ID   VM3_CROVE               Reviewed;          20 AA.
AC   C0HL97;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like uracoina-1 {ECO:0000305|PubMed:11451438};
DE            EC=3.4.24.- {ECO:0000269|PubMed:11451438};
DE   AltName: Full=Snake venom metalloprotease {ECO:0000250|UniProtKB:O93523};
DE            Short=SVMP {ECO:0000250|UniProtKB:O93523};
DE   Flags: Fragment;
OS   Crotalus vegrandis (Uracoan rattlesnake) (Crotalus durissus vegrandis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184545 {ECO:0000303|PubMed:11451438};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:11451438};
RX   PubMed=11451438; DOI=10.1016/s0167-4838(01)00217-5;
RA   Aguilar I., Giron M.E., Rodriguez-Acosta A.;
RT   "Purification and characterisation of a haemorrhagic fraction from the
RT   venom of the Uracoan rattlesnake Crotalus vegrandis.";
RL   Biochim. Biophys. Acta 1548:57-65(2001).
CC   -!- FUNCTION: Snake venom zinc metalloprotease that possesses hemorrhagic
CC       activity (minimum hemorrhagic dose, MHD=4.7 ug) when injected
CC       intradermally into mice. Degrades the alpha-chain of fibrinogen (FGA).
CC       {ECO:0000269|PubMed:11451438}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O93523};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O93523};
CC   -!- ACTIVITY REGULATION: Inhibited by ethylenediaminetetraacetic acid
CC       (EDTA) and 1,10-phenanthroline. Not inhibited by tosyl-L-lysine
CC       chloromethyl ketone (TCLK) and phenylmethanesulfonylfluoride (PMSF).
CC       {ECO:0000269|PubMed:11451438}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-9. {ECO:0000269|PubMed:11451438};
CC       Temperature dependence:
CC         Activity is stable between 20-40 degrees Celsius, decreases at higher
CC         temperatures and is lost at 70 degrees Celsius.
CC         {ECO:0000269|PubMed:11451438};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11451438}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11451438}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11451438}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HL97; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Fibrinogenolytic toxin; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..>20
FT                   /note="Zinc metalloproteinase-disintegrin-like uracoina-1"
FT                   /evidence="ECO:0000269|PubMed:11451438"
FT                   /id="PRO_0000444119"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:11451438"
SQ   SEQUENCE   20 AA;  2434 MW;  2E05703A5C9E5C7E CRC64;
     HQKYNPFRFV ELVLVVDKAM