VM3B1_BOTJR
ID VM3B1_BOTJR Reviewed; 547 AA.
AC Q1PHZ4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like BjussuMP-1;
DE EC=3.4.24.-;
DE AltName: Full=BjussuMP-I;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor; Fragment;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15246772; DOI=10.1016/j.toxicon.2004.06.002;
RA Mazzi M.V., Marcussi S., Carlos G.B., Stabeli R.G., Franco J.J.,
RA Ticli F.K., Cintra A.C.O., Franca S.C., Soares A.M., Sampaio S.V.;
RT "A new hemorrhagic metalloprotease from Bothrops jararacussu snake venom:
RT isolation and biochemical characterization.";
RL Toxicon 44:215-223(2004).
RN [2]
RP FUNCTION, PROTEIN SEQUENCE OF 134-154, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=17081786; DOI=10.1016/j.jmgm.2006.09.010;
RA Mazzi M.V., Magro A.J., Amui S.F., Oliveira C.Z., Ticli F.K., Stabeli R.G.,
RA Fuly A.L., Rosa J.C., Braz A.S.K., Fontes M.R.M., Sampaio S.V.,
RA Soares A.M.;
RT "Molecular characterization and phylogenetic analysis of BjussuMP-I: a RGD-
RT P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake
RT venom.";
RL J. Mol. Graph. Model. 26:69-85(2007).
CC -!- FUNCTION: This protein is a zinc metalloprotease from snake venom that
CC causes hemorrhage in mice after intradermal injection. It inhibits
CC platelet aggregation induced by collagen and ADP. Has moderate edema
CC activity, but no myotoxic activity. It hydrolyzes the Aalpha-chain and
CC more slowly the Bbeta-chain of fibrinogen, without affecting the gamma-
CC chains. It also shows proteolytic activity on casein. It is unable to
CC clot plasma. It also shows bactericidal activity against E.coli and
CC S.aureus. {ECO:0000269|PubMed:15246772, ECO:0000269|PubMed:17081786}.
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: Completely inhibited by EDTA, EGTA, 1,10-
CC phenanthroline, and partially by beta-mercaptoethanol. Is not inhibited
CC by aprotinin and leupeptin. {ECO:0000269|PubMed:15246772}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-8.0. {ECO:0000269|PubMed:15246772};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15246772};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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}.
CC -!- CAUTION: The motif D/ECD-tripeptide is missing. {ECO:0000305}.
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DR EMBL; DQ408681; ABD73129.1; -; mRNA.
DR AlphaFoldDB; Q1PHZ4; -.
DR SMR; Q1PHZ4; -.
DR MEROPS; M12.338; -.
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:0042742; P:defense response to bacterium; 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; IPR006586; ADAM_Cys-rich.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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 Antibiotic; Antimicrobial; Calcium; Cell adhesion impairing toxin;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..133
FT /evidence="ECO:0000269|PubMed:17081786"
FT /id="PRO_0000329987"
FT CHAIN 134..547
FT /note="Zinc metalloproteinase-disintegrin-like BjussuMP-1"
FT /id="PRO_0000329988"
FT DOMAIN 141..337
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 339..421
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 252..332
FT /evidence="ECO:0000250"
FT DISULFID 292..316
FT /evidence="ECO:0000250"
FT DISULFID 294..299
FT /evidence="ECO:0000250"
FT DISULFID 353..363
FT /evidence="ECO:0000250"
FT DISULFID 362..385
FT /evidence="ECO:0000250"
FT DISULFID 376..382
FT /evidence="ECO:0000250"
FT DISULFID 381..406
FT /evidence="ECO:0000250"
FT DISULFID 394..413
FT /evidence="ECO:0000250"
FT DISULFID 425..437
FT /evidence="ECO:0000250"
FT DISULFID 444..494
FT /evidence="ECO:0000250"
FT DISULFID 459..501
FT /evidence="ECO:0000250"
FT DISULFID 472..482
FT /evidence="ECO:0000250"
FT DISULFID 489..526
FT /evidence="ECO:0000250"
FT DISULFID 520..531
FT /evidence="ECO:0000250"
FT CONFLICT 149
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="M -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 547 AA; 61985 MW; 091A61487B7CD0ED CRC64;
EFKVNGEPVV LHLEKNKGLF SEDYSETHYS PDGRQITTYP PVEDHCYYHG RIENDADSTA
SISACNGLKG HFKLQGETYL IEPLKLSDSE AHAVYKYENV EKEDEAPKMC GVTETNWEYE
EPIKKASKLV VTAEQQKFPY RYVEIVVVVD RRMVTKYNGD LKKIRKWVYE LVNIVNNIYR
SLNVHVALVG LEIWSKGDKI TVQPDSDYTL NSFGEWRERD LLPRKKHDNA QLLTAVVFDG
PTIGRAYIAG MCDPRHSVGV VMDHSKENLQ VAVTMAHELG HNLGMEHDEN QCHCDAPSCV
MASVLSVVLS YEFSDCSQNQ YQTYLTKHNP QCILNEPLLT VSGNELLEAG EECDCGAPEN
PCCDAATCKL RPGAQCAEGL CCDQCRFKGA GKICRRARGD NPDDRCTGQS ADCPRNRFHR
NGQPCLYNHG YCYNGKCPIM FYQCYFLFGS NATVAEDDCF NNNKKGDKYF YCRKENEKYI
PCAQEDVKCG RLFCDNKKYP CHYNYSEDLD FGMVDHGTKC ADGKVCSNRQ CVDVNEAYKS
TTVFSLI
