VM3LB_BOTLC
ID VM3LB_BOTLC Reviewed; 324 AA.
AC P86092;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Zinc metalloproteinase leucurolysin-B {ECO:0000303|PubMed:17963685};
DE Short=Leuc-B;
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 PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Venom {ECO:0000269|PubMed:17963685};
RX PubMed=17963685; DOI=10.1016/j.abb.2007.10.002;
RA Sanchez E.F., Gabriel L.M., Gontijo S., Gremski L.H., Veiga S.S.,
RA Evangelista K.S., Eble J.A., Richardson M.;
RT "Structural and functional characterization of a P-III metalloproteinase,
RT leucurolysin-B, from Bothrops leucurus venom.";
RL Arch. Biochem. Biophys. 468:193-204(2007).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that acts as a potent
CC hemorrhagic toxin. Hydrolyzes the insulin B chain at the 14-Ala-|-Leu-
CC 15 bond but not the 16-Tyr-|-Leu-17 bond. Degrades the alpha-chain of
CC fibrin and hydrolyzes the Aalpha-chain of fibrinogen (FGA) while
CC leaving the beta and gamma chains unaffected. Degrades type-I collagen
CC and its gelatin. Degrades the alpha-1 chain of type-IV collagen and its
CC gelatin but not the alpha-2 chain. Degrades plasma fibronectin, plasma
CC vitronectin and basement membrane enactin. It inhibits collagen-induced
CC platelet aggregation. {ECO:0000269|PubMed:17963685}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P30431};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P30431};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, but not by PMSF. Pre-incubation
CC with 2 mM DTT completely abolishes activity.
CC {ECO:0000269|PubMed:17963685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-9.3 with dimethyl casein as substrate.
CC {ECO:0000269|PubMed:17963685};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius with dimethyl casein as
CC substrate. {ECO:0000269|PubMed:17963685};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17963685}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17963685}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17963685}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17963685}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17963685,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: Does not interact with alpha-1/beta-1 or alpha-2/beta-1
CC integrin. {ECO:0000305|PubMed:17963685}.
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; P86092; -.
DR SMR; P86092; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA:UniProtKB.
DR GO; GO:0035806; P:modulation of blood coagulation in another organism; IDA:UniProtKB.
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 Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 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; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..324
FT /note="Zinc metalloproteinase leucurolysin-B"
FT /id="PRO_0000363164"
FT DOMAIN <1..119
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 127..213
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 191..193
FT /note="D/ECD-tripeptide"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P30431"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P30431"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P30431"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..114
FT /evidence="ECO:0000250|UniProtKB:P28891"
FT DISULFID 74..98
FT /evidence="ECO:0000250|UniProtKB:P28891"
FT DISULFID 76..81
FT /evidence="ECO:0000250|UniProtKB:P28891"
FT DISULFID 130..159
FT /evidence="ECO:0000250"
FT DISULFID 141..154
FT /evidence="ECO:0000250"
FT DISULFID 143..149
FT /evidence="ECO:0000250"
FT DISULFID 153..176
FT /evidence="ECO:0000250"
FT DISULFID 167..173
FT /evidence="ECO:0000250"
FT DISULFID 172..198
FT /evidence="ECO:0000250"
FT DISULFID 185..205
FT /evidence="ECO:0000255"
FT DISULFID 192..224
FT /evidence="ECO:0000250"
FT DISULFID 217..229
FT /evidence="ECO:0000250"
FT DISULFID 236..286
FT /evidence="ECO:0000250"
FT DISULFID 251..295
FT /evidence="ECO:0000250"
FT DISULFID 264..274
FT /evidence="ECO:0000250"
FT DISULFID 281..315
FT /evidence="ECO:0000250"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:17963685"
SQ SEQUENCE 324 AA; 36262 MW; 7A6F2716C810BC09 CRC64;
DTVLLNRISH DNAQLLAIVF NENVIGKAYT GGMCDPRYSV GVVMDHSPIN RLVADTMAHE
MGHNLGIHHD TGSCSCGGHS CIMSRVISHQ PLQYFSNCSY IEYWDFITKL NPQCILNEPL
RTDIVSPPVC GNELLEMGEE CDCGSPRNCR DLCCDAATCK LHSWVECESG ECCDQCRFIK
AGNVCRPPRK ECDVAEACTG QSAQCPTDDF KRNGQPCLNN YAYCYQGNCP IMYHQCYALF
GSDATMAQDS CFQVNKKGNE YFYCRLENGI NIPCAQEDVK CGRLFCHNMK YEQDCNYSDR
GMVDNGTKCA EGKVCNSNRQ AYQR
