PA2GC_MOUSE
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 03-AUG-2022, entry version 158.
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 STRING; 10090.ENSMUSP00000101434; -.
DR GlyGen; P48076; 1 site.
DR PaxDb; P48076; -.
DR PRIDE; P48076; -.
DR ProteomicsDB; 294320; -.
DR DNASU; 18781; -.
DR GeneID; 18781; -.
DR KEGG; mmu:18781; -.
DR CTD; 391013; -.
DR MGI; MGI:106638; Pla2g2c.
DR eggNOG; KOG4087; Eukaryota.
DR InParanoid; P48076; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P48076; -.
DR BioGRID-ORCS; 18781; 2 hits in 74 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:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISO:MGI.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 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
