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O15496 (PA2GX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 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 names
Name:PLA2G10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length165 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. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit. Ref.6

Subcellular location

Secreted.

Tissue specificity

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

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Non-traceable author statement PubMed 18511424. Source: BHF-UCL

axon guidance

Inferred from direct assay PubMed 15927955. Source: MGI

cholesterol homeostasis

Inferred from sequence or structural similarity PubMed 20844270. Source: BHF-UCL

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lysophospholipid transport

Inferred from direct assay PubMed 15927955. Source: MGI

negative regulation of cholesterol efflux

Inferred from sequence or structural similarity PubMed 20844270. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20844270. Source: BHF-UCL

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

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

phosphatidylinositol acyl-chain remodeling

Traceable author statement. Source: Reactome

phosphatidylserine acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of arachidonic acid secretion

Inferred from sequence or structural similarity PubMed 20844270. Source: BHF-UCL

positive regulation of cellular protein metabolic process

Inferred from mutant phenotype PubMed 18511424. Source: BHF-UCL

positive regulation of lipid storage

Inferred from mutant phenotype PubMed 18511424. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Inferred by curator PubMed 18511424. Source: BHF-UCL

positive regulation of prostaglandin secretion

Inferred from mutant phenotype PubMed 18511424. Source: BHF-UCL

regulation of macrophage activation

Inferred from mutant phenotype PubMed 18511424. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipase A2 activity

Traceable author statement Ref.1. Source: ProtInc

phospholipase activity

Inferred from sequence or structural similarity PubMed 20844270. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 4211 Potential
PRO_0000022764
Chain43 – 165123Group 10 secretory phospholipase A2
PRO_0000022765

Sites

Active site881 Ref.6
Active site1331 Ref.6
Metal binding681Calcium; via carbonyl oxygen
Metal binding701Calcium; via carbonyl oxygen
Metal binding721Calcium; via carbonyl oxygen
Metal binding891Calcium

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 111 Ref.6
Disulfide bond67 ↔ 157 Ref.6
Disulfide bond69 ↔ 85 Ref.6
Disulfide bond84 ↔ 139 Ref.6
Disulfide bond90 ↔ 164 Ref.6
Disulfide bond91 ↔ 132 Ref.6
Disulfide bond100 ↔ 125 Ref.6
Disulfide bond118 ↔ 130 Ref.6

Secondary structure

....................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15496 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: AD197A164319F102

FASTA16518,153
        10         20         30         40         50         60 
MGPLPVCLPI MLLLLLPSLL LLLLLPGPGS GEASRILRVH RRGILELAGT VGCVGPRTPI 

        70         80         90        100        110        120 
AYMKYGCFCG LGGHGQPRDA IDWCCHGHDC CYTRAEEAGC SPKTERYSWQ CVNQSVLCGP 

       130        140        150        160 
AENKCQELLC KCDQEIANCL AQTEYNLKYL FYPQFLCEPD SPKCD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10555.1.
RefSeqNP_003552.1. NM_003561.1.
XP_006721021.1. XM_006720958.1.
XP_006725277.1. XM_006725214.1.
UniGeneHs.567366.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LE6X-ray1.97A/B/C43-165[»]
1LE7X-ray2.09A/B43-165[»]
ProteinModelPortalO15496.
SMRO15496. Positions 43-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO15496. 1 interaction.
MINTMINT-1411106.
STRING9606.ENSP00000393847.

Chemistry

BindingDBO15496.
ChEMBLCHEMBL4342.

Proteomic databases

PaxDbO15496.
PRIDEO15496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000438167; ENSP00000393847; ENSG00000069764.
GeneID8399.
KEGGhsa:8399.
UCSCuc002dcq.3. human.

Organism-specific databases

CTD8399.
GeneCardsGC16M014767.
H-InvDBHIX0026959.
HGNCHGNC:9029. PLA2G10.
HPAHPA041893.
MIM603603. gene.
neXtProtNX_O15496.
PharmGKBPA33360.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284162.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidO15496.
KOK01047.
OMACQELLCK.
OrthoDBEOG7N63PF.
PhylomeDBO15496.
TreeFamTF319283.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO15496.
BgeeO15496.
CleanExHS_PLA2G10.
GenevestigatorO15496.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15496.
GeneWikiPLA2G10.
GenomeRNAi8399.
NextBio31434.
PROO15496.
SOURCESearch...

Entry information

Entry namePA2GX_HUMAN
AccessionPrimary (citable) accession number: O15496
Secondary accession number(s): Q14DU3, Q6NT23
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 137 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM