ID   VM1CR_CROAT             Reviewed;          43 AA.
AC   P0DJ42;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Snake venom metalloproteinase crotalin;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Fragments;
OS   Crotalus atrox (Western 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=8730;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=11776320;
RA   Wu W.-B., Peng H.-C., Huang T.-F.;
RT   "Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of
RT   Crotalus atrox.";
RL   Thromb. Haemost. 86:1501-1511(2001).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9473223;
RA   Chang M.-C., Lin H.-K., Peng H.-C., Huang T.-F.;
RT   "Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib
RT   antagonist from venom of Crotalus atrox.";
RL   Blood 91:1582-1589(1998).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ristocin-
CC       induced platelet aggregation by abolishing the binding of von
CC       Willebrand factor (vWF) to platelet glycoprotein Ib alpha (GPIBA)
CC       through the cleavage of both GP1BA and vWF. Also has fibrinogenolytic
CC       activities by degrading the alpha- (FGA) and beta-chain (FGB) of
CC       fibrinogen. In vivo, induces a slight hemorrhage when applied to chick
CC       chorioallantoic membrane and has potent antithrombic effect.
CC       {ECO:0000269|PubMed:11776320, ECO:0000269|PubMed:9473223}.
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: This protein autoproteolytically degrades to 10 kDa and 14 kDa
CC       fragments in the presence of SDS. Interestingly, the two fragments, as
CC       well as reduced crotalin are able to bind vWF, indicating that the
CC       binding activity does not require a specific protein conformation.
CC   -!- MISCELLANEOUS: Does not induce thrombocytopenia after injection into
CC       mice. {ECO:0000305|PubMed:9473223}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: This fragmental protein is 100% identical to atrolysin-B (AC
CC       Q90391) and may be the same protein. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJ42; -.
DR   SMR; P0DJ42; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043655; C:host extracellular space; NAS: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:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR   GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR   GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW   Toxin; Zinc.
FT   CHAIN           <1..43
FT                   /note="Snake venom metalloproteinase crotalin"
FT                   /id="PRO_0000417625"
FT   DOMAIN          <1..43
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        18..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        38..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000305"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   43 AA;  5015 MW;  44E044B32663B3EA CRC64;
     LLRRKSHDHA QNHDGDKCLR GASLGYYQSF LNQYKPQCIL NKP