ID   VM3CR_CROVV             Reviewed;          51 AA.
AC   P0C7N3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like crovidisin;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragments;
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   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=9016825; DOI=10.1006/abbi.1996.9787;
RA   Liu C.-Z., Huang T.-F.;
RT   "Crovidisin, a collagen-binding protein isolated from snake venom of
RT   Crotalus viridis, prevents platelet-collagen interaction.";
RL   Arch. Biochem. Biophys. 337:291-299(1997).
RN   [2]
RP   FUNCTION AS THERAPEUTIC AGENT FOR OCULAR DISORDERS.
RX   PubMed=9395771; DOI=10.1076/ceyr.16.11.1119.5106;
RA   Yang C.-H., Liu C.-Z., Huang T.-F., Yang C.-M., Lui K.-R., Chen M.-S.,
RA   Hung P.-T.;
RT   "Inhibition of RPE cell-mediated matrix adhesion and collagen gel
RT   contraction by crovidisin, a collagen-binding snake venom protein.";
RL   Curr. Eye Res. 16:1119-1126(1997).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=15037024; DOI=10.1016/j.toxicon.2003.10.008;
RA   Tang C.-H., Yang R.-S., Liu C.-Z., Huang T.-F., Fu W.-M.;
RT   "Differential susceptibility of osteosarcoma cells and primary osteoblasts
RT   to cell detachment caused by snake venom metalloproteinase protein.";
RL   Toxicon 43:11-20(2004).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase-disintegrin-like that
CC       blocks the interaction between platelets and collagen fibers through
CC       its binding to collagen fibers, resulting in the blockade of collagen-
CC       mediated platelet functions such as adhesion, release reaction,
CC       thromboxane formation, and aggregation. Binds selectively to collagen
CC       type I with high affinity. Also exerts proteolytic activity to matrix.
CC       {ECO:0000269|PubMed:15037024, ECO:0000269|PubMed:9395771}.
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:0000269|PubMed:9016825}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C7N3; -.
DR   SMR; P0C7N3; -.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Apoptosis; Direct protein sequencing; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>51
FT                   /note="Zinc metalloproteinase-disintegrin-like crovidisin"
FT                   /id="PRO_0000340301"
FT   DOMAIN          <1..>12
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          <13..>18
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         51
SQ   SEQUENCE   51 AA;  5657 MW;  CCF0D898EC268043 CRC64;
     AMVTKNNGDL DKSGTECRLY CKDNSPGQNN SCKMFYSNED EHKGMVLPGT K