VM2J2_BOTJA
ID VM2J2_BOTJA Reviewed; 477 AA.
AC Q98SP2; Q9PS47;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase jararafibrase-2 {ECO:0000303|PubMed:1523677};
DE Short=SVMP {ECO:0000303|PubMed:15737609};
DE EC=3.4.24.- {ECO:0000269|PubMed:8087204};
DE AltName: Full=Jararafibrase II {ECO:0000303|PubMed:1523677};
DE Contains:
DE RecName: Full=Disintegrin bothrostatin {ECO:0000303|PubMed:15737609};
DE Short=D-BTT {ECO:0000303|PubMed:15737609};
DE Flags: Precursor;
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], FUNCTION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom gland;
RX PubMed=15737609; DOI=10.1016/j.bbrc.2005.01.148;
RA Fernandez J.H., Silva C.A., Assakura M.T., Camargo A.C.M., Serrano S.M.T.;
RT "Molecular cloning, functional expression, and molecular modeling of
RT bothrostatin, a new highly active disintegrin from Bothrops jararaca
RT venom.";
RL Biochem. Biophys. Res. Commun. 329:457-464(2005).
RN [2]
RP PROTEIN SEQUENCE OF 188-236, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=1523677; DOI=10.1016/0041-0101(92)90383-g;
RA Maruyama M., Sugiki M., Yoshida E., Mihara H., Nakajima N.;
RT "Purification and characterization of two fibrinolytic enzymes from
RT Bothrops jararaca (jararaca) venom.";
RL Toxicon 30:853-864(1992).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=8087204; DOI=10.1159/000468668;
RA Maruyama M., Tanigawa M., Sugiki M., Yoshida E., Mihara H.;
RT "Purification and characterization of low molecular weight
RT fibrinolytic/hemorrhagic enzymes from snake (Bothrops jararaca) venom.";
RL Enzyme Protein 47:124-135(1993).
CC -!- FUNCTION: [Snake venom metalloproteinase jararafibrase-2]: Impairs
CC hemostasis in the envenomed animal (By similarity). Does not exhibit
CC detectable plasminogen activating activity. Has hemagglutinating
CC activity on red blood cells. Cleaves insulin B chain at '38-Ala-|-Leu-
CC 39' and '40-Tyr-|-Leu-41' bonds (PubMed:8087204). {ECO:0000250,
CC ECO:0000269|PubMed:1523677, ECO:0000269|PubMed:15737609,
CC ECO:0000269|PubMed:8087204}.
CC -!- FUNCTION: [Disintegrin bothrostatin]: This recombinant protein shows
CC high inhibitory activity on collagen-induced platelet aggregation.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline and EDTA.
CC {ECO:0000269|PubMed:1523677}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1523677}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AF345931; AAK15542.1; -; mRNA.
DR PIR; A42766; A42766.
DR AlphaFoldDB; Q98SP2; -.
DR SMR; Q98SP2; -.
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 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 InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /evidence="ECO:0000269|PubMed:1523677"
FT /id="PRO_0000326423"
FT CHAIN 188..389
FT /note="Snake venom metalloproteinase jararafibrase-2"
FT /id="PRO_0000326424"
FT PROPEP 390..404
FT /evidence="ECO:0000250"
FT /id="PRO_0000326425"
FT CHAIN 405..477
FT /note="Disintegrin bothrostatin"
FT /id="PRO_0000326426"
FT DOMAIN 193..389
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 396..477
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 455..457
FT /note="Cell attachment site"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 304..384
FT /evidence="ECO:0000250"
FT DISULFID 344..368
FT /evidence="ECO:0000250"
FT DISULFID 346..351
FT /evidence="ECO:0000250"
FT DISULFID 410..419
FT /evidence="ECO:0000250"
FT DISULFID 412..420
FT /evidence="ECO:0000250"
FT DISULFID 425..439
FT /evidence="ECO:0000250"
FT DISULFID 433..463
FT /evidence="ECO:0000250"
FT DISULFID 438..442
FT /evidence="ECO:0000250"
FT DISULFID 451..470
FT /evidence="ECO:0000250"
FT CONFLICT 188
FT /note="T -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 53440 MW; AC973EE7767E10B3 CRC64;
MIEVLLVTIC LAAFPYQGSS IILESGNVND YEVIYPRKVT ALPKGAVQPK YEDAMQYELK
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG RKITTNPPVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VFKFENVEKE DEAPKMCGVT QNWESYEPIK
KASQSNLTPE HQRYIELFLV VDHGMFMKYN GNSDKIRRRI HQMVNIMKEA YRYLYIDIAL
TGVEIWSNKD MINVQPAAPQ TLDSFGEWRK TDLLNRKSHD NAQLLTSTDF KDQTIGLAYW
GSMCDPKRST AVIEDHSETD LLVAVTMAHE LGHNLGIRHD TGSCSCGGYS CIMAPVISHD
IAKYFSDCSY IQCWDFIMKD NPQCILNKQL RTDTVSTPVS GKNFGAGEEC DCGTPGNPCC
DAVTCKLRPG AQCAEGLCCD QCRFMKEGTV CRRARGDDMD DYCNGISAGC PRNPFHA
