VM3L_BOTLC
ID VM3L_BOTLC Reviewed; 93 AA.
AC P0DJ87;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like leucurogin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
OS Bothrops leucurus (Whitetail lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157295;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21641921; DOI=10.1016/j.toxicon.2011.05.013;
RA Higuchi D.A., Almeida M.C., Barros C.C., Sanchez E.F., Pesquero P.R.,
RA Lang E.A., Samaan M., Araujo R.C., Pesquero J.B., Pesquero J.L.;
RT "Leucurogin, a new recombinant disintegrin cloned from Bothrops leucurus
RT (white-tailed-jararaca) with potent activity upon platelet aggregation and
RT tumor growth.";
RL Toxicon 58:123-129(2011).
CC -!- FUNCTION: Snake venom zinc metalloprotease that possesses hemorrhagic
CC activity (By similarity). The disintegrin-like domain has been
CC expressed and named leucurogin. This recombinant disintegrin is able to
CC inhibit collagen-induced platelet aggregation but not ADP- or
CC arachidonic acid-induced platelet aggregation. In addition, this
CC disintegrin has been observed to inhibit the growth of experimental
CC Ehrlich tumor and to have anti-angiogenesis effect on the sponge
CC implant model. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DJ87; -.
DR SMR; P0DJ87; -.
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; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..>93
FT /note="Zinc metalloproteinase-disintegrin-like leucurogin"
FT /id="PRO_0000413953"
FT DOMAIN 8..>93
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..74
FT /note="D/ECD-tripeptide"
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 BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 11..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 22..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 24..30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 34..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 48..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 53..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 66..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT NON_TER 1
FT NON_TER 93
SQ SEQUENCE 93 AA; 9710 MW; 09ABADA02DA399C5 CRC64;
LGTDIISPPV CGNELLEVGE ECDCGTPENC QNECCDAATC KLKSGSECGH GDCCEQCKFT
KSGTECRASM SECDPAEHCT GQSSECPADV GHK
