VM3B2_BOTJA
ID VM3B2_BOTJA Reviewed; 218 AA.
AC Q0NZX9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like bothrojarin-2;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DEVELOPMENTAL STAGE: This protein seems to be found in newborn
CC B.jararaca venom but not in adult snake venom.
CC {ECO:0000269|PubMed:20146532}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20146532}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {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; DQ375437; ABD34830.1; -; mRNA.
DR AlphaFoldDB; Q0NZX9; -.
DR SMR; Q0NZX9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; 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 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN <1..218
FT /note="Zinc metalloproteinase-disintegrin-like bothrojarin-
FT 2"
FT /id="PRO_0000329984"
FT DOMAIN 14..100
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 78..80
FT /note="D/ECD-tripeptide"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 28..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 30..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 40..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 54..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 59..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 72..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 79..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 104..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 123..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 138..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 151..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 168..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT NON_TER 1
SQ SEQUENCE 218 AA; 24286 MW; BC570203DD855958 CRC64;
RQNRHEASCR IVSPPVCGNE LLEKGEECDC GSPRNCRDPC CDAATCKLHS WVECESGECC
DQCRFIKAGN VCRPQRSECD IAESCTGQSA QCPTDDFHKN GQPCLSNYGY CYNGNCPIMH
HQCYALFGSG AIVAQDGCFK FNDRGDKFFY CRKENVIITP CAQEDVKCGR LFCHTKKSEC
DFDYSEDPDY GMVDHGTKCA DGKVCNSNRQ CVDVTTAY
