VM1B2_BOTJR
ID VM1B2_BOTJR Reviewed; 369 AA.
AC Q7T1T4; A4ZQ21;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Snake venom metalloproteinase BjussuMP-2;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=BOJUMET I;
DE AltName: Full=BjussuMP-II;
DE AltName: Full=Nonhemorrhagic metalloprotease MP-II;
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].
RC TISSUE=Venom gland;
RX PubMed=15134836; DOI=10.1016/j.biochi.2004.02.002;
RA Kashima S., Roberto P.G., Soares A.M., Astolfi-Filho S., Pereira J.O.,
RA Giuliati S., Faria M. Jr., Xavier M.A.S., Fontes M.R.M., Giglio J.R.,
RA Franca S.C.;
RT "Analysis of Bothrops jararacussu venomous gland transcriptome focusing on
RT structural and functional aspects: I -- gene expression profile of highly
RT expressed phospholipases A2.";
RL Biochimie 86:211-219(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-356, PROTEIN SEQUENCE OF 152-171,
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18006118; DOI=10.1016/j.peptides.2007.10.010;
RA Marcussi S., Bernardes C.P., Santos-Filho N.A., Mazzi M.V., Oliveira C.Z.,
RA Izidoro L.F.M., Fuly A.L., Magro A.J., Braz A.S.K., Fontes M.R.M.,
RA Giglio J.R., Soares A.M.;
RT "Molecular and functional characterization of a new non-hemorrhagic
RT metalloprotease from Bothrops jararacussu snake venom with antiplatelet
RT activity.";
RL Peptides 28:2328-2339(2007).
CC -!- FUNCTION: This metalloproteinase displays proteolytic activity on
CC fibrin, fibrinogen, collagen, casein and gelatin. It inhibits ADP- and
CC collagen-induced platelet aggregation and displays a very low edema
CC inducing activity. {ECO:0000269|PubMed:18006118}.
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. Conserves its activity upon fibrinogen when
CC incubated with cobalt, magnesium ions up to 40 mM, but loses the
CC proteolytic activity when incubated with manganese, fer, zinc or
CC calcium ions. {ECO:0000269|PubMed:18006118}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18006118};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18006118}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18006118}.
CC -!- MISCELLANEOUS: Does not induce hemorrhage, myotoxicity and lethality
CC and does not show any clotting or anticoagulant activity on human
CC citrated plasma. {ECO:0000305|PubMed:18006118}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; AY255005; AAP78952.1; -; mRNA.
DR EMBL; EF369492; ABP48735.1; -; mRNA.
DR AlphaFoldDB; Q7T1T4; -.
DR SMR; Q7T1T4; -.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT PROPEP <1..151
FT /evidence="ECO:0000269|PubMed:18006118"
FT /id="PRO_0000409491"
FT CHAIN 152..369
FT /note="Snake venom metalloproteinase BjussuMP-2"
FT /id="PRO_0000329977"
FT DOMAIN 159..355
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 270..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 310..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 312..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CONFLICT 354
FT /note="E -> K (in Ref. 2; ABP48735)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 369 AA; 41957 MW; BA5BD8DB5FF6FA9B CRC64;
TELPKGAVQP KYEDAMQYEF KGNGEPVVLH LEKNKGLFSE DYSETHYSPD GRQIITYPPF
EDHCYYHGRI ENDADSTASI SACNGLKGHF KLQGETYLIE PLKLSDSEAH AVYKYENVEK
EDEAPKMCGV TETNWESYEP IKKASPSNLT PEQQKFSPRY IEVAVVADHR MFKKYNSNLN
TIRKWVHEMV NSMNGVYRSM DVHLSLANLE VWSKKDLINV QKDSRETLKS FGEWRERDLL
PRISHDNAQL LTAVVFDQQT IGRAYIAGMC DPRHSVGVVM DHSKENLQVA VTMAHELGHN
LGMEHDENQC HCDAPSCVMA SVLSVVLSYE FSDCSQNQYQ TYLTKHNPQC ILNEPLLTVS
GNELLEAGE
