VM2_CROAD
ID VM2_CROAD Reviewed; 488 AA.
AC J9Z332;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Zinc metalloproteinase-disintegrin VMP-II;
DE Short=CamVMP-II;
DE EC=3.4.24.-;
DE AltName: Full=Disintegrin r-Cam-dis;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION OF RECOMBINANT DISINTEGRIN.
RC TISSUE=Venom gland;
RX PubMed=23313448; DOI=10.1016/j.toxicon.2012.12.025;
RA Suntravat M., Jia Y., Lucena S.E., Sanchez E.E., Perez J.C.;
RT "cDNA cloning of a snake venom metalloproteinase from the eastern
RT diamondback rattlesnake (Crotalus adamanteus), and the expression of its
RT disintegrin domain with anti-platelet effects.";
RL Toxicon 64:43-54(2013).
CC -!- FUNCTION: Zinc metalloproteinase-disintegrin VMP-II: inhibits ADP-
CC induced platelet aggregation (probably by binding integrin alpha-
CC IIb/beta-3 (ITGA2B/ITGB3)) and degrades fibrinogen. {ECO:0000250}.
CC -!- FUNCTION: Recombinant disintegrin r-Cam-dis (413-488): this recombinant
CC protein inhibits platelet adhesion to fibrinogen (IC(50) is 1 nM),
CC inhibits collagen- (IC(50) is 18 nM) and ADP-induced (IC(50) is 6 nM)
CC platelet aggregation, and also inhibits platelet function on clot
CC retraction. May act by binding integrin alpha-IIb/beta-3
CC (ITGA2B/ITGB3). {ECO:0000269|PubMed:23313448}.
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: Homodimer; disulfide-linked (disintegrin).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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}.
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DR EMBL; JX457344; AFS49715.1; -; mRNA.
DR AlphaFoldDB; J9Z332; -.
DR SMR; J9Z332; -.
DR BRENDA; 3.4.24.1; 1709.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000424623"
FT CHAIN 192..488
FT /note="Zinc metalloproteinase-disintegrin VMP-II"
FT /id="PRO_0000424624"
FT DOMAIN 198..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
FT /note="Cell attachment site"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..391
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 407..426
FT /evidence="ECO:0000255"
FT DISULFID 418..436
FT /evidence="ECO:0000250"
FT DISULFID 420..431
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..474
FT /evidence="ECO:0000250"
FT DISULFID 462..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 54823 MW; A019BE359C3CE72B CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQLK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLSDSEAHA VYKYENVEKE DEASKMCGVT ETNWESYEPI
KKASQSNIPP EEEAFYQRYI ELVVVADHRM YTKYDGDKTE ISSIIYEIVN TLTQIFRPLH
IRVALIGLEI WSSGELSKVT LSADDTLEAF GEWRKTVLMN RKRHDNAQLL TGMIFNETIE
GRTYKSGMCN PKHSVGIVRD YRTRRHFVAN RMAHELGHNL GIDHDRDSCT CGANSCIMSA
TVSNEPSSQF SDCSLNKYLN YIVRYQSTTR CLHNEPSETD IVSPPFCGNY FKEVGEDCDC
GPPANCQNPC CDAATCKLTT GSQCAEGLCC DQCKFTKKGT ACRPARGDWN DDTCTGQSAD
CPRNGLYG
