VM2V2_CROVV
ID VM2V2_CROVV Reviewed; 478 AA.
AC C9E1R9; H6WCH5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Zinc metalloproteinase/disintegrin VMP-II;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin viridistatin-2;
DE AltName: Full=Disintegrin beta subunit;
DE Flags: Precursor;
OS Crotalus viridis viridis (Prairie rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8742;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 406-478, AND FUNCTION (DISINTEGRIN).
RC TISSUE=Venom gland;
RX PubMed=22465495; DOI=10.1016/j.toxicon.2012.03.011;
RA Lucena S.E., Jia Y., Soto J.G., Parral J., Cantu E., Brannon J.,
RA Lardner K., Ramos C.J., Seoane A.I., Sanchez E.E.;
RT "Anti-invasive and anti-adhesive activities of a recombinant disintegrin,
RT r-viridistatin 2, derived from the Prairie rattlesnake (Crotalus viridis
RT viridis).";
RL Toxicon 60:31-39(2012).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin viridistatin-2]: This recombinant protein
CC inhibits ADP-induced platelet aggregation in whole human blood and this
CC effect is concentration-dependent with an IC(50) of 34 nM.
CC {ECO:0000269|PubMed:22465495}.
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: Heterodimer; disulfide-linked (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR EMBL; GQ451440; ACV83934.1; -; mRNA.
DR EMBL; JQ071899; AEY81222.1; -; mRNA.
DR AlphaFoldDB; C9E1R9; -.
DR SMR; C9E1R9; -.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond;
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..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000407406"
FT CHAIN 191..393
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000407407"
FT PROPEP 394..405
FT /evidence="ECO:0000250"
FT /id="PRO_0000407408"
FT CHAIN 406..478
FT /note="Disintegrin viridistatin-2"
FT /id="PRO_0000407409"
FT DOMAIN 197..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 414..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 456..458
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 308..388
FT /evidence="ECO:0000250"
FT DISULFID 348..372
FT /evidence="ECO:0000250"
FT DISULFID 350..355
FT /evidence="ECO:0000250"
FT DISULFID 420..443
FT /evidence="ECO:0000250"
FT DISULFID 421
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 426
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 434..440
FT /evidence="ECO:0000250"
FT DISULFID 439..464
FT /evidence="ECO:0000250"
FT DISULFID 452..471
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 53814 MW; 86327C050C52BC53 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGELYLIEP LKFPDSEAHA VFKYENVEKE DNAPKMCGVT QNWKSYEPIK
KASQLNLTPE QQRFPQRYIE LVIVADHRMF TKYNSNLNTI RIWVHEIVNT INVFYRSLHI
VVSLTDLEIW SNQDQINVQS AAADTLEAFG EWRETVLLNR ISHDNAQLLT AINFQGNIIG
RAYTGSMCDP RKSVGIITDH SAINLWVAVT MAHELAHNLG ISHDGNQCHC DANSCIMSEE
LSEELSFEFS DCSLNQYQTY LTDHNPQCML NEPLGTDTVS RNELLEAGEE CDCGSPANPC
CDAATCKLRP GAQCAEGLCC DQCRFIKKGK ICRRARGDNP DDRCTGQSAD CPRNRFHA
