VM3B1_BOTJA
ID VM3B1_BOTJA Reviewed; 166 AA.
AC Q0NZY0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like bothrojarin-1;
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; DQ375436; ABD34829.1; -; mRNA.
DR AlphaFoldDB; Q0NZY0; -.
DR SMR; Q0NZY0; -.
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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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..>166
FT /note="Zinc metalloproteinase-disintegrin-like bothrojarin-
FT 1"
FT /id="PRO_0000329983"
FT DOMAIN 5..91
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 69..71
FT /note="D/ECD-tripeptide"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 8..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 19..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 21..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 31..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 45..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 50..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 63..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 70..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 95..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 114..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 142..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT NON_TER 1
FT NON_TER 166
SQ SEQUENCE 166 AA; 17951 MW; 40885BC7ECA3069F CRC64;
DIVSPPVCGN YFVEVGEECD CGRPGKCQNP CCNATTCKLT PGSQCADGLC CDQCRFKGAG
TECRAARSEC DIAESCTGQS PECPTDDFQR NGQPCLNNQG YCYNGNCPIL DHQCHNLFGA
GATVAPDACF NFNRRGQGIY YCRKQNGVTI PCARKDIKCG RLFCVQ
