LECG_BOTIN
ID LECG_BOTIN Reviewed; 158 AA.
AC Q6QX33;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=C-type lectin BiL {ECO:0000303|PubMed:15519291};
DE Short=BiLec {ECO:0000303|PubMed:16730365};
DE Short=CTL {ECO:0000303|PubMed:15519291, ECO:0000303|PubMed:16730365};
DE Flags: Precursor;
OS Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-39 AND 56-78, MASS
RP SPECTROMETRY, FUNCTION, SUBUNIT, 3D-STRUCTURE MODELING, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15519291; DOI=10.1016/j.abb.2004.08.018;
RA Guimaraes-Gomes V., Oliveira-Carvalho A.L., Junqueira-de-Azevedo I.L.M.,
RA Dutra D.L.S., Pujol-Luz M., Castro H.C., Ho P.L., Zingali R.B.;
RT "Cloning, characterization, and structural analysis of a C-type lectin from
RT Bothrops insularis (BiL) venom.";
RL Arch. Biochem. Biophys. 432:1-11(2004).
RN [2]
RP PROTEIN SEQUENCE OF 24-58, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=16730365; DOI=10.1016/j.toxicon.2006.02.016;
RA Braga M.D., Martins A.M., Amora D.N., de Menezes D.B., Toyama M.H.,
RA Toyama D.O., Marangoni S., Barbosa P.S., de Sousa Alves R., Fonteles M.C.,
RA Monteiro H.S.;
RT "Purification and biological effects of C-type lectin isolated from
RT Bothrops insularis venom.";
RL Toxicon 47:859-867(2006).
CC -!- FUNCTION: Lectin with a hemagglutinating activity that is inhibited by
CC galactose, lactose and EDTA (PubMed:15519291). Is calcium-dependent
CC (PubMed:15519291). Shows effects on the renal function of isolated
CC perfused rat kidneys by increasing both perfusion pressure (PP) and
CC renal vascular resistance (RVR) (PubMed:16730365). In addition, the
CC urinary flow and glomerular filtration rate (GFR) decreases
CC significantly (PubMed:16730365). The changes observed may reflect
CC direct injury to the glomerular and tubular renal cells, and the rise
CC in permeability in the glomerular endothelial cells, may be the effect
CC of interactions of C-type lectin with endothelial cells or due to
CC release of other mediators by mesangial, tubular and endothelial cells
CC (PubMed:16730365). {ECO:0000269|PubMed:15519291,
CC ECO:0000269|PubMed:16730365}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15519291}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15519291}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15519291}.
CC -!- MASS SPECTROMETRY: Mass=16217.85; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15519291};
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY522720; AAS01426.1; -; mRNA.
DR AlphaFoldDB; Q6QX33; -.
DR SMR; Q6QX33; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15519291"
FT CHAIN 24..158
FT /note="C-type lectin BiL"
FT /evidence="ECO:0000305|PubMed:15519291"
FT /id="PRO_0000355252"
FT DOMAIN 33..155
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 119..121
FT /note="Galactose-binding"
FT /evidence="ECO:0000250|UniProtKB:P21963"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT DISULFID 26..37
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT DISULFID 54..154
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT DISULFID 61..156
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT DISULFID 109
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT DISULFID 129..146
FT /evidence="ECO:0000250|UniProtKB:P83519"
FT CONFLICT 28
FT /note="Q -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="L -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18636 MW; 0FA6303E34967EE4 CRC64;
MGRFIFVSFG LLVVFLSLSG AKGNNCPQDW LPMNGLCYKI FDELKAWKDA EMFCRKYKPG
CHLASFHLYG ESPEIAEYIS DYHKGQSEVW IGLWDKKKDF SWEWTDRSCT DYLSWDKNQP
DHYQNKEFCV ELVSDTGYRL WNDQVCESKN AFLCQCKF
