ID   VM2A_CROAT              Reviewed;          12 AA.
AC   P0DTB7;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Snake venom metalloproteinase CatroxMP-II {ECO:0000303|PubMed:29761254};
DE            Short=SVMP {ECO:0000303|PubMed:29761254};
DE            EC=3.4.24.- {ECO:0000269|PubMed:29761254};
DE   AltName: Full=Fibrinogenolytic metalloproteinase {ECO:0000303|PubMed:29761254};
DE   Flags: Fragment;
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, FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC   TISSUE=Venom;
RX   PubMed=29761254; DOI=10.1007/s10534-018-0107-5;
RA   Suntravat M., Langlais P.R., Sanchez E.E., Nielsen V.G.;
RT   "CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated
RT   from Crotalus atrox venom.";
RL   BioMetals 31:585-593(2018).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase that cleaves both
CC       alpha- and beta-chains of fibrinogen, but not the gamma-chain
CC       (PubMed:29761254). {ECO:0000269|PubMed:29761254}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:29761254};
CC   -!- ACTIVITY REGULATION: Inhibited by carbon monoxide (CO)
CC       (PubMed:29761254). This inhibition is explained by the presence of heme
CC       attached to the enzyme and modulated by CO (PubMed:29761254). The state
CC       change of heme induced by CO (carboxyheme or metheme) may inhibit the
CC       enzyme (PubMed:29761254). {ECO:0000269|PubMed:29761254}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29761254}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29761254}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000250|UniProtKB:P34182}.
CC   -!- MISCELLANEOUS: This is the first SVMP that is heme-bound and carbon
CC       monoxide-inhibited. The heme-binding may serve to regulate SVMP
CC       activity during envenomation, with both protective and aggressive
CC       purposes. First, if the venom gland is elaborating CO via the enzymatic
CC       action of heme oxygenase, then inhibition of SVMP by CO is likely
CC       important in preventing this enzyme from disrupting the epithelial
CC       barrier of the gland and injuring the snake. Second, given that the
CC       body temperature of snakes tend to be between 20 and 30 degrees
CC       Celsius, the rate of elaboration of CO would not need to be that great
CC       to inhibit the enzymes, as the affinity of CO for heme is at its
CC       highest in this range. Third, when a prey animal is envenomed, CO would
CC       be expected to diffuse from SVMP and bind to the myriad of hemes found
CC       in mitochondrial cytochromes and hemoglobin in red cells perfusing the
CC       bite site. Fourth, in the case of mammalian prey such as rodents with
CC       body temperatures of 36-37 degrees Celsius, it again would be expected
CC       that CO would bind less well to heme-bound SVMP and quickly be
CC       released. Such rapid removal of CO from SVMP would be analogous to
CC       'unsheathing a sword' allowing enzymatic action to start and ultimately
CC       incapacitating the envenomed prey. {ECO:0000305|PubMed:29761254}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..>12
FT                   /note="Snake venom metalloproteinase CatroxMP-II"
FT                   /evidence="ECO:0000305|PubMed:29761254"
FT                   /id="PRO_0000449318"
FT   NON_TER         12
SQ   SEQUENCE   12 AA;  1545 MW;  CE649367F4DB4416 CRC64;
     NPEHQRYVEL FI