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Protein

Group 10 secretory phospholipase A2

Gene

PLA2G10

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. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine.

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi68Calcium; via carbonyl oxygen1
Metal bindingi70Calcium; via carbonyl oxygen1
Metal bindingi72Calcium; via carbonyl oxygen1
Active sitei881 Publication1
Metal bindingi89Calcium1
Active sitei1331 Publication1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: Reactome
  • phospholipase activity Source: BHF-UCL

GO - Biological processi

  • arachidonic acid metabolic process Source: BHF-UCL
  • arachidonic acid secretion Source: InterPro
  • axon guidance Source: MGI
  • cholesterol homeostasis Source: BHF-UCL
  • lipid catabolic process Source: UniProtKB-KW
  • lysophospholipid transport Source: MGI
  • negative regulation of cholesterol efflux Source: BHF-UCL
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • phosphatidic acid biosynthetic process Source: Reactome
  • phosphatidylcholine acyl-chain remodeling Source: Reactome
  • phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  • phosphatidylglycerol acyl-chain remodeling Source: Reactome
  • phosphatidylinositol acyl-chain remodeling Source: Reactome
  • phosphatidylserine acyl-chain remodeling Source: Reactome
  • positive regulation of arachidonic acid secretion Source: BHF-UCL
  • positive regulation of cellular protein metabolic process Source: BHF-UCL
  • positive regulation of lipid storage Source: BHF-UCL
  • positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • positive regulation of prostaglandin secretion Source: BHF-UCL
  • regulation of macrophage activation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS00970-MONOMER.
BRENDAi3.1.1.4. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483166. Synthesis of PA.

Chemistry databases

SwissLipidsiSLP:000001084.

Names & Taxonomyi

Protein namesi
Recommended name:
Group 10 secretory phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group X secretory phospholipase A2
Short name:
GX sPLA2
Short name:
sPLA2-X
Phosphatidylcholine 2-acylhydrolase 10
Gene namesi
Name:PLA2G10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:9029. PLA2G10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi8399.
OpenTargetsiENSG00000069764.
ENSG00000276870.
PharmGKBiPA33360.

Chemistry databases

ChEMBLiCHEMBL4342.
GuidetoPHARMACOLOGYi1422.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000002276432 – 42Sequence analysisAdd BLAST11
ChainiPRO_000002276543 – 165Group 10 secretory phospholipase A2Add BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 1111 Publication
Disulfide bondi67 ↔ 1571 Publication
Disulfide bondi69 ↔ 851 Publication
Disulfide bondi84 ↔ 1391 Publication
Disulfide bondi90 ↔ 1641 Publication
Disulfide bondi91 ↔ 1321 Publication
Disulfide bondi100 ↔ 1251 Publication
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi118 ↔ 1301 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO15496.
PeptideAtlasiO15496.
PRIDEiO15496.

PTM databases

iPTMnetiO15496.

Expressioni

Tissue specificityi

Found in spleen, thymus, peripheral blood leukocytes, pancreas, lung, and colon.

Gene expression databases

BgeeiENSG00000069764.
CleanExiHS_PLA2G10.
ExpressionAtlasiO15496. baseline and differential.
GenevisibleiO15496. HS.

Organism-specific databases

HPAiHPA041893.

Interactioni

Protein-protein interaction databases

BioGridi113987. 52 interactors.
IntActiO15496. 1 interactor.
MINTiMINT-1411106.
STRINGi9606.ENSP00000393847.

Chemistry databases

BindingDBiO15496.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 54Combined sources11
Beta strandi55 – 57Combined sources3
Helixi59 – 62Combined sources4
Beta strandi63 – 65Combined sources3
Turni66 – 68Combined sources3
Beta strandi69 – 72Combined sources4
Helixi80 – 97Combined sources18
Turni102 – 104Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi116 – 118Combined sources3
Helixi124 – 141Combined sources18
Helixi147 – 149Combined sources3
Helixi154 – 156Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
4UY1X-ray2.20A/B43-165[»]
5G3MX-ray1.85A/B43-165[»]
ProteinModelPortaliO15496.
SMRiO15496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15496.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiO15496.
KOiK01047.
OMAiQELLCKC.
OrthoDBiEOG091G0UZ3.
PhylomeDBiO15496.
TreeFamiTF319283.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O15496-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT
60 70 80 90 100
VGCVGPRTPI AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC
110 120 130 140 150
SPKTERYSWQ CVNQSVLCGP AENKCQELLC KCDQEIANCL AQTEYNLKYL
160
FYPQFLCEPD SPKCD
Length:165
Mass (Da):18,153
Last modified:June 16, 2009 - v3
Checksum:iAD197A164319F102
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95301 mRNA. Translation: AAB64410.1.
CR456885 mRNA. Translation: CAG33166.1.
AC009167 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85104.1.
BC069539 mRNA. Translation: AAH69539.1.
BC106731 mRNA. Translation: AAI06732.1.
BC106732 mRNA. Translation: AAI06733.1.
BC111804 mRNA. Translation: AAI11805.1.
CCDSiCCDS10555.1.
RefSeqiNP_003552.1. NM_003561.2.
UniGeneiHs.567366.

Genome annotation databases

EnsembliENST00000438167; ENSP00000393847; ENSG00000069764.
ENST00000621727; ENSP00000479397; ENSG00000276870.
GeneIDi8399.
KEGGihsa:8399.
UCSCiuc002dcq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95301 mRNA. Translation: AAB64410.1.
CR456885 mRNA. Translation: CAG33166.1.
AC009167 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85104.1.
BC069539 mRNA. Translation: AAH69539.1.
BC106731 mRNA. Translation: AAI06732.1.
BC106732 mRNA. Translation: AAI06733.1.
BC111804 mRNA. Translation: AAI11805.1.
CCDSiCCDS10555.1.
RefSeqiNP_003552.1. NM_003561.2.
UniGeneiHs.567366.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
4UY1X-ray2.20A/B43-165[»]
5G3MX-ray1.85A/B43-165[»]
ProteinModelPortaliO15496.
SMRiO15496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113987. 52 interactors.
IntActiO15496. 1 interactor.
MINTiMINT-1411106.
STRINGi9606.ENSP00000393847.

Chemistry databases

BindingDBiO15496.
ChEMBLiCHEMBL4342.
GuidetoPHARMACOLOGYi1422.
SwissLipidsiSLP:000001084.

PTM databases

iPTMnetiO15496.

Proteomic databases

PaxDbiO15496.
PeptideAtlasiO15496.
PRIDEiO15496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000438167; ENSP00000393847; ENSG00000069764.
ENST00000621727; ENSP00000479397; ENSG00000276870.
GeneIDi8399.
KEGGihsa:8399.
UCSCiuc002dcq.4. human.

Organism-specific databases

CTDi8399.
DisGeNETi8399.
GeneCardsiPLA2G10.
H-InvDBHIX0026959.
HGNCiHGNC:9029. PLA2G10.
HPAiHPA041893.
MIMi603603. gene.
neXtProtiNX_O15496.
OpenTargetsiENSG00000069764.
ENSG00000276870.
PharmGKBiPA33360.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiO15496.
KOiK01047.
OMAiQELLCKC.
OrthoDBiEOG091G0UZ3.
PhylomeDBiO15496.
TreeFamiTF319283.

Enzyme and pathway databases

BioCyciZFISH:HS00970-MONOMER.
BRENDAi3.1.1.4. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483166. Synthesis of PA.

Miscellaneous databases

EvolutionaryTraceiO15496.
GeneWikiiPLA2G10.
GenomeRNAii8399.
PROiO15496.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000069764.
CleanExiHS_PLA2G10.
ExpressionAtlasiO15496. baseline and differential.
GenevisibleiO15496. HS.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA2GX_HUMAN
AccessioniPrimary (citable) accession number: O15496
Secondary accession number(s): Q14DU3, Q6NT23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 16, 2009
Last modified: November 30, 2016
This is version 159 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.