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Calcium-dependent phospholipase A2 (EC 3.1.1.4) (Group V phospholipase A2) (PLA2-10) (Phosphatidylcholine 2-acylhydrolase 5)

 PA2G5_RAT               Reviewed;         137 AA.
P51433; Q6DQ96;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 136.
RecName: Full=Calcium-dependent phospholipase A2;
EC=3.1.1.4;
AltName: Full=Group V phospholipase A2;
AltName: Full=PLA2-10;
AltName: Full=Phosphatidylcholine 2-acylhydrolase 5;
Flags: Precursor;
Name=Pla2g5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7947992; DOI=10.1016/0005-2760(94)90099-X;
Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.;
"Cloning, expression and partial characterization of a novel rat
phospholipase A2.";
Biochim. Biophys. Acta 1215:115-120(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Ovary;
Liang N.S., Su Q.B., Li Y., Yang F., Lu Y., Xie Y.A.;
"Cloning and sequence determination of rat group V phospholipase A2
from ovary.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes L-
alpha-palmitoyl-2-oleoyl phosphatidylcholine more efficiently than
L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L-alpha-1-
palmitoyl-2-arachidonyl phosphatidylethanolamine or L-alpha-1-
stearoyl-2-arachidonyl phosphatidylinositol.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: This enzyme lacks one of the seven disulfide bonds found in
similar PA2 proteins.
-!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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EMBL; U03763; AAA82112.1; -; mRNA.
EMBL; AY651028; AAT68714.1; -; mRNA.
EMBL; BC085745; AAH85745.1; -; mRNA.
RefSeq; NP_058870.1; NM_017174.1.
RefSeq; XP_006239201.1; XM_006239139.3.
RefSeq; XP_008762432.1; XM_008764210.2.
UniGene; Rn.20244; -.
ProteinModelPortal; P51433; -.
SMR; P51433; -.
STRING; 10116.ENSRNOP00000022715; -.
PaxDb; P51433; -.
Ensembl; ENSRNOT00000022716; ENSRNOP00000022715; ENSRNOG00000016838.
GeneID; 29354; -.
KEGG; rno:29354; -.
UCSC; RGD:62051; rat.
CTD; 5322; -.
RGD; 62051; Pla2g5.
eggNOG; KOG4087; Eukaryota.
eggNOG; ENOG411283D; LUCA.
GeneTree; ENSGT00760000119160; -.
HOGENOM; HOG000231749; -.
HOVERGEN; HBG008137; -.
InParanoid; P51433; -.
KO; K01047; -.
OMA; YCLKRNL; -.
OrthoDB; EOG091G0UZ3; -.
PhylomeDB; P51433; -.
TreeFam; TF319283; -.
Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
Reactome; R-RNO-1483166; Synthesis of PA.
PRO; PR:P51433; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000016838; -.
Genevisible; P51433; RN.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:RGD.
GO; GO:0008201; F:heparin binding; IDA:RGD.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0050482; P:arachidonic acid secretion; IDA:RGD.
GO; GO:0019370; P:leukotriene biosynthetic process; IDA:RGD.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006663; P:platelet activating factor biosynthetic process; IDA:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
2: Evidence at transcript level;
Calcium; Complete proteome; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 137 Calcium-dependent phospholipase A2.
/FTId=PRO_0000022763.
ACT_SITE 67 67 {ECO:0000250}.
ACT_SITE 111 111 {ECO:0000250}.
METAL 47 47 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 49 49 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 51 51 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 68 68 Calcium. {ECO:0000250}.
DISULFID 46 137 {ECO:0000250}.
DISULFID 48 64 {ECO:0000250}.
DISULFID 63 117 {ECO:0000250}.
DISULFID 70 110 {ECO:0000250}.
DISULFID 79 103 {ECO:0000250}.
DISULFID 97 108 {ECO:0000250}.
SEQUENCE 137 AA; 15996 MW; B21607EF741FA608 CRC64;
MKRLLTLAWF LACSVPAVPG GLLELKSMIE KVTGKNAVKN YGFYGCYCGW GGHGTPKDGT
DWCCRMHDRC YGLLEEKHCA IRTQSYDYRF TQDLVICEHD SFCPVRLCAC DRKLVYCLRR
NLWSYNRLYQ YYPNFLC


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