VM1_BOTPI
ID VM1_BOTPI Reviewed; 198 AA.
AC P0DL29;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Snake venom metalloproteinase BpirMP;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Alpha-fibrinogenase;
DE AltName: Full=Fibrinolytic metalloproteinase;
DE AltName: Full=Zinc metalloproteinase;
DE Flags: Fragment;
OS Bothrops pirajai (Piraja's lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=113192;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MASS SPECTROMETRY.
RX PubMed=23385358; DOI=10.1016/j.jprot.2013.01.021;
RA Bernardes C.P., Menaldo D.L., Camacho E., Rosa J.C., Escalante T.,
RA Rucavado A., Lomonte B., Gutierrez J.M., Sampaio S.V.;
RT "Proteomic analysis of Bothrops pirajai snake venom and characterization of
RT BpirMP, a new P-I metalloproteinase.";
RL J. Proteomics 80:250-267(2013).
CC -!- FUNCTION: Zinc metalloprotease that preferentially degrades Aalpha
CC chain of fibrinogen (FGA) (at a dose of 5 ug, whereas at a dose of 10
CC ug, both FGA and FGB are completely degraded). Degrades fibrin gel in a
CC dose-dependent manner, as well blood clots formed in vitro
CC (thrombolytic activity). Induces hemorrhage (in the dorsal skin of
CC mice), with an MHD of 50 ug. The basal membrane components collagen
CC (all chains of type IV) (COL4A4), fibronectin (FN1), laminin and
CC nidogen are all degraded by this toxin. {ECO:0000269|PubMed:23385358}.
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 the chelating agents EDTA, EGTA and
CC 1,10-phenanthroline. Is not inhibited by serine proteinase inhibitors
CC aprotinin, leupeptin and benzamidine. {ECO:0000269|PubMed:23385358}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-10.5. {ECO:0000269|PubMed:23385358};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:23385358};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=23140; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23385358};
CC -!- MISCELLANEOUS: Is unable to promote plasma coagulation. Does not
CC degrade gamma chain of fibrinogen (FGG) (PubMed:23385358).
CC {ECO:0000305|PubMed:23385358}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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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; IPR034027; Reprolysin_adamalysin.
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; Fibrinogenolytic toxin;
KW Fibrinolytic toxin; Hemorrhagic toxin; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..198
FT /note="Snake venom metalloproteinase BpirMP"
FT /id="PRO_0000422307"
FT DOMAIN 1..197
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 4
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 112..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 152..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 154..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT UNSURE 3
FT /note="Assigned by comparison with orthologs"
FT UNSURE 16
FT /note="Assigned by comparison with orthologs"
FT UNSURE 21
FT /note="Assigned by comparison with orthologs"
FT UNSURE 24
FT /note="Assigned by comparison with orthologs"
FT UNSURE 46
FT /note="Assigned by comparison with orthologs"
FT UNSURE 48
FT /note="Assigned by comparison with orthologs"
FT UNSURE 51
FT /note="Assigned by comparison with orthologs"
FT UNSURE 56
FT /note="Assigned by comparison with orthologs"
FT UNSURE 59
FT /note="Assigned by comparison with orthologs"
FT UNSURE 60
FT /note="Assigned by comparison with orthologs"
FT UNSURE 63
FT /note="Assigned by comparison with orthologs"
FT UNSURE 64
FT /note="Assigned by comparison with orthologs"
FT UNSURE 70
FT /note="Assigned by comparison with orthologs"
FT UNSURE 71
FT /note="Assigned by comparison with orthologs"
FT UNSURE 81
FT /note="Assigned by comparison with orthologs"
FT UNSURE 82
FT /note="Assigned by comparison with orthologs"
FT UNSURE 85
FT /note="Assigned by comparison with orthologs"
FT UNSURE 91
FT /note="Assigned by comparison with orthologs"
FT UNSURE 92
FT /note="Assigned by comparison with orthologs"
FT UNSURE 93
FT /note="Assigned by comparison with orthologs"
FT UNSURE 96
FT /note="Assigned by comparison with orthologs"
FT UNSURE 100
FT /note="Assigned by comparison with orthologs"
FT UNSURE 101
FT /note="Assigned by comparison with orthologs"
FT UNSURE 103
FT /note="Assigned by comparison with orthologs"
FT UNSURE 108
FT /note="Assigned by comparison with orthologs"
FT UNSURE 127
FT /note="Assigned by comparison with orthologs"
FT UNSURE 129
FT /note="Assigned by comparison with orthologs"
FT UNSURE 130
FT /note="Assigned by comparison with orthologs"
FT UNSURE 139
FT /note="Assigned by comparison with orthologs"
FT UNSURE 143
FT /note="Assigned by comparison with orthologs"
FT UNSURE 151
FT /note="Assigned by comparison with orthologs"
FT UNSURE 176
FT /note="Assigned by comparison with orthologs"
FT UNSURE 192
FT /note="Assigned by comparison with orthologs"
FT UNSURE 193
FT /note="Assigned by comparison with orthologs"
FT UNSURE 194
FT /note="Assigned by comparison with orthologs"
FT UNSURE 195
FT /note="Assigned by comparison with orthologs"
FT NON_TER 1
SQ SEQUENCE 198 AA; 22586 MW; 9B4ACD0D1F749F03 CRC64;
TYIEVAVVAD HRMFKKYNSN LNTIRKWVHE MVNSMNGVYR SMDVHLSLAN LEVWSKKDLI
NVQKDSRETL KSFGEWRERD LLPRISHDNA QLLTAIVFDQ QTIGRAYIGG MCDPRHSVGV
VMDHSKINLQ VAVTMAHELG HNLGMEHDEN QCHCDAPSCV MXXXXXXXXX XXXXXCXXXX
XXXXXTKHNP QCILNEPL
