PA2B_TRIGS
ID PA2B_TRIGS Reviewed; 136 AA.
AC A8E2V9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Basic phospholipase A2 Tgc-K49;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Trimeresurus gracilis (Kikuchi habu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=109781;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=22115990; DOI=10.1016/j.toxicon.2011.10.016;
RA Tsai I.-H., Tsai T.-S., Wang Y.-M., Tu M.-C., Chang H.-C.;
RT "Cloning and characterization of Trimeresurus gracilis venom phospholipases
RT A(2): comparison with Ovophis okinavensis venom and the systematic
RT implications.";
RL Toxicon 59:151-157(2012).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC K49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein is not found in the crude venom.
CC {ECO:0000305|PubMed:22115990}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY764142; AAW92122.1; -; mRNA.
DR AlphaFoldDB; A8E2V9; -.
DR SMR; A8E2V9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
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 Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism; Secreted;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000250"
FT CHAIN 16..136
FT /note="Basic phospholipase A2 Tgc-K49"
FT /id="PRO_0000419054"
FT ACT_SITE 62
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT DISULFID 41..130
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 43..59
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 58..110
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 64..136
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 65..103
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 72..96
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 90..101
FT /evidence="ECO:0000250|UniProtKB:Q90249"
SQ SEQUENCE 136 AA; 15508 MW; 91E49886F5F5AF16 CRC64;
MRTLWIVAVL LVGEGSLIQL WEMIFQEMGK GAAKKYGLYG CNCGMGHRGR PVDATDRCCS
VHKCCYKKLT DCDPKTDRYS YSWENGAIVC GGDDPCRKEV CECDKATTIC FRDNLDTYDK
KYKIYLKFLC KKPEPC
