VM3_BOTMO
ID VM3_BOTMO Reviewed; 33 AA.
AC P0DKR0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like moojenin {ECO:0000303|PubMed:22975266};
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase {ECO:0000303|PubMed:22975266};
DE Short=SVMP {ECO:0000303|PubMed:22975266};
DE Contains:
DE RecName: Full=Disintegrin-like {ECO:0000303|PubMed:22975266};
DE Flags: Fragment;
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, FUNCTION, BIOASSAY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=22975266; DOI=10.1016/j.toxicon.2012.08.017;
RA de Morais N.C., Neves Mamede C.C., Fonseca K.C., de Queiroz M.R.,
RA Gomes-Filho S.A., Santos-Filho N.A., Bordon K.D., Beletti M.E.,
RA Sampaio S.V., Arantes E.C., de Oliveira F.;
RT "Isolation and characterization of moojenin, an acid-active, anticoagulant
RT metalloproteinase from Bothrops moojeni venom.";
RL Toxicon 60:1251-1258(2012).
CC -!- FUNCTION: Metalloproteinase moojenin: snake venom metalloproteinase
CC that cleaves both alpha- and beta-chains of fibrinogen, but not the
CC gamma-chain. Shows a coagulant activity on bovine plasma about 3.1 fold
CC lower than crude venom. Renders the blood incoagulable when
CC intraperitoneally administered into mice. Induces necrosis in liver and
CC muscle, but does not cause histological alterations in mouse lungs,
CC kidney or heart. {ECO:0000269|PubMed:22975266}.
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: The fibrinogenolytic and coagulant activities of
CC the moojenin were abolished by preincubation with EDTA, 1,10-
CC phenanthroline and beta-mercaptoethanol. {ECO:0000269|PubMed:22975266}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:22975266};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:22975266};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22975266}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22975266}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22975266}.
CC -!- PTM: The N-terminus (from the N-terminal region of the
CC metalloproteinase domain) is blocked. {ECO:0000305}.
CC -!- MISCELLANEOUS: Does not cause hemorrhage in mice with doses up to 50 g.
CC Intraplantar injection of moojenin (50 mg) into the rat hind-paw does
CC not cause significant edematogenic or hyperalgesic effects
CC (PubMed:22975266). {ECO:0000305|PubMed:22975266}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DKR0; -.
DR SMR; P0DKR0; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR036436; Disintegrin_dom_sf.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Myotoxin; Protease; Secreted;
KW Toxin; Zinc.
FT CHAIN <1..>33
FT /note="Zinc metalloproteinase-disintegrin-like moojenin"
FT /id="PRO_0000420184"
FT CHAIN 1..>33
FT /note="Disintegrin-like"
FT /id="PRO_0000420185"
FT DOMAIN 8..>33
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 11..30
FT /note="In disintegrin-like; alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 11..?
FT /note="In zinc metalloproteinase-disintegrin-like moojenin;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 22..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 24..30
FT /note="In zinc metalloproteinase-disintegrin-like moojenin;
FT alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT NON_TER 1
FT NON_TER 33
SQ SEQUENCE 33 AA; 3461 MW; 1A5528F473F28164 CRC64;
LGPDIVSPPV CGNELLEVGE ECDCGTPENC QNE
