VM2TA_TRIGA
ID VM2TA_TRIGA Reviewed; 480 AA.
AC P15503;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin trigramin-alpha;
DE AltName: Full=Platelet aggregation activation inhibitor;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=2377470; DOI=10.1093/nar/18.14.4255;
RA Neeper M.P., Jacobson M.A.;
RT "Sequence of a cDNA encoding the platelet aggregation inhibitor
RT trigramin.";
RL Nucleic Acids Res. 18:4255-4255(1990).
RN [2]
RP PROTEIN SEQUENCE OF 408-479.
RC TISSUE=Venom;
RX PubMed=2653425; DOI=10.1021/bi00428a037;
RA Huang T.-F., Holt J.C., Kirby E.P., Niewiarowski S.;
RT "Trigramin: primary structure and its inhibition of von Willebrand factor
RT binding to glycoprotein IIb/IIIa complex on human platelets.";
RL Biochemistry 28:661-666(1989).
RN [3]
RP PROTEIN SEQUENCE OF 408-479.
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).
RN [4]
RP PROTEIN SEQUENCE OF 408-419.
RC TISSUE=Venom;
RX PubMed=3680247; DOI=10.1016/s0021-9258(18)47710-1;
RA Huang T.-F., Holt J.C., Lukasiewicz H., Niewiarowski S.;
RT "Trigramin. A low molecular weight peptide inhibiting fibrinogen
RT interaction with platelet receptors expressed on glycoprotein IIb-IIIa
RT complex.";
RL J. Biol. Chem. 262:16157-16163(1987).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin trigramin-alpha]: Inhibits platelet aggregation
CC induced by ADP, thrombin, platelet-activating factor and collagen. Acts
CC by inhibiting fibrinogen interaction with platelet receptors
CC GPIIb/GPIIIa (ITGA2B/ITGB3).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {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 EMBL; X51530; CAA35910.1; -; mRNA.
DR PIR; S12589; A30065.
DR AlphaFoldDB; P15503; -.
DR SMR; P15503; -.
DR MEROPS; M12.163; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000029006"
FT CHAIN 191..407
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000029007"
FT CHAIN 408..480
FT /note="Disintegrin trigramin-alpha"
FT /id="PRO_0000029008"
FT DOMAIN 197..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 399..480
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 458..460
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..386
FT /evidence="ECO:0000250"
FT DISULFID 348..370
FT /evidence="ECO:0000250"
FT DISULFID 350..353
FT /evidence="ECO:0000250"
FT DISULFID 413..428
FT /evidence="ECO:0000250"
FT DISULFID 415..423
FT /evidence="ECO:0000250"
FT DISULFID 422..445
FT /evidence="ECO:0000250"
FT DISULFID 436..442
FT /evidence="ECO:0000250"
FT DISULFID 441..466
FT /evidence="ECO:0000250"
FT DISULFID 454..473
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 53494 MW; 601415FF3A4E0D50 CRC64;
MIQVLLITIC LAVFPYQGSS IILESGNLND YEVVYPEKVT ALPKGAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSEIHYSPDG REITAYPSVE DHCYYHGRIE NDADSTASIS
ACDGLKGHFK LQGEMYLIEP LELSDSEAHA VFKYENVEKE DEPPKMCGVT QNWESYESTK
KASQLNVTPE QQRFPQRYIK LGIFVDHGMY TKYSGNSERI TKRVHQMINN INMMCRALNI
VTTLSVLEIW SEKDLITVQA SAPTTLTLFG AWRETVLLNR TSHDHAQLLT ATIFNGNVIG
RAPVGGMCDP KRSVAIVRDH NAIVFVVAVT MTHEMGHNLG MHHDEDKCNC NTCIMSKVLS
RQPSKYFSEC SKDYYQTFLT NHNPQCILNA PLRTDTVSTP VSGNELLEAG EDCDCGSPAN
PCCDAATCKL IPGAQCGEGL CCDQCSFIEE GTVCRIARGD DLDDYCNGRS AGCPRNPFHA
