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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Calcium; via carbonyl oxygen
Metal bindingi70 – 701Calcium; via carbonyl oxygen
Metal bindingi72 – 721Calcium; via carbonyl oxygen
Active sitei88 – 8811 Publication
Metal bindingi89 – 891Calcium
Active sitei133 – 13311 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phospholipase A2 activity Source: ProtInc
  3. phospholipase activity Source: BHF-UCL

GO - Biological processi

  1. arachidonic acid metabolic process Source: BHF-UCL
  2. axon guidance Source: MGI
  3. cholesterol homeostasis Source: BHF-UCL
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. lipid catabolic process Source: UniProtKB-KW
  6. lysophospholipid transport Source: MGI
  7. negative regulation of cholesterol efflux Source: BHF-UCL
  8. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  9. phosphatidic acid biosynthetic process Source: Reactome
  10. phosphatidylcholine acyl-chain remodeling Source: Reactome
  11. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
  12. phosphatidylglycerol acyl-chain remodeling Source: Reactome
  13. phosphatidylinositol acyl-chain remodeling Source: Reactome
  14. phosphatidylserine acyl-chain remodeling Source: Reactome
  15. phospholipid metabolic process Source: Reactome
  16. positive regulation of arachidonic acid secretion Source: BHF-UCL
  17. positive regulation of cellular protein metabolic process Source: BHF-UCL
  18. positive regulation of lipid storage Source: BHF-UCL
  19. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  20. positive regulation of prostaglandin secretion Source: BHF-UCL
  21. regulation of macrophage activation Source: BHF-UCL
  22. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

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
ProteomesiUP000005640: Chromosome 16, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:9029. PLA2G10.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 4211Sequence AnalysisPRO_0000022764Add
BLAST
Chaini43 – 165123Group 10 secretory phospholipase A2PRO_0000022765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi118 ↔ 1301 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO15496.
PRIDEiO15496.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO15496.
CleanExiHS_PLA2G10.
ExpressionAtlasiO15496. baseline.
GenevestigatoriO15496.

Organism-specific databases

HPAiHPA041893.

Interactioni

Protein-protein interaction databases

IntActiO15496. 1 interaction.
MINTiMINT-1411106.
STRINGi9606.ENSP00000393847.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5411Combined sources
Beta strandi55 – 573Combined sources
Helixi59 – 624Combined sources
Beta strandi63 – 653Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 724Combined sources
Helixi80 – 9718Combined sources
Turni102 – 1043Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi115 – 1184Combined sources
Helixi124 – 14118Combined sources
Helixi147 – 1493Combined sources
Helixi154 – 1563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
4UY1X-ray2.20A/B43-165[»]
ProteinModelPortaliO15496.
SMRiO15496. Positions 43-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15496.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG284162.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiO15496.
KOiK01047.
OMAiCQELLCK.
OrthoDBiEOG7N63PF.
PhylomeDBiO15496.
TreeFamiTF319283.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[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_003561.1.
XP_006721021.1. XM_006720958.1.
XP_006725277.1. XM_006725214.1.
UniGeneiHs.567366.

Genome annotation databases

EnsembliENST00000438167; ENSP00000393847; ENSG00000069764.
ENST00000621727; ENSP00000479397; ENSG00000276870.
GeneIDi8399.
KEGGihsa:8399.
UCSCiuc002dcq.3. 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_003561.1.
XP_006721021.1. XM_006720958.1.
XP_006725277.1. XM_006725214.1.
UniGeneiHs.567366.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
4UY1X-ray2.20A/B43-165[»]
ProteinModelPortaliO15496.
SMRiO15496. Positions 43-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO15496. 1 interaction.
MINTiMINT-1411106.
STRINGi9606.ENSP00000393847.

Chemistry

BindingDBiO15496.
ChEMBLiCHEMBL4342.

Proteomic databases

PaxDbiO15496.
PRIDEiO15496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000438167; ENSP00000393847; ENSG00000069764.
ENST00000621727; ENSP00000479397; ENSG00000276870.
GeneIDi8399.
KEGGihsa:8399.
UCSCiuc002dcq.3. human.

Organism-specific databases

CTDi8399.
GeneCardsiGC16M014767.
H-InvDBHIX0026959.
HGNCiHGNC:9029. PLA2G10.
HPAiHPA041893.
MIMi603603. gene.
neXtProtiNX_O15496.
PharmGKBiPA33360.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284162.
GeneTreeiENSGT00760000119160.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiO15496.
KOiK01047.
OMAiCQELLCK.
OrthoDBiEOG7N63PF.
PhylomeDBiO15496.
TreeFamiTF319283.

Enzyme and pathway databases

ReactomeiREACT_120722. Acyl chain remodelling of PI.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
REACT_121369. Acyl chain remodelling of PE.
REACT_121384. Acyl chain remodelling of PS.

Miscellaneous databases

EvolutionaryTraceiO15496.
GeneWikiiPLA2G10.
GenomeRNAii8399.
NextBioi31434.
PROiO15496.
SOURCEiSearch...

Gene expression databases

BgeeiO15496.
CleanExiHS_PLA2G10.
ExpressionAtlasiO15496. baseline.
GenevestigatoriO15496.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2."
    Cupillard L., Koumanov K., Mattei M.-G., Lazdunski M., Lambeau G.
    J. Biol. Chem. 272:15745-15752(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Lung.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes."
    Pan Y.H., Yu B.Z., Singer A.G., Ghomashchi F., Lambeau G., Gelb M.H., Jain M.K., Bahnson B.J.
    J. Biol. Chem. 277:29086-29093(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 43-165, DISULFIDE BONDS, ACTIVE SITE, COFACTOR, CALCIUM-BINDING SITES.

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: January 7, 2015
This is version 142 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

External Data

Dasty 3

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 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.