ID   LEC1_BITGA              Reviewed;         159 AA.
AC   Q6T7B7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=C-type lectin 1;
DE            Short=CTL;
DE   Flags: Precursor;
OS   Bitis gabonica (Gaboon adder) (Gaboon viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA   Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA   Ribeiro J.M.C.;
RT   "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT   full-length transcripts (cDNA) and proteins.";
RL   Gene 337:55-69(2004).
CC   -!- FUNCTION: Lectin which recognizes specific carbohydrate structures and
CC       agglutinates a variety of animal cells by binding to cell-surface
CC       glycoproteins and glycolipids. May be a calcium-dependent lectin (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
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; AY429477; AAR06851.1; -; mRNA.
DR   AlphaFoldDB; Q6T7B7; -.
DR   SMR; Q6T7B7; -.
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; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 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..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..159
FT                   /note="C-type lectin 1"
FT                   /id="PRO_0000355248"
FT   DOMAIN          33..156
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           119..121
FT                   /note="Sugar-binding"
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         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        54..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        61..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        130..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   159 AA;  18626 MW;  C54788F6EB696B81 CRC64;
     MGRFIFISFG LLVVFFFLSG AKGSTCPFHW LPMYGLCYKI FDKLKTWNDA EMFCRKYKPG
     CHLASLHSKR DSIEFAEYIS DYRKGWGNVW IGMWGRKEGL TCEWTDGSST TYVAWKQNLT
     DHYLNKDLFC AEIVSYTGYR LWNKQDCKVK NAFLCQCGF