PA2AF_TRIST
ID PA2AF_TRIST Reviewed; 138 AA.
AC Q6H3C8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Acidic phospholipase A2 Ts-A6;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=CTs-A6;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-39, FUNCTION, AND MASS
RP SPECTROMETRY.
RC STRAIN=Chinese, and Taiwan; TISSUE=Venom, and Venom gland;
RX PubMed=12959640; DOI=10.1042/bj20030818;
RA Tsai I.-H., Wang Y.-M., Chen Y.-H., Tsai T.-S., Tu M.-C.;
RT "Venom phospholipases A2 of bamboo viper (Trimeresurus stejnegeri):
RT molecular characterization, geographic variations and evidence of multiple
RT ancestries.";
RL Biochem. J. 377:215-223(2004).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows a moderate
CC inhibition of ADP-induced human platelet aggregation when tested on
CC platelet rich plasma. Exhibits high hydrolytic activities and prefers
CC the anionic micelles (dPPC with deoxycholate) to the zwitterionic
CC micelles (dPPC with Triton X-100). PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:12959640}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13939; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12959640};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:12959640, T.stejnegeri was formerly named
CC T.gramineus, supposing that this protein is the same as PLA-VI from
CC T.gramineus. They have been kept separated, because T.gramineus and
CC T.stejnegeri are considered as being two different species (see
CC http://reptile-database.org). {ECO:0000305}.
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DR EMBL; AY211941; AAP48899.1; -; mRNA.
DR AlphaFoldDB; Q6H3C8; -.
DR SMR; Q6H3C8; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12959640"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 Ts-A6"
FT /id="PRO_0000419070"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..138
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15707 MW; 45D3F960A246BDE1 CRC64;
MRALWIMAVL LLGVEGHLMQ FENMIKKVTG RSGIWWYGSY GCYCGKGGQG LPQDASDRCC
FVHDCCYGKV NGCDPKDDFY VYSSENRDIV CGEDNPCTKE ICECDKAAAI CFRDNMDTYQ
NKYWFYPSSN CNEESEPC
