VM2JR_BOTJA
ID VM2JR_BOTJA Reviewed; 156 AA.
AC Q0NZX6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Zinc metalloproteinase-disintegrin jararin;
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: Snake venom zinc metalloproteinase that inhibits ADP-induced
CC platelet aggregation (probably by binding integrin alpha-IIb/beta-3
CC (ITGA2B/ITGB3)) and degrades fibrinogen. {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-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Asn-18 is present instead of the conserved His which is
CC expected to be zinc-binding residue. There is therefore some
CC uncertainty concerning the enzymatic activity of this protein.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ375440; ABD34833.1; -; mRNA.
DR AlphaFoldDB; Q0NZX6; -.
DR SMR; Q0NZX6; -.
DR MEROPS; M12.313; -.
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 Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc;
KW Zymogen.
FT CHAIN <1..156
FT /note="Zinc metalloproteinase-disintegrin jararin"
FT /id="PRO_0000329980"
FT DOMAIN <1..67
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 75..156
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..139
FT /note="Cell attachment site"
FT ACT_SITE 9
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 23..47
FT /evidence="ECO:0000250"
FT DISULFID 25..30
FT /evidence="ECO:0000250"
FT DISULFID 78..97
FT /evidence="ECO:0000255"
FT DISULFID 89..107
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
FT DISULFID 101..124
FT /evidence="ECO:0000250"
FT DISULFID 115..121
FT /evidence="ECO:0000250"
FT DISULFID 120..145
FT /evidence="ECO:0000250"
FT DISULFID 133..152
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 156 AA; 16835 MW; F87B1557D027E844 CRC64;
FVANRMAHEL GHNLGIDNDR DSCSCGANSC IMSATVSNEP SSRFSDCSLN QYSSDLINYY
GCLLNEPLRT DIVSPPFCGN YYPEVGEDCD CGPPANCQNP CCDAATCKLT TGSQCAEGLC
CDQCKFIKAR QICRKGRGDN PDDRCTGQSG DCPRNS
