VM3V_CROVV
ID VM3V_CROVV Reviewed; 177 AA.
AC A2CJE3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like viristiarin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
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=17112685; DOI=10.1016/j.gene.2006.09.020;
RA Soto J.G., White S.A., Reyes S.R., Regalado R., Sanchez E.E., Perez J.C.;
RT "Molecular evolution of PIII-SVMP and RGD disintegrin genes from the genus
RT Crotalus.";
RL Gene 389:66-72(2007).
CC -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ676500; ABG77584.1; -; mRNA.
DR AlphaFoldDB; A2CJE3; -.
DR SMR; A2CJE3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..>177
FT /note="Zinc metalloproteinase-disintegrin-like viristiarin"
FT /id="PRO_0000406577"
FT DOMAIN <1..63
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 41..43
FT /note="D/ECD-tripeptide"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 3..26
FT /evidence="ECO:0000250"
FT DISULFID 17..23
FT /evidence="ECO:0000250"
FT DISULFID 22..48
FT /evidence="ECO:0000250"
FT DISULFID 35..55
FT /evidence="ECO:0000250"
FT DISULFID 42..74
FT /evidence="ECO:0000250"
FT DISULFID 67..79
FT /evidence="ECO:0000250"
FT DISULFID 86..136
FT /evidence="ECO:0000250"
FT DISULFID 101..147
FT /evidence="ECO:0000250"
FT DISULFID 114..124
FT /evidence="ECO:0000250"
FT DISULFID 131..173
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 177
SQ SEQUENCE 177 AA; 19578 MW; A2E3F7D620C8FFDF CRC64;
NPCCDAATCK LKSGSQCGHG DCCEQCKFSK SGTECRASMS ECDPAEHCTG QSSECPADVF
HKNGQPCLDN YGYCYNGNCP IMYHQCYDLF GADVYEAEDS CFERNQKGNY YGYCRKENGN
KIPCAPEDVK CGRLYCKDNS PGQNNPCKMF YSNEDEHKGM VLPGTKCADG KVCSNRQ
