ID   VM3B4_BOTJA             Reviewed;          97 AA.
AC   Q0NZX7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like bothrojarin-4;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragment;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16919699; DOI=10.1016/j.toxicon.2006.07.010;
RA   Cidade D.A.P., Wermelinger L.S., Lobo-Hajdu G., Davila A.M.R., Bon C.,
RA   Zingali R.B., Albano R.M.;
RT   "Molecular diversity of disintegrin-like domains within metalloproteinase
RT   precursors of Bothrops jararaca.";
RL   Toxicon 48:590-599(2006).
CC   -!- FUNCTION: The hemorrhagic metalloproteinase-disintegrin-like
CC       bothrojarin-1 is a potent inhibitor of collagen-induced platelet
CC       aggregation by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. It
CC       does not present any fibrinogen-clotting activity (By similarity).
CC       {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-III
CC       subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR   EMBL; DQ375439; ABD34832.1; -; mRNA.
DR   AlphaFoldDB; Q0NZX7; -.
DR   SMR; Q0NZX7; -.
DR   PRIDE; Q0NZX7; -.
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.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc;
KW   Zymogen.
FT   CHAIN           <1..>97
FT                   /note="Zinc metalloproteinase-disintegrin-like bothrojarin-
FT                   4"
FT                   /id="PRO_0000329986"
FT   DOMAIN          4..90
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           68..70
FT                   /note="D/ECD-tripeptide; atypical (KCD)"
FT   BINDING         6
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        18..31
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        30..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        44..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        49..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        62..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   NON_TER         1
FT   NON_TER         97
SQ   SEQUENCE   97 AA;  10531 MW;  3F90076C25C7C47F CRC64;
     IVSPPVCGNY FVEVGEECDC GLPRNCQNQC CNATTCKLIP GAQCEDGECC ERCQFKGAGN
     VCRPRRSKCD IAESCTGQSP DCPTDRFRRN GVSCLNN