ID   LECG1_BUNFA             Reviewed;         158 AA.
AC   Q90WI8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=C-type lectin BfL-1;
DE            Short=CTL;
DE   Flags: Precursor;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=11600152; DOI=10.1016/s0041-0101(01)00172-6;
RA   Zha H.-G., Lee W.-H., Zhang Y.;
RT   "Cloning of cDNAs encoding C-type lectins from Elapidae snakes Bungarus
RT   fasciatus and Bungarus multicinctus.";
RL   Toxicon 39:1887-1892(2001).
RN   [2]
RP   3D-STRUCTURE MODELING.
RX   PubMed=17046438; DOI=10.1016/j.toxicon.2006.08.006;
RA   Abreu P.A., Albuquerque M.G., Rodrigues C.R., Castro H.C.;
RT   "Structure-function inferences based on molecular modeling, sequence-based
RT   methods and biological data analysis of snake venom lectins.";
RL   Toxicon 48:690-701(2006).
CC   -!- FUNCTION: Galactose-binding lectin which recognizes specific
CC       carbohydrate structures and agglutinates a variety of animal cells by
CC       binding to cell-surface glycoproteins and glycolipids. May be a
CC       calcium-dependent lectin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   EMBL; AF354270; AAK43584.1; -; mRNA.
DR   AlphaFoldDB; Q90WI8; -.
DR   SMR; Q90WI8; -.
DR   PRIDE; Q90WI8; -.
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   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Lectin; Metal-binding; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..158
FT                   /note="C-type lectin BfL-1"
FT                   /id="PRO_0000355258"
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   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        54..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        61..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        129..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   158 AA;  18638 MW;  ECF85936FA4182B8 CRC64;
     MGHFTFIGLC LLAMFLSLSG AECYTCPIDW LPKNGLCYKV FSKHKTWFDA EMYCRKFKPG
     CHLASLHSNA DAVEFSEYIS DYLTGQGHVW IGLRDTKKKY IWEWTDRSRT DFLPWRKKQP
     DHFNNNEFCV EIVNFTGYLQ WNDDNCAALR PFLCQCKY