Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BZM1 (PG12A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 XIIA secretory phospholipase A2

Short name=GXII sPLA2
Short name=sPLA2-XII
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase 12A
Gene names
Name:PLA2G12A
Synonyms:PLA2G12
ORF Names:FKSG38, UNQ2519/PRO6012
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length189 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. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or -phosphatidylethanolamine. Ref.5

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted. Cytoplasm Ref.5.

Tissue specificity

Abundantly expressed in heart, skeletal muscle, kidney, liver and pancreas.

Sequence similarities

Belongs to the phospholipase A2 family.

Mass spectrometry

Molecular mass is 18702.6±0.5 Da from positions 22 - 189. Determined by MALDI. Ref.1

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

extracellular region

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipase A2 activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Probable
Chain23 – 189167Group XIIA secretory phospholipase A2
PRO_0000022770

Sites

Active site1101 By similarity
Active site1251 By similarity
Metal binding881Calcium; via carbonyl oxygen By similarity
Metal binding901Calcium; via carbonyl oxygen By similarity
Metal binding921Calcium; via carbonyl oxygen By similarity
Metal binding1111Calcium By similarity

Experimental info

Sequence conflict94 – 952Missing in AAG50289. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BZM1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7979881D6E9223A4

FASTA18921,067
        10         20         30         40         50         60 
MALLSRPALT LLLLLMAAVV RCQEQAQTTD WRATLKTIRN GVHKIDTYLN AALDLLGGED 

        70         80         90        100        110        120 
GLCQYKCSDG SKPFPRYGYK PSPPNGCGSP LFGVHLNIGI PSLTKCCNQH DRCYETCGKS 

       130        140        150        160        170        180 
KNDCDEEFQY CLSKICRDVQ KTLGLTQHVQ ACETTVELLF DSVIHLGCKP YLDSQRAACR 


CHYEEKTDL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and recombinant expression of a structurally novel human secreted phospholipase A2."
Gelb M.H., Valentin E., Ghomashchi F., Lazdunski M., Lambeau G.
J. Biol. Chem. 275:39823-39826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MASS SPECTROMETRY.
[2]"Identification of FKSG38, a novel gene located on human chromosome 4q25."
Wang Y.-G., Gong L.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Tissue: Uterus.
[5]"Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII)."
Murakami M., Masuda S., Shimbara S., Bezzine S., Lazdunski M., Lambeau G., Gelb M.H., Matsukura S., Kokubu F., Adachi M., Kudo I.
J. Biol. Chem. 278:10657-10667(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF306567 mRNA. Translation: AAG50243.1.
AF332892 mRNA. Translation: AAG50289.1.
AY359024 mRNA. Translation: AAQ89383.1.
BC017218 mRNA. Translation: AAH17218.1.
RefSeqNP_110448.2. NM_030821.4.
UniGeneHs.389452.

3D structure databases

ProteinModelPortalQ9BZM1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123539. 10 interactions.
IntActQ9BZM1. 10 interactions.
STRING9606.ENSP00000243501.

Chemistry

ChEMBLCHEMBL6122.

PTM databases

PhosphoSiteQ9BZM1.

Polymorphism databases

DMDM20143881.

Proteomic databases

PaxDbQ9BZM1.
PeptideAtlasQ9BZM1.
PRIDEQ9BZM1.

Protocols and materials databases

DNASU81579.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243501; ENSP00000243501; ENSG00000123739.
ENST00000502283; ENSP00000425274; ENSG00000123739.
GeneID81579.
KEGGhsa:81579.
UCSCuc003hzp.3. human.

Organism-specific databases

CTD81579.
GeneCardsGC04M110631.
HGNCHGNC:18554. PLA2G12A.
HPAHPA035909.
MIM611652. gene.
neXtProtNX_Q9BZM1.
PharmGKBPA38347.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68062.
HOGENOMHOG000247019.
HOVERGENHBG053577.
InParanoidQ9BZM1.
KOK01047.
OMADRCYDTC.
OrthoDBEOG7J1818.
PhylomeDBQ9BZM1.
TreeFamTF323302.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9BZM1.
BgeeQ9BZM1.
CleanExHS_PLA2G12A.
GenevestigatorQ9BZM1.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
IPR010711. PLipase_A2_secretory_G12.
[Graphical view]
PANTHERPTHR12824. PTHR12824. 1 hit.
PfamPF06951. PLA2G12. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLA2G12A. human.
GeneWikiPLA2G12A.
GenomeRNAi81579.
NextBio71900.
PROQ9BZM1.
SOURCESearch...

Entry information

Entry namePG12A_HUMAN
AccessionPrimary (citable) accession number: Q9BZM1
Secondary accession number(s): Q9BZ89
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 124 of the entry and version 1 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM