VM2_TRIST
ID VM2_TRIST Reviewed; 484 AA.
AC P0DM87;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Zinc metalloproteinase-disintegrin stejnitin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
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], PYROGLUTAMATE FORMATION AT GLN-193,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17403531; DOI=10.1016/j.toxicon.2006.11.030;
RA Han Y.P., Lu X.Y., Wang X.F., Xu J.;
RT "Isolation and characterization of a novel P-II class snake venom
RT metalloproteinase from Trimeresurus stejnegeri.";
RL Toxicon 49:889-898(2007).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced
CC platelet aggregation in human platelet-rich plasma (IC(50) is 175 nM)
CC and cleaves alpha-(FGA) and subsequently the beta-chain (FGG) of bovine
CC fibrinogen, leaving the gamma-chain unaffected. It is also able to
CC inhibit proliferatin of ECV304 cells by inducing apoptosis of these
CC cells. {ECO:0000269|PubMed:17403531}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17403531}.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein does not undergo proteolytic processing to
CC release the disintegrin domain. {ECO:0000305}.
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DR AlphaFoldDB; P0DM87; -.
DR SMR; P0DM87; -.
DR PRIDE; P0DM87; -.
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.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..192
FT /evidence="ECO:0000250"
FT /id="PRO_0000424617"
FT CHAIN 193..484
FT /note="Zinc metalloproteinase-disintegrin stejnitin"
FT /id="PRO_0000424618"
FT DOMAIN 194..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..484
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 462..464
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:17403531"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 305..387
FT /evidence="ECO:0000250"
FT DISULFID 345..369
FT /evidence="ECO:0000250"
FT DISULFID 347..352
FT /evidence="ECO:0000250"
FT DISULFID 403..422
FT /evidence="ECO:0000255"
FT DISULFID 414..432
FT /evidence="ECO:0000250"
FT DISULFID 416..427
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 440..446
FT /evidence="ECO:0000250"
FT DISULFID 445..470
FT /evidence="ECO:0000250"
FT DISULFID 458..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 484 AA; 54436 MW; 277A659A7EA79682 CRC64;
MIQVLLVTIC LAVFPYQGNS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIQ NDADLTASIS
ACNGLKGYFK LQGETYLIEP LKLPDSEAHA VFKYENVEKE DEAPKMCGVT ETNWESDEPI
KKASQLNLTP DEQRFIELVI VADHRMYTKY DGDETEISSK IYEIANDLNV IFRALYIHVA
LIGLEIWPSG ELCNVTLSAD DTLDSFAEWT KRDLQKRKRH DNAQLLTGMI FNEKIEGRAY
KKTMCHWKRS VGIVRDHRTR PHFVANRMAH GLGHNLGINH DGDSCTCGAN SCIMSATVSN
DPSSRFSDCS LNQYSSDIIH NPYTSRCLYN GPWKTDIVSP PVCGNYYVEV GEDCDCGPPA
NCQNRCCDAA TCRLTPGSQC AEGLCCEQCR FSTEGKLCRE AKGDWNNDYC SGQSGDCPRN
PFRA
