PG12A_HUMAN
ID PG12A_HUMAN Reviewed; 189 AA.
AC Q9BZM1; Q9BZ89;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Group XIIA secretory phospholipase A2;
DE Short=GXII sPLA2;
DE Short=sPLA2-XII;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 12A;
DE Flags: Precursor;
GN Name=PLA2G12A; Synonyms=PLA2G12; ORFNames=FKSG38, UNQ2519/PRO6012;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=11031251; DOI=10.1074/jbc.c000671200;
RA Gelb M.H., Valentin E., Ghomashchi F., Lazdunski M., Lambeau G.;
RT "Cloning and recombinant expression of a structurally novel human secreted
RT phospholipase A2.";
RL J. Biol. Chem. 275:39823-39826(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Identification of FKSG38, a novel gene located on human chromosome 4q25.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12522102; DOI=10.1074/jbc.m211325200;
RA Murakami M., Masuda S., Shimbara S., Bezzine S., Lazdunski M., Lambeau G.,
RA Gelb M.H., Matsukura S., Kokubu F., Adachi M., Kudo I.;
RT "Cellular arachidonate-releasing function of novel classes of secretory
RT phospholipase A2s (groups III and XII).";
RL J. Biol. Chem. 278:10657-10667(2003).
CC -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity
CC toward sn-2-arachidonoyl- or linoleoyl-phosphatidylcholine or
CC -phosphatidylethanolamine. {ECO:0000269|PubMed:12522102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q9BZM1; P28799: GRN; NbExp=3; IntAct=EBI-3916751, EBI-747754;
CC Q9BZM1; O76024: WFS1; NbExp=3; IntAct=EBI-3916751, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12522102}. Cytoplasm
CC {ECO:0000269|PubMed:12522102}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart, skeletal muscle,
CC kidney, liver and pancreas.
CC -!- MASS SPECTROMETRY: Mass=18702.6; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11031251};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF306567; AAG50243.1; -; mRNA.
DR EMBL; AF332892; AAG50289.1; -; mRNA.
DR EMBL; AY359024; AAQ89383.1; -; mRNA.
DR EMBL; BC017218; AAH17218.1; -; mRNA.
DR CCDS; CCDS3686.1; -.
DR RefSeq; NP_110448.2; NM_030821.4.
DR AlphaFoldDB; Q9BZM1; -.
DR BioGRID; 123539; 15.
DR IntAct; Q9BZM1; 13.
DR STRING; 9606.ENSP00000243501; -.
DR BindingDB; Q9BZM1; -.
DR ChEMBL; CHEMBL6122; -.
DR iPTMnet; Q9BZM1; -.
DR PhosphoSitePlus; Q9BZM1; -.
DR BioMuta; PLA2G12A; -.
DR DMDM; 20143881; -.
DR EPD; Q9BZM1; -.
DR jPOST; Q9BZM1; -.
DR MassIVE; Q9BZM1; -.
DR MaxQB; Q9BZM1; -.
DR PaxDb; Q9BZM1; -.
DR PeptideAtlas; Q9BZM1; -.
DR PRIDE; Q9BZM1; -.
DR ProteomicsDB; 79873; -.
DR Antibodypedia; 26354; 210 antibodies from 28 providers.
DR DNASU; 81579; -.
DR Ensembl; ENST00000243501.10; ENSP00000243501.5; ENSG00000123739.11.
DR GeneID; 81579; -.
DR KEGG; hsa:81579; -.
DR MANE-Select; ENST00000243501.10; ENSP00000243501.5; NM_030821.5; NP_110448.2.
DR UCSC; uc003hzp.4; human.
DR CTD; 81579; -.
DR DisGeNET; 81579; -.
DR GeneCards; PLA2G12A; -.
DR HGNC; HGNC:18554; PLA2G12A.
DR HPA; ENSG00000123739; Low tissue specificity.
DR MIM; 611652; gene.
DR neXtProt; NX_Q9BZM1; -.
DR OpenTargets; ENSG00000123739; -.
DR PharmGKB; PA38347; -.
DR VEuPathDB; HostDB:ENSG00000123739; -.
DR eggNOG; ENOG502QU22; Eukaryota.
DR GeneTree; ENSGT00390000008798; -.
DR InParanoid; Q9BZM1; -.
DR OMA; HDCDEEF; -.
DR OrthoDB; 1299904at2759; -.
DR PhylomeDB; Q9BZM1; -.
DR TreeFam; TF323302; -.
DR PathwayCommons; Q9BZM1; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q9BZM1; -.
DR BioGRID-ORCS; 81579; 30 hits in 1041 CRISPR screens.
DR ChiTaRS; PLA2G12A; human.
DR GeneWiki; PLA2G12A; -.
DR GenomeRNAi; 81579; -.
DR Pharos; Q9BZM1; Tbio.
DR PRO; PR:Q9BZM1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BZM1; protein.
DR Bgee; ENSG00000123739; Expressed in oviduct epithelium and 192 other tissues.
DR ExpressionAtlas; Q9BZM1; baseline and differential.
DR Genevisible; Q9BZM1; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; NAS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR010711; PLA2G12.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR12824; PTHR12824; 1.
DR Pfam; PF06951; PLA2G12; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000305"
FT CHAIN 23..189
FT /note="Group XIIA secretory phospholipase A2"
FT /id="PRO_0000022770"
FT ACT_SITE 110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CONFLICT 94..95
FT /note="Missing (in Ref. 2; AAG50289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21067 MW; 7979881D6E9223A4 CRC64;
MALLSRPALT LLLLLMAAVV RCQEQAQTTD WRATLKTIRN GVHKIDTYLN AALDLLGGED
GLCQYKCSDG SKPFPRYGYK PSPPNGCGSP LFGVHLNIGI PSLTKCCNQH DRCYETCGKS
KNDCDEEFQY CLSKICRDVQ KTLGLTQHVQ ACETTVELLF DSVIHLGCKP YLDSQRAACR
CHYEEKTDL
