PA2GC_RAT
ID PA2GC_RAT Reviewed; 150 AA.
AC P39878;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
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.
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 -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57473.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U07798; AAA57473.1; ALT_INIT; mRNA.
DR PIR; B54762; B54762.
DR RefSeq; NP_062075.1; NM_019202.2.
DR RefSeq; XP_006239204.1; XM_006239142.3.
DR RefSeq; XP_006239205.1; XM_006239143.3.
DR RefSeq; XP_008762435.1; XM_008764213.2.
DR AlphaFoldDB; P39878; -.
DR SMR; P39878; -.
DR STRING; 10116.ENSRNOP00000039825; -.
DR GlyGen; P39878; 1 site.
DR PaxDb; P39878; -.
DR GeneID; 29387; -.
DR KEGG; rno:29387; -.
DR UCSC; RGD:3340; rat.
DR CTD; 391013; -.
DR RGD; 3340; Pla2g2c.
DR eggNOG; KOG4087; Eukaryota.
DR InParanoid; P39878; -.
DR OrthoDB; 1422829at2759; -.
DR PRO; PR:P39878; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR GO; GO:0005543; F:phospholipid binding; 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; IBA:GO_Central.
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_0000022754"
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"
SQ SEQUENCE 150 AA; 16919 MW; F80575BE19A3B7FF CRC64;
MKGIAVFLVF IFCWTTSTLS SFWQFQRMVK HITGRSAFFS YYGYGCYCGL GGRGIPVDAT
DRCCWAHDCC YHKLKEYGCQ PILNAYQFAI VNGTVTCGCT MGGGCLCGQK ACECDKLSVY
CFKENLATYE KTFKQLFPTR PQCGRDKLHC
