PG12A_MOUSE
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 03-AUG-2022, entry version 156.
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 STRING; 10090.ENSMUSP00000029629; -.
DR PhosphoSitePlus; Q9EPR2; -.
DR EPD; Q9EPR2; -.
DR MaxQB; Q9EPR2; -.
DR PaxDb; Q9EPR2; -.
DR PeptideAtlas; Q9EPR2; -.
DR PRIDE; Q9EPR2; -.
DR ProteomicsDB; 288128; -. [Q9EPR2-1]
DR ProteomicsDB; 288129; -. [Q9EPR2-2]
DR Antibodypedia; 26354; 210 antibodies from 28 providers.
DR DNASU; 66350; -.
DR Ensembl; ENSMUST00000029629; ENSMUSP00000029629; ENSMUSG00000027999. [Q9EPR2-1]
DR Ensembl; ENSMUST00000061165; ENSMUSP00000053651; ENSMUSG00000027999. [Q9EPR2-2]
DR GeneID; 66350; -.
DR KEGG; mmu:66350; -.
DR UCSC; uc008rip.3; mouse. [Q9EPR2-2]
DR UCSC; uc012cxt.2; mouse. [Q9EPR2-1]
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; HDCDEEF; -.
DR OrthoDB; 1299904at2759; -.
DR PhylomeDB; Q9EPR2; -.
DR TreeFam; TF323302; -.
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 73 CRISPR screens.
DR PRO; PR:Q9EPR2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9EPR2; protein.
DR Bgee; ENSMUSG00000027999; Expressed in ileal epithelium and 227 other tissues.
DR ExpressionAtlas; Q9EPR2; baseline and differential.
DR Genevisible; Q9EPR2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IC:MGI.
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 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
