Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Group 3 secretory phospholipase A2

Gene

PLA2G3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Enzyme regulationi

Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi158Calcium; via carbonyl oxygenBy similarity1
Metal bindingi160Calcium; via carbonyl oxygenBy similarity1
Metal bindingi162Calcium; via carbonyl oxygenBy similarity1
Active sitei1841
Metal bindingi185CalciumBy similarity1
Active sitei214PROSITE-ProRule annotation1

GO - Molecular functioni

  • calcium-dependent phospholipase A2 activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • phospholipase A2 activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cilium biogenesis/degradation, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS01970-MONOMER.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482925. Acyl chain remodelling of PG.

Chemistry databases

SwissLipidsiSLP:000001086.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PLA2G3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17934. PLA2G3.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • mast cell granule Source: GOC
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi167N → S: Loss of glycosylation. 1 Publication1
Mutagenesisi184H → Q: Loss of PGE2 synthesis. 2 Publications1
Mutagenesisi280N → S: Loss of glycosylation. 1 Publication1

Organism-specific databases

DisGeNETi50487.
OpenTargetsiENSG00000100078.
PharmGKBiPA38267.

Chemistry databases

ChEMBLiCHEMBL4667.

Polymorphism and mutation databases

BioMutaiPLA2G3.
DMDMi317373314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000002299220 – 509Group 3 secretory phospholipase A2Add BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi159 ↔ 181By similarity
Glycosylationi167N-linked (GlcNAc...)1 Publication1
Disulfide bondi180 ↔ 220By similarity
Disulfide bondi187 ↔ 213By similarity
Disulfide bondi211 ↔ 244By similarity
Glycosylationi280N-linked (GlcNAc...)1 Publication1
Glycosylationi325N-linked (GlcNAc...)Sequence analysis1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
Glycosylationi439N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylation does not affect the catalytic activity, but is required for proper secretion. A nonglycosylated form was observed in several cell types.1 Publication
In several cell types, the N- and C-termini are cleaved off.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9NZ20.
PaxDbiQ9NZ20.
PeptideAtlasiQ9NZ20.
PRIDEiQ9NZ20.

PTM databases

iPTMnetiQ9NZ20.
PhosphoSitePlusiQ9NZ20.

Expressioni

Tissue specificityi

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).1 Publication

Inductioni

By IL1B/interleukin-1 beta and TNF in microvascular endothelial cells (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000100078.
CleanExiHS_PLA2G3.
GenevisibleiQ9NZ20. HS.

Organism-specific databases

HPAiHPA021016.

Interactioni

Protein-protein interaction databases

BioGridi119074. 2 interactors.
IntActiQ9NZ20. 2 interactors.
STRINGi9606.ENSP00000215885.

Structurei

3D structure databases

ProteinModelPortaliQ9NZ20.
SMRiQ9NZ20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 291Phospholipase A2-likeAdd BLAST142

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IF4P. Eukaryota.
ENOG4111S6V. LUCA.
GeneTreeiENSGT00530000063569.
HOGENOMiHOG000147808.
HOVERGENiHBG053481.
InParanoidiQ9NZ20.
KOiK01047.
OMAiLAPPLDC.
OrthoDBiEOG091G06KL.
PhylomeDBiQ9NZ20.
TreeFamiTF324679.

Family and domain databases

Gene3Di1.20.90.10. 2 hits.
InterProiIPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PfamiPF05826. Phospholip_A2_2. 2 hits.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 2 hits.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NZ20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVQAGLFGM LGFLGVALGG SPALRWYRTS CHLTKAVPGN PLGYLSFLAK
60 70 80 90 100
DAQGLALIHA RWDAHRRLQS CSWEDEPELT AAYGALCAHE TAWGSFIHTP
110 120 130 140 150
GPELQRALAT LQSQWEACRA LEESPAGARK KRAAGQSGVP GGGHQREKRG
160 170 180 190 200
WTMPGTLWCG VGDSAGNSSE LGVFQGPDLC CREHDRCPQN ISPLQYNYGI
210 220 230 240 250
RNYRFHTISH CDCDTRFQQC LQNQHDSISD IVGVAFFNVL EIPCFVLEEQ
260 270 280 290 300
EACVAWYWWG GCRMYGTVPL ARLQPRTFYN ASWSSRATSP TPSSRSPAPP
310 320 330 340 350
KPRQKQHLRK GPPHQKGSKR PSKANTTALQ DPMVSPRLDV APTGLQGPQG
360 370 380 390 400
GLKPQGARWV CRSFRRHLDQ CEHQIGPREI EFQLLNSAQE PLFHCNCTRR
410 420 430 440 450
LARFLRLHSP PEVTNMLWEL LGTTCFKLAP PLDCVEGKNC SRDPRAIRVS
460 470 480 490 500
ARHLRRLQQR RHQLQDKGTD ERQPWPSEPL RGPMSFYNQC LQLTQAARRP

DRQQKSWSQ
Length:509
Mass (Da):57,167
Last modified:January 11, 2011 - v2
Checksum:iED03BED129B0BC9F
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02455570S → A.2 PublicationsCorresponds to variant rs2232176dbSNPEnsembl.1
Natural variantiVAR_024556116E → Q.Corresponds to variant rs2074734dbSNPEnsembl.1
Natural variantiVAR_020288157L → V.Corresponds to variant rs2074735dbSNPEnsembl.1
Natural variantiVAR_056581307H → Y.Corresponds to variant rs2232180dbSNPEnsembl.1
Natural variantiVAR_024557322S → R.Corresponds to variant rs2072193dbSNPEnsembl.1
Natural variantiVAR_034366378R → Q.Corresponds to variant rs2232183dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220490 mRNA. Translation: AAF44746.1.
AC005005 Genomic DNA. Translation: AAD15617.1. Sequence problems.
BC025316 mRNA. Translation: AAH25316.1.
CCDSiCCDS13889.1.
RefSeqiNP_056530.2. NM_015715.4.
UniGeneiHs.149623.

Genome annotation databases

EnsembliENST00000215885; ENSP00000215885; ENSG00000100078.
GeneIDi50487.
KEGGihsa:50487.
UCSCiuc003aka.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220490 mRNA. Translation: AAF44746.1.
AC005005 Genomic DNA. Translation: AAD15617.1. Sequence problems.
BC025316 mRNA. Translation: AAH25316.1.
CCDSiCCDS13889.1.
RefSeqiNP_056530.2. NM_015715.4.
UniGeneiHs.149623.

3D structure databases

ProteinModelPortaliQ9NZ20.
SMRiQ9NZ20.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119074. 2 interactors.
IntActiQ9NZ20. 2 interactors.
STRINGi9606.ENSP00000215885.

Chemistry databases

ChEMBLiCHEMBL4667.
SwissLipidsiSLP:000001086.

PTM databases

iPTMnetiQ9NZ20.
PhosphoSitePlusiQ9NZ20.

Polymorphism and mutation databases

BioMutaiPLA2G3.
DMDMi317373314.

Proteomic databases

EPDiQ9NZ20.
PaxDbiQ9NZ20.
PeptideAtlasiQ9NZ20.
PRIDEiQ9NZ20.

Protocols and materials databases

DNASUi50487.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215885; ENSP00000215885; ENSG00000100078.
GeneIDi50487.
KEGGihsa:50487.
UCSCiuc003aka.4. human.

Organism-specific databases

CTDi50487.
DisGeNETi50487.
GeneCardsiPLA2G3.
H-InvDBHIX0016386.
HGNCiHGNC:17934. PLA2G3.
HPAiHPA021016.
MIMi611651. gene.
neXtProtiNX_Q9NZ20.
OpenTargetsiENSG00000100078.
PharmGKBiPA38267.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF4P. Eukaryota.
ENOG4111S6V. LUCA.
GeneTreeiENSGT00530000063569.
HOGENOMiHOG000147808.
HOVERGENiHBG053481.
InParanoidiQ9NZ20.
KOiK01047.
OMAiLAPPLDC.
OrthoDBiEOG091G06KL.
PhylomeDBiQ9NZ20.
TreeFamiTF324679.

Enzyme and pathway databases

BioCyciZFISH:HS01970-MONOMER.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482925. Acyl chain remodelling of PG.

Miscellaneous databases

GenomeRNAii50487.
PROiQ9NZ20.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100078.
CleanExiHS_PLA2G3.
GenevisibleiQ9NZ20. HS.

Family and domain databases

Gene3Di1.20.90.10. 2 hits.
InterProiIPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PfamiPF05826. Phospholip_A2_2. 2 hits.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 2 hits.
PROSITEiPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA2G3_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ20
Secondary accession number(s): O95768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.