ID   PA2GC_MOUSE             Reviewed;         150 AA.
AC   P48076;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 172.
DE   RecName: Full=Group IIC secretory phospholipase A2;
DE            Short=GIIC sPLA2;
DE            Short=sPLA2-IIC;
DE            EC=3.1.1.4;
DE   AltName: Full=14 kDa phospholipase A2;
DE   AltName: Full=PLA2-8;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase 2C;
DE   Flags: Precursor;
GN   Name=Pla2g2c;
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].
RX   PubMed=9057094;
RX   DOI=10.1002/(sici)1097-4644(19970301)64:3<369::aid-jcb3>3.0.co;2-t;
RA   Chen J., Shao C., Lazar V., Srivastava C.H., Lee W., Tischfield J.A.;
RT   "Localization of group IIc low molecular weight phospholipase A2 mRNA to
RT   meiotic cells in the mouse.";
RL   J. Cell. Biochem. 64:369-375(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-150.
RX   PubMed=8083202; DOI=10.1016/s0021-9258(17)31613-7;
RA   Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.;
RT   "Cloning and characterization of novel rat and mouse low molecular weight
RT   Ca(2+)-dependent phospholipase A2s containing 16 cysteines.";
RL   J. Biol. Chem. 269:23018-23024(1994).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. Testis PA2 may be important in the
CC       production of prostaglandins, by the release of arachidonic acid, which
CC       in turn are necessary for the contractions of the seminiferous tubules
CC       and the testicular capsule; they also seem to decrease sperm transit
CC       time through the male reproductive tract.
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, ECO:0000255|PROSITE-
CC         ProRule:PRU10036};
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 {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- DEVELOPMENTAL STAGE: Expressed mainly in pachytene and secondary
CC       spermatocytes and round spermatids and predominates in stage VI-VII
CC       tubules.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   EMBL; U18119; AAC52936.1; -; mRNA.
DR   CCDS; CCDS18831.1; -.
DR   PIR; A54762; A54762.
DR   RefSeq; NP_032894.2; NM_008868.3.
DR   AlphaFoldDB; P48076; -.
DR   SMR; P48076; -.
DR   FunCoup; P48076; 412.
DR   STRING; 10090.ENSMUSP00000101434; -.
DR   BindingDB; P48076; -.
DR   ChEMBL; CHEMBL5169135; -.
DR   GlyCosmos; P48076; 1 site, No reported glycans.
DR   GlyGen; P48076; 1 site.
DR   PaxDb; 10090-ENSMUSP00000101434; -.
DR   ProteomicsDB; 294320; -.
DR   DNASU; 18781; -.
DR   GeneID; 18781; -.
DR   KEGG; mmu:18781; -.
DR   AGR; MGI:106638; -.
DR   CTD; 391013; -.
DR   MGI; MGI:106638; Pla2g2c.
DR   eggNOG; KOG4087; Eukaryota.
DR   InParanoid; P48076; -.
DR   OrthoDB; 5841574at2759; -.
DR   PhylomeDB; P48076; -.
DR   BioGRID-ORCS; 18781; 2 hits in 79 CRISPR screens.
DR   PRO; PR:P48076; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P48076; protein.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR   GO; GO:0046471; P:phosphatidylglycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0009395; P:phospholipid catabolic process; ISO:GO_Central.
DR   CDD; cd00125; PLA2c; 1.
DR   FunFam; 1.20.90.10:FF:000008; Phospholipase A(2); 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR001211; PLA2.
DR   InterPro; IPR016090; PLA2-like_dom.
DR   InterPro; IPR033112; PLA2_Asp_AS.
DR   InterPro; IPR033113; PLA2_histidine.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR11716:SF5; INACTIVE GROUP IIC SECRETORY PHOSPHOLIPASE A2-RELATED; 1.
DR   PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..150
FT                   /note="Group IIC secretory phospholipase A2"
FT                   /id="PRO_0000022753"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..150
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..107
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..105
FT                   /evidence="ECO:0000255"
FT   CONFLICT        28
FT                   /note="M -> W (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="Y -> W (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   150 AA;  16983 MW;  C2D5EF5E7B19972F CRC64;
     MKGIAIFLVF IFYWTTSTLS SFWQFQRMVK HVTGRSAFFS YYGYGCYCGL GGKGLPVDAT
     DRCCWAHDCC YHKLKEYGCQ PILNAYQFTI VNGTVTCGCT VASSCPCGQK ACECDKQSVY
     CFKENLATYE KAFKQLFPTR PQCGRDKLQC
//