ID PA21B_CANFA Reviewed; 146 AA. AC P06596; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 04-NOV-2008, entry version 74. 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 Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; 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=90306027; PubMed=2142076; RA Kerfelec B., Laforge K.S., Vasiloudes P., Puigserver A., Scheele G.A.; RT "Isolation and sequence of the canine pancreatic phospholipase A2 RT gene."; RL Eur. J. Biochem. 190:299-304(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87175472; PubMed=3562437; RA Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A.; RT "Primary structures of canine pancreatic lipase and phospholipase A2 RT messenger RNAs."; RL Pancreas 1:430-437(1986). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00035; BAA00023.1; -; mRNA. DR EMBL; M35301; AAA30883.1; -; mRNA. DR PIR; S11316; PSDG. DR RefSeq; NP_001003320.1; -. DR UniGene; Cfa.40293; -. DR HSSP; P00592; 1HN4. DR Ensembl; ENSCAFG00000010263; Canis familiaris. DR GeneID; 404011; -. DR KEGG; cfa:404011; -. DR HOVERGEN; P06596; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. 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 2: Evidence at transcript level; KW Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted; KW Signal. FT SIGNAL 1 15 FT PROPEP 16 22 FT /FTId=PRO_0000022733. FT CHAIN 23 146 Phospholipase A2. FT /FTId=PRO_0000022734. FT ACT_SITE 70 70 By similarity. FT ACT_SITE 121 121 By similarity. 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; 16236 MW; F6258ED9527F3692 CRC64; MKFLVLAALL TVAAAEGGIS PRAVWQFRNM IKCTIPESDP LKDYNDYGCY CGLGGSGTPV DELDKCCQTH DHCYSEAKKL DSCKFLLDNP YTKIYSYSCS GSEITCSSKN KDCQAFICNC DRSAAICFSK APYNKEHKNL DTKKYC //