VM11_BOTMO
ID VM11_BOTMO Reviewed; 200 AA.
AC P0DQT6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Snake venom metalloproteinase BmooMP-I {ECO:0000303|PubMed:32946987};
DE Short=SVMP;
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 PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH
RP ZINC ION, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=32946987; DOI=10.1016/j.biochi.2020.09.001;
RA Salvador G.H.M., Borges R.J., Eulalio M.M.C., Dos Santos L.D.,
RA Fontes M.R.M.;
RT "Biochemical, pharmacological and structural characterization of BmooMP-I,
RT a new P-I metalloproteinase from Bothrops moojeni venom.";
RL Biochimie 179:54-64(2020).
CC -!- FUNCTION: Zinc metalloprotease that displays fibrinogenolytic,
CC gelatinase and weak hemorrhagic activities (PubMed:32946987). Degrades
CC the three chain of fibrinogen Aalpha-chain (FGA), Bbeta-chain (FGB),
CC and gamma (FGG) (PubMed:32946987). {ECO:0000269|PubMed:32946987}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:32946987};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:32946987};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:32946987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32946987}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:32946987}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR PDB; 6X5X; X-ray; 1.92 A; A=1-200.
DR PDBsum; 6X5X; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase 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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Zinc.
FT CHAIN 1..200
FT /note="Snake venom metalloproteinase BmooMP-I"
FT /evidence="ECO:0000269|PubMed:32946987"
FT /id="PRO_0000455524"
FT DOMAIN 5..200
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 8
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT DISULFID 116..195
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT DISULFID 155..179
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT DISULFID 157..162
FT /evidence="ECO:0000269|PubMed:32946987,
FT ECO:0007744|PDB:6X5X"
FT UNSURE 1
FT /note="A OR T"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 24
FT /note="N OR D"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 26
FT /note="N OR D"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 60
FT /note="I OR V"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 71
FT /note="N OR R"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 173
FT /note="T OR V"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 181
FT /note="Q OR E"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 182
FT /note="N OR D"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 183
FT /note="E OR Q"
FT /evidence="ECO:0000305|PubMed:32946987"
FT UNSURE 185
FT /note="Q OR E"
FT /evidence="ECO:0000305|PubMed:32946987"
SQ SEQUENCE 200 AA; 22545 MW; CDA2943DA9DE4DAD CRC64;
AFSPRYIELA VVADNGMFTK YNSNLNTIRT RVHEMVNTVN GFYSSVNANA SLANLQVWSI
KDLIKVEKDS NKTLTSFGEW RERDLLPRIS HDHAQLLTTI VFDNYVIGRS RSGKMCDPEQ
SVGVVRDHSK NNLWVAVTMA HELGHNLDMH HDDTCSCGAK SCIMASVLSK TKSYAFSTCS
QNEYQTFLTK HNPQCILNEP
