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Q9QXX3 (PA2GX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length151 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.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed in various tissues including the lung, thymus, and spleen.

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
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence orthology PubMed 15927955. Source: MGI

cholesterol homeostasis

Inferred from mutant phenotype PubMed 20844270. Source: BHF-UCL

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lysophospholipid transport

Inferred from sequence orthology PubMed 15927955. Source: MGI

negative regulation of cholesterol efflux

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

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 20844270. Source: BHF-UCL

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of arachidonic acid secretion

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

positive regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipid storage

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

regulation of macrophage activation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipase A2 activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase activity

Inferred from mutant phenotype PubMed 20844270. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.2
Propeptide18 – 2811
PRO_0000022766
Chain29 – 151123Group 10 secretory phospholipase A2
PRO_0000022767

Sites

Active site741 By similarity
Active site1191 By similarity
Metal binding541Calcium; via carbonyl oxygen By similarity
Metal binding561Calcium; via carbonyl oxygen By similarity
Metal binding581Calcium; via carbonyl oxygen By similarity
Metal binding751Calcium By similarity

Amino acid modifications

Disulfide bond39 ↔ 97 By similarity
Disulfide bond53 ↔ 143 By similarity
Disulfide bond55 ↔ 71 By similarity
Disulfide bond70 ↔ 125 By similarity
Disulfide bond76 ↔ 150 By similarity
Disulfide bond77 ↔ 118 By similarity
Disulfide bond86 ↔ 111 By similarity
Disulfide bond104 ↔ 116 By similarity

Experimental info

Sequence conflict1511N → D in AAG43522. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QXX3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 05D15E70BC2C9294

FASTA15117,005
        10         20         30         40         50         60 
MLLLLLLLLL GPGPGFSEAT RRSHVYKRGL LELAGTLDCV GPRSPMAYMN YGCYCGLGGH 

        70         80         90        100        110        120 
GEPRDAIDWC CYHHDCCYSR AQDAGCSPKL DRYPWKCMDH HILCGPAENK CQELLCRCDE 

       130        140        150 
ELAYCLAGTE YHLKYLFFPS ILCEKDSPKC N 

« Hide

References

[1]"On the diversity of secreted phospholipases A2. Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes."
Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.
J. Biol. Chem. 274:31195-31202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor."
Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K., Fujii N., Ishizaki J., Arita H., Hanasaki K.
Arch. Biochem. Biophys. 381:31-42(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-30, CHARACTERIZATION.
Strain: BALB/c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF166097 mRNA. Translation: AAF04498.2.
AF210429 mRNA. Translation: AAG43522.1.
CCDSCCDS27967.1.
RefSeqNP_036117.1. NM_011987.3.
UniGeneMm.4214.

3D structure databases

ProteinModelPortalQ9QXX3.
SMRQ9QXX3. Positions 29-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000023364.

Chemistry

BindingDBQ9QXX3.
ChEMBLCHEMBL4200.

Proteomic databases

PRIDEQ9QXX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023364; ENSMUSP00000023364; ENSMUSG00000022683.
GeneID26565.
KEGGmmu:26565.
UCSCuc007ygh.1. mouse.

Organism-specific databases

CTD8399.
MGIMGI:1347522. Pla2g10.

Phylogenomic databases

eggNOGNOG284162.
GeneTreeENSGT00710000106605.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidQ9QXX3.
KOK01047.
OMACDEELAY.
PhylomeDBQ9QXX3.
TreeFamTF319283.

Gene expression databases

ArrayExpressQ9QXX3.
BgeeQ9QXX3.
CleanExMM_PLA2G10.
GenevestigatorQ9QXX3.

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

NextBio304643.
PROQ9QXX3.
SOURCESearch...

Entry information

Entry namePA2GX_MOUSE
AccessionPrimary (citable) accession number: Q9QXX3
Secondary accession number(s): Q9EQK6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot