ID   VM1_CROMM               Reviewed;         414 AA.
AC   Q8JJ51;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
OS   Crotalus molossus molossus (Northern black-tailed rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=31151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Dagda R.K., Gasanov S.E., Rael E.D.;
RT   "Molecular cloning and DNA sequence analysis of four metalloproteinase
RT   cDNAs from Northern blacktailed rattlesnake (Crotalus molossus molossus).";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF378289; AAM27041.1; -; mRNA.
DR   AlphaFoldDB; Q8JJ51; -.
DR   SMR; Q8JJ51; -.
DR   MEROPS; M12.150; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Pyrrolidone carboxylic acid;
KW   Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..190
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000408030"
FT   CHAIN           191..393
FT                   /note="Snake venom metalloproteinase"
FT                   /id="PRO_5000060572"
FT   PROPEP          394..414
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000408031"
FT   DOMAIN          197..393
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         191
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..388
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        348..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   414 AA;  46908 MW;  08C746681BC55085 CRC64;
     MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYELK
     VNGEPVVLHL EKNKELFSKD YSETHYSPDG RKITTNPSVE DHCYYRGRIE NDADSTASIS
     ACNGLKGHFK LQGEMYLIEP LVLSDSEAHA VFKLENVEKE DGGPKMCGVT QNWESYEPIK
     KASDLNFNSD QQRFAKRYVE LVIVADHRMF MKYKSDLFSI CSRVHDIVNF INWFYRSLNI
     RVSLTDLGIW SDQDYITVQS SAENTLHSFG EWGKSVLLKQ KRHDNAQLLT AIVLDEDTLG
     LAYLSSMCNP WTSVEIIQDH SPINLLMGVT MAHELGHNLG MKHDEKDCLR GATLCIMRPG
     LTPGRSYEFS DDSMGYYQSF LDQYKPQCIL NKPLRIDPVS TPVSGNELLE AGEE