Q9NZ20. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.4. 247. |
Gene expression databases | |
| Bgee | Q9NZ20. |
| CleanEx | HS_PLA2G3. |
| GermOnline | ENSG00000100078. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. IPR008774. Phospholipase_A2_met. [Graphical view] |
| Gene3D | G3DSA:1.20.90.10. Phospholipase_A2. 1 hit. |
| PANTHER | PTHR12253. Phospholipase_A2_met. 1 hit. |
| Pfam | PF05826. Phospholip_A2_2. 1 hit. [Graphical view] |
| SMART | SM00085. PA2c. 1 hit. [Graphical view] |
| PROSITE | PS00119. PA2_ASP. False negative. PS00118. PA2_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 53048. |
| SOURCE | Search... |
Entry information
| Entry name | PA2G3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NZ20 Secondary accession number(s): O95768 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


