VM1BI_BOTMO
ID VM1BI_BOTMO Reviewed; 205 AA.
AC P85314;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Snake venom metalloproteinase BmooMPalpha-I {ECO:0000303|PubMed:18187176, ECO:0000303|PubMed:19706302};
DE Short=SVMP {ECO:0000303|PubMed:18187176, ECO:0000303|PubMed:19706302};
DE EC=3.4.24.-;
OS Bothrops moojeni (Lance-headed viper) (Caissaca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=98334;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-63; 81-172 AND 195-204,
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18187176; DOI=10.1016/j.toxicon.2007.11.017;
RA Bernardes C.P., Santos-Filho N.A., Costa T.R., Gomes M.S.R., Torres F.S.,
RA Costa J., Borges M.H., Richardson M., dos Santos D.M.,
RA de Castro Pimenta A.M., Homsi-Brandeburgo M.I., Soares A.M.,
RA de Oliveira F.;
RT "Isolation and structural characterization of a new fibrin(ogen)olytic
RT metalloproteinase from Bothrops moojeni snake venom.";
RL Toxicon 51:574-584(2008).
RN [2] {ECO:0000312|PDB:3GBO}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 5-204 IN COMPLEX WITH ZINC ION
RP AND CALCIUM ION, IDENTIFICATION BY MASS SPECTROMETRY, METAL BINDING, AND
RP DISULFIDE BONDS.
RX PubMed=19706302; DOI=10.1016/j.toxicon.2009.08.013;
RA Akao P.K., Tonoli C.C., Navarro M.S., Cintra A.C., Neto J.R., Arni R.K.,
RA Murakami M.T.;
RT "Structural studies of BmooMPalpha-I, a non-hemorrhagic metalloproteinase
RT from Bothrops moojeni venom.";
RL Toxicon 55:361-368(2010).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that cleaves the alpha
CC chain of fibrinogen (FGA) first followed by the beta chain (FGB) and
CC shows no effect on the gamma chain. Cleaves only the beta chain of
CC fibrin, leaving the gamma-dimer untouched. Shows proteolytic activity
CC towards azocasein. Causes defibrinogenation when intraperitoneally
CC administered on mice. {ECO:0000269|PubMed:18187176}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P83512};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P83512};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. Not inhibited by the serine
CC proteinase inhibitors aprotinin and benzamidine.
CC {ECO:0000269|PubMed:18187176}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:18187176};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18187176}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18187176}.
CC -!- MASS SPECTROMETRY: Mass=23095; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18187176};
CC -!- MISCELLANEOUS: Is devoid of hemorrhagic, thrombin-like, and
CC phospholipase A2 activities. Has no hemorrhagic activity in mice
CC (PubMed:18187176). {ECO:0000305|PubMed:18187176}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR PDB; 3GBO; X-ray; 1.77 A; A=5-204.
DR PDBsum; 3GBO; -.
DR AlphaFoldDB; P85314; -.
DR SMR; P85314; -.
DR MEROPS; M12.338; -.
DR EvolutionaryTrace; P85314; -.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Fibrinogenolytic toxin; Fibrinolytic toxin; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..205
FT /note="Snake venom metalloproteinase BmooMPalpha-I"
FT /id="PRO_0000312772"
FT DOMAIN 8..204
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 145
FT /evidence="ECO:0000250|UniProtKB:P83512,
FT ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT ProRule:PRU10095"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19706302"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19706302"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19706302"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 119..199
FT /evidence="ECO:0000269|PubMed:19706302,
FT ECO:0007744|PDB:3GBO"
FT DISULFID 159..183
FT /evidence="ECO:0000269|PubMed:19706302,
FT ECO:0007744|PDB:3GBO"
FT DISULFID 161..166
FT /evidence="ECO:0000269|PubMed:19706302,
FT ECO:0007744|PDB:3GBO"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:3GBO"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3GBO"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3GBO"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3GBO"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3GBO"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3GBO"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:3GBO"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3GBO"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:3GBO"
SQ SEQUENCE 205 AA; 23279 MW; B309E96A76F875CE CRC64;
EQQKFSPRYI ELVVVADHGM FKKYNSNLNT IRKWVHEMVN SMNGFYRSVD VTASLANLEV
WSKKDLINVQ KDSRETLKSF GEWRERDLLP RISHDNAQLL TAIVFDGHTI GRAYTGGMCD
PRHSVGVVMD HSPKNLQVAV TMAHELGHNL GMHHDGNQCH CDAASCIMAD SLSVVLSYEF
SDCSQNQYQT YLTKHNPQCI LNEPL
