ID   PA21B_RAT               Reviewed;         146 AA.
AC   P04055;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   04-NOV-2008, entry version 72.
DE   RecName: Full=Phospholipase A2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Group IB phospholipase A2;
DE   Flags: Precursor;
GN   Name=Pla2g1b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86223862; PubMed=3754861;
RA   Ohara O., Tamaki M., Nakamura E., Tsuruta Y., Fujii Y., Shin M.,
RA   Teraoka H., Okamoto M.;
RT   "Dog and rat pancreatic phospholipases A2: complete amino acid
RT   sequences deduced from complementary DNAs.";
RL   J. Biochem. 99:733-739(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89076874; PubMed=2909239; DOI=10.1016/0167-4781(89)90141-3;
RA   Sakata T., Nakamura E., Tsuruta Y., Tamaki M., Teraoka H., Tojo H.,
RA   Ono T., Okamoto M.;
RT   "Presence of pancreatic-type phospholipase A2 mRNA in rat gastric
RT   mucosa and lung.";
RL   Biochim. Biophys. Acta 1007:124-126(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-54.
RX   MEDLINE=85054750; PubMed=6501264;
RA   Ono T., Tojo H., Inoue K., Kagamiyama H., Yamano T., Okamoto M.;
RT   "Rat pancreatic phospholipase A2: purification, characterization, and
RT   N-terminal amino acid sequence.";
RL   J. Biochem. 96:785-792(1984).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
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DR   EMBL; D00036; BAA00024.1; -; mRNA.
DR   PIR; A92008; PSRT.
DR   RefSeq; NP_113773.1; -.
DR   UniGene; Rn.4283; -.
DR   HSSP; P00593; 4BP2.
DR   Ensembl; ENSRNOG00000001153; Rattus norvegicus.
DR   GeneID; 29526; -.
DR   KEGG; rno:29526; -.
DR   RGD; 61949; Pla2g1b.
DR   HOVERGEN; P04055; -.
DR   NextBio; 609488; -.
DR   ArrayExpress; P04055; -.
DR   GermOnline; ENSRNOG00000001153; Rattus norvegicus.
DR   GO; GO:0043498; F:cell surface binding; IDA:UniProtKB.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0015758; P:glucose transport; ISS:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR   InterPro; IPR016090; Phospholipase_A2.
DR   InterPro; IPR013090; Phospholipase_A2_AS.
DR   InterPro; IPR001211; Phospholipase_A2_euk.
DR   Gene3D; G3DSA:1.20.90.10; Phospholipase_A2; 1.
DR   PANTHER; PTHR11716; Phospholipase_A2; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   ProDom; PD000303; PhospholipaseA2; 1.
DR   SMART; SM00085; PA2c; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Metal-binding; Secreted; Signal.
FT   SIGNAL        1     15
FT   PROPEP       16     22       Activation peptide.
FT                                /FTId=PRO_0000022747.
FT   CHAIN        23    146       Phospholipase A2.
FT                                /FTId=PRO_0000022748.
FT   ACT_SITE     70     70
FT   ACT_SITE    121    121
FT   METAL        50     50       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        52     52       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        54     54       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        71     71       Calcium (By similarity).
FT   DISULFID     33     99       By similarity.
FT   DISULFID     49    146       By similarity.
FT   DISULFID     51     67       By similarity.
FT   DISULFID     66    127       By similarity.
FT   DISULFID     73    120       By similarity.
FT   DISULFID     83    113       By similarity.
FT   DISULFID    106    118       By similarity.
SQ   SEQUENCE   146 AA;  16424 MW;  7EC4F7A491B913D0 CRC64;
     MKLLLLAALL TAGVTAHSIS TRAVWQFRNM IKCTIPGSDP LREYNNYGCY CGLGGSGTPV
     DDLDRCCQTH DHCYNQAKKL ESCKFLIDNP YTNTYSYKCS GNVITCSDKN NDCESFICNC
     DRQAAICFSK VPYNKEYKDL DTKKHC
//