VM2B_TRIGA
ID VM2B_TRIGA Reviewed; 73 AA.
AC P17495;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Disintegrin trigramin-beta-2;
DE AltName: Full=Platelet aggregation activation inhibitor;
DE Contains:
DE RecName: Full=Disintegrin trigramin-beta-1;
OS Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=8767;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=2320569; DOI=10.1073/pnas.87.7.2471;
RA Dennis M.S., Henzel W.J., Pitti R.M., Lipari M.T., Napier M.A.,
RA Deisher T.A., Bunting S., Lazarus R.A.;
RT "Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms:
RT evidence for a family of platelet-aggregation inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2471-2475(1990).
CC -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC binding to the alpha-IIb/beta-3 receptor (ITGA2B/ITGB3) on the platelet
CC surface and inhibits aggregation induced by ADP, thrombin, platelet-
CC activating factor and collagen. {ECO:0000269|PubMed:2320569}.
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR PIR; D35982; D35982.
DR AlphaFoldDB; P17495; -.
DR SMR; P17495; -.
DR ELM; P17495; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..73
FT /note="Disintegrin trigramin-beta-2"
FT /id="PRO_0000045889"
FT CHAIN 1..72
FT /note="Disintegrin trigramin-beta-1"
FT /id="PRO_0000045890"
FT DOMAIN 1..73
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 51..53
FT /note="Cell attachment site"
FT DISULFID 6..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 8..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 21..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 29..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 34..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 47..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 73 AA; 7634 MW; E080C4B34367C734 CRC64;
EAGKDCDCGS PANPCCDAAT CKLLPGAQCG EGPCCDQCSF MKKGTICRRA RGDDLDDYCN
GRSAGCPRNP FHA
