ID PA21B_TRIFL Reviewed; 138 AA. AC P06859; Q92118; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 2. DT 04-NOV-2008, entry version 77. DE RecName: Full=Phospholipase A2 isozyme 1; DE EC=3.1.1.4; DE AltName: Full=Phospholipase A2 isozyme I; DE AltName: Full=pgPLA 1a/pgPLA 2a; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase; DE Flags: Precursor; OS Trimeresurus flavoviridis (Habu) (Protobothrops flavoviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Viperidae; Crotalinae; Trimeresurus. OX NCBI_TaxID=88087; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RX MEDLINE=91185340; PubMed=1707052; RA Oda N., Ogawa T., Ohno M., Sasaki H., Sakaki Y., Kihara H.; RT "Cloning and sequence analysis of cDNA for Trimeresurus flavoviridis RT phospholipase A2, and consequent revision of the amino acid RT sequence."; RL J. Biochem. 108:816-821(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME [THR37]PLA2). RC TISSUE=Venom gland; RX MEDLINE=92409555; PubMed=1528861; RA Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y., RA Kihara H., Ohno M.; RT "Unusually high conservation of untranslated sequences in cDNAs for RT Trimeresurus flavoviridis phospholipase A2 isozymes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=93317604; PubMed=8327468; RA Nakashima K., Ogawa T., Oda N., Hattori M., Sakaki Y., Kihara H., RA Ohno M.; RT "Accelerated evolution of Trimeresurus flavoviridis venom gland RT phospholipase A2 isozymes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:5964-5968(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=94369106; PubMed=7765285; RA Nakashima K., Nobuhisa I., Ogawa T., Hattori M., Sakaki Y., Kihara H., RA Ohno M.; RT "Polymorphisms of Trimeresurus flavoviridis venom gland phospholipase RT A2 isozyme genes."; RL Biosci. Biotechnol. Biochem. 58:1510-1511(1994). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Amami-Oshima, and Okinawa; RA Chijiwa T., Yamaguchi Y., Ogawa T., Deshimaru M., Nobuhisa I., RA Nakashima K., Oda-Ueda N., Shimohigashi Y., Fukumaki Y., Hattori S., RA Ohno M.; RT "Regional evolution of Trimeresurus flavoviridis venom-gland RT phospholipase A2 isoenzymes."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 17-138. RC TISSUE=Venom; RX MEDLINE=86168106; PubMed=3514593; RA Tanaka S., Mohri N., Kihara H., Ohno M.; RT "Amino acid sequence of Trimeresurus flavoviridis phospholipase A2."; RL J. Biochem. 99:281-289(1986). RN [7] RP PROTEIN SEQUENCE OF 17-47. RC TISSUE=Venom; RX MEDLINE=87179112; PubMed=3564060; DOI=10.1016/0041-0101(86)90138-8; RA Kini R.M., Kawabata S., Iwanaga S.; RT "Comparison of amino terminal region of three isoenzymes of RT phospholipases A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from Trimeresurus RT flavoviridis (habu snake) venom and the complete amino acid sequence RT of the basic phospholipase, TFV PL-X."; RL Toxicon 24:1117-1129(1986). RN [8] RP ACTIVE SITES. RX MEDLINE=90186681; PubMed=2628422; RA Kohzuma T., Oda N., Kihara H., Ohno M.; RT "Investigation of an active site histidine-aspartate couple in RT Trimeresurus flavoviridis phospholipase A2."; RL J. Biochem. 106:1054-1058(1989). 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 -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II CC subfamily. 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; D10070; BAA00962.1; -; mRNA. DR EMBL; D10720; BAA01563.1; -; mRNA. DR EMBL; D10722; BAA01565.1; -; Genomic_DNA. DR EMBL; D10724; BAA01567.1; -; Genomic_DNA. DR EMBL; AB072174; BAB68547.1; -; mRNA. DR EMBL; AB072175; BAB68548.1; -; mRNA. DR PIR; A46169; A46169. DR PIR; A48188; A48188. DR PIR; B48188; PSTVIF. DR HSSP; P51972; 1VAP. DR SMR; P06859; 18-138. DR HOVERGEN; P06859; -. 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 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; KW Metal-binding; Polymorphism; Secreted; Signal. FT SIGNAL 1 16 FT CHAIN 17 138 Phospholipase A2 isozyme 1. FT /FTId=PRO_0000022952. FT ACT_SITE 63 63 FT ACT_SITE 104 104 FT METAL 43 43 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 45 45 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 47 47 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 64 64 Calcium (By similarity). FT DISULFID 42 131 By similarity. FT DISULFID 44 60 By similarity. FT DISULFID 59 110 By similarity. FT DISULFID 65 138 By similarity. FT DISULFID 66 103 By similarity. FT DISULFID 73 97 By similarity. FT DISULFID 91 101 By similarity. FT VARIANT 15 15 D -> E. FT VARIANT 53 53 K -> T (in isozyme [Thr37]PLA2). FT CONFLICT 85 88 NNGD -> QGN (in Ref. 6; AA sequence). FT CONFLICT 92 92 E -> G (in Ref. 6; AA sequence). FT CONFLICT 95 97 GPC -> DPCD (in Ref. 6; AA sequence). SQ SEQUENCE 138 AA; 15535 MW; FF24B8253FEA1A1A CRC64; MRTLWIMAVL LVGVDGGLWQ FENMIIKVVK KSGILSYSAY GCYCGWGGRG KPKDATDRCC FVHDCCYGKV TGCNPKLGKY TYSWNNGDIV CEGDGPCKEV CECDRAAAIC FRDNLDTYDR NKYWRYPASN CQEDSEPC //