ID   PG12A_MOUSE             Reviewed;         192 AA.
AC   Q9EPR2; Q3TQC4; Q9CQR3; Q9CTL1; Q9D7L3; Q9EPR1;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   02-SEP-2026, entry version 173.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AKR/J;
RX   PubMed=11278438; DOI=10.1074/jbc.m008837200;
RA   Ho I.C., Arm J.P., Bingham C.O. III, Choi A., Austen K.F., Glimcher L.H.;
RT   "A novel group of phospholipase A2s preferentially expressed in type 2
RT   helper T cells.";
RL   J. Biol. Chem. 276:18321-18326(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Olfactory epithelium;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPR2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPR2-2; Sequence=VSP_004509;
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   EMBL; AY007381; AAG23336.1; -; mRNA.
DR   EMBL; AY007382; AAG23337.1; -; mRNA.
DR   EMBL; AK003183; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK009133; BAB26094.1; -; mRNA.
DR   EMBL; AK010011; BAB26641.1; -; mRNA.
DR   EMBL; AK010174; BAB26747.1; -; mRNA.
DR   EMBL; AK163693; BAE37460.1; -; mRNA.
DR   EMBL; BC051117; AAH51117.1; -; mRNA.
DR   CCDS; CCDS17836.1; -. [Q9EPR2-1]
DR   CCDS; CCDS17837.1; -. [Q9EPR2-2]
DR   RefSeq; NP_075685.2; NM_023196.4. [Q9EPR2-1]
DR   RefSeq; NP_904359.1; NM_183423.3. [Q9EPR2-2]
DR   AlphaFoldDB; Q9EPR2; -.
DR   FunCoup; Q9EPR2; 903.
DR   STRING; 10090.ENSMUSP00000029629; -.
DR   PhosphoSitePlus; Q9EPR2; -.
DR   jPOST; Q9EPR2; -.
DR   PaxDb; 10090-ENSMUSP00000029629; -.
DR   PeptideAtlas; Q9EPR2; -.
DR   ProteomicsDB; 288128; -. [Q9EPR2-1]
DR   ProteomicsDB; 288129; -. [Q9EPR2-2]
DR   Antibodypedia; 26354; 215 antibodies from 30 providers.
DR   DNASU; 66350; -.
DR   Ensembl; ENSMUST00000029629.15; ENSMUSP00000029629.9; ENSMUSG00000027999.16. [Q9EPR2-1]
DR   Ensembl; ENSMUST00000061165.9; ENSMUSP00000053651.7; ENSMUSG00000027999.16. [Q9EPR2-2]
DR   GeneID; 66350; -.
DR   KEGG; mmu:66350; -.
DR   UCSC; uc008rip.3; mouse. [Q9EPR2-2]
DR   UCSC; uc012cxt.2; mouse. [Q9EPR2-1]
DR   AGR; MGI:1913600; -.
DR   CTD; 81579; -.
DR   MGI; MGI:1913600; Pla2g12a.
DR   VEuPathDB; HostDB:ENSMUSG00000027999; -.
DR   eggNOG; ENOG502QU22; Eukaryota.
DR   GeneTree; ENSGT00390000008798; -.
DR   HOGENOM; CLU_093969_1_0_1; -.
DR   InParanoid; Q9EPR2; -.
DR   OMA; RAACMCQ; -.
DR   OrthoDB; 3935740at2759; -.
DR   PhylomeDB; Q9EPR2; -.
DR   Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-MMU-1483166; Synthesis of PA.
DR   BioGRID-ORCS; 66350; 5 hits in 78 CRISPR screens.
DR   PRO; PR:Q9EPR2; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9EPR2; protein.
DR   Bgee; ENSMUSG00000027999; Expressed in ileal epithelium and 231 other cell types or tissues.
DR   ExpressionAtlas; Q9EPR2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IC:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   FunFam; 1.20.90.10:FF:000004; Group XIIA secretory phospholipase A2; 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR033113; PLA2_histidine.
DR   InterPro; IPR010711; PLA2G12.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR12824; GROUP XII SECRETORY PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12824:SF7; GROUP XIIA SECRETORY PHOSPHOLIPASE A2; 1.
DR   Pfam; PF06951; PLA2G12; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..192
FT                   /note="Group XIIA secretory phospholipase A2"
FT                   /id="PRO_0000022771"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..73
FT                   /note="MVTPRPAPARSPALLLLLLLATARGQEQDQTTDWRATLKTIRNGIHKIDTYL
FT                   NAALDLLGGEDGLCQYKCSDG -> MKDYHSGPGKYWEPFAFPVGCSGTEEEEGLRIGR
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004509"
FT   CONFLICT        11
FT                   /note="S -> G (in Ref. 1; AAG23336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="P -> H (in Ref. 2; BAB26094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   192 AA;  21319 MW;  670ACE8F6AB6FCA2 CRC64;
     MVTPRPAPAR SPALLLLLLL ATARGQEQDQ TTDWRATLKT IRNGIHKIDT YLNAALDLLG
     GEDGLCQYKC SDGSKPVPRY GYKPSPPNGC GSPLFGVHLN IGIPSLTKCC NQHDRCYETC
     GKSKNDCDEE FQYCLSKICR DVQKTLGLSQ NVQACETTVE LLFDSVIHLG CKPYLDSQRA
     ACWCRYEEKT DL
//