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Q9NZ20 (PA2G3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Group 3 secretory phospholipase A2

EC=3.1.1.4
Alternative name(s):
Group III secretory phospholipase A2
Short name=GIII sPLA2
Short name=sPLA2-III
Phosphatidylcholine 2-acylhydrolase 3
Gene names
Name:PLA2G3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Plays a role in ciliogenesis. Ref.4 Ref.7

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

Secreted. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole Ref.4 Ref.7.

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/interleukin-1 beta and TNF in microvascular endothelial cells (at protein level). Ref.5

Post-translational modification

N-glycosylation does not affect the catalytic 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.

Sequence caution

The sequence AAD15617.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Lipid degradation
Lipid metabolism
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium morphogenesis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylcholine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylethanolamine acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcentriole

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 509490Group 3 secretory phospholipase A2
PRO_0000022992

Regions

Region150 – 291142Phospholipase A2-like

Sites

Active site1841
Active site2141 By similarity
Metal binding1581Calcium; via carbonyl oxygen By similarity
Metal binding1601Calcium; via carbonyl oxygen By similarity
Metal binding1621Calcium; via carbonyl oxygen By similarity
Metal binding1851Calcium By similarity

Amino acid modifications

Glycosylation1671N-linked (GlcNAc...) Ref.5
Glycosylation2801N-linked (GlcNAc...) Ref.5
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Disulfide bond159 ↔ 181 By similarity
Disulfide bond180 ↔ 220 By similarity
Disulfide bond187 ↔ 213 By similarity
Disulfide bond211 ↔ 244 By similarity

Natural variations

Natural variant701S → A. Ref.1 Ref.3
Corresponds to variant rs2232176 [ dbSNP | Ensembl ].
VAR_024555
Natural variant1161E → Q.
Corresponds to variant rs2074734 [ dbSNP | Ensembl ].
VAR_024556
Natural variant1571L → V.
Corresponds to variant rs2074735 [ dbSNP | Ensembl ].
VAR_020288
Natural variant3071H → Y.
Corresponds to variant rs2232180 [ dbSNP | Ensembl ].
VAR_056581
Natural variant3221S → R.
Corresponds to variant rs2072193 [ dbSNP | Ensembl ].
VAR_024557
Natural variant3781R → Q.
Corresponds to variant rs2232183 [ dbSNP | Ensembl ].
VAR_034366

Experimental info

Mutagenesis1671N → S: Loss of glycosylation. Ref.5
Mutagenesis1841H → Q: Loss of PGE2 synthesis. Ref.4 Ref.5
Mutagenesis2801N → S: Loss of glycosylation. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9NZ20 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: ED03BED129B0BC9F

FASTA50957,167
        10         20         30         40         50         60 
MGVQAGLFGM LGFLGVALGG SPALRWYRTS CHLTKAVPGN PLGYLSFLAK DAQGLALIHA 

        70         80         90        100        110        120 
RWDAHRRLQS CSWEDEPELT AAYGALCAHE TAWGSFIHTP GPELQRALAT LQSQWEACRA 

       130        140        150        160        170        180 
LEESPAGARK KRAAGQSGVP GGGHQREKRG WTMPGTLWCG VGDSAGNSSE LGVFQGPDLC 

       190        200        210        220        230        240 
CREHDRCPQN ISPLQYNYGI RNYRFHTISH CDCDTRFQQC LQNQHDSISD IVGVAFFNVL 

       250        260        270        280        290        300 
EIPCFVLEEQ EACVAWYWWG GCRMYGTVPL ARLQPRTFYN ASWSSRATSP TPSSRSPAPP 

       310        320        330        340        350        360 
KPRQKQHLRK GPPHQKGSKR PSKANTTALQ DPMVSPRLDV APTGLQGPQG GLKPQGARWV 

       370        380        390        400        410        420 
CRSFRRHLDQ CEHQIGPREI EFQLLNSAQE PLFHCNCTRR LARFLRLHSP PEVTNMLWEL 

       430        440        450        460        470        480 
LGTTCFKLAP PLDCVEGKNC SRDPRAIRVS ARHLRRLQQR RHQLQDKGTD ERQPWPSEPL 

       490        500 
RGPMSFYNQC LQLTQAARRP DRQQKSWSQ 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT ALA-70.
[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. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-70.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Functional genomic screen for modulators of ciliogenesis and cilium length."
Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF220490 mRNA. Translation: AAF44746.1.
AC005005 Genomic DNA. Translation: AAD15617.1. Sequence problems.
BC025316 mRNA. Translation: AAH25316.1.
RefSeqNP_056530.2. NM_015715.3.
UniGeneHs.149623.

3D structure databases

ProteinModelPortalQ9NZ20.
SMRQ9NZ20. Positions 154-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119074. 2 interactions.
IntActQ9NZ20. 2 interactions.
STRING9606.ENSP00000215885.

Chemistry

ChEMBLCHEMBL4667.

PTM databases

PhosphoSiteQ9NZ20.

Polymorphism databases

DMDM317373314.

Proteomic databases

PaxDbQ9NZ20.
PRIDEQ9NZ20.

Protocols and materials databases

DNASU50487.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215885; ENSP00000215885; ENSG00000100078.
GeneID50487.
KEGGhsa:50487.
UCSCuc003aka.3. human.

Organism-specific databases

CTD50487.
GeneCardsGC22M031530.
H-InvDBHIX0016386.
HGNCHGNC:17934. PLA2G3.
HPAHPA021016.
MIM611651. gene.
neXtProtNX_Q9NZ20.
PharmGKBPA38267.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86301.
HOGENOMHOG000147808.
HOVERGENHBG053481.
InParanoidQ9NZ20.
KOK01047.
OMAHTPGPEL.
OrthoDBEOG7DFXBZ.
PhylomeDBQ9NZ20.
TreeFamTF324679.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ9NZ20.
CleanExHS_PLA2G3.
GenevestigatorQ9NZ20.

Family and domain databases

Gene3D1.20.90.10. 2 hits.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PfamPF05826. Phospholip_A2_2. 2 hits.
[Graphical view]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 2 hits.
PROSITEPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi50487.
NextBio53048.
PROQ9NZ20.
SOURCESearch...

Entry information

Entry namePA2G3_HUMAN
AccessionPrimary (citable) accession number: Q9NZ20
Secondary accession number(s): O95768
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM