ID   LECG_HOPST              Reviewed;         158 AA.
AC   D2YVK1;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=C-type lectin galactose-binding isoform;
DE            Short=CTL;
DE   AltName: Full=Venom C-type lectin galactose binding isoform;
DE   Flags: Precursor;
OS   Hoplocephalus stephensii (Stephens' banded snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Hoplocephalus.
OX   NCBI_TaxID=196418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21115100; DOI=10.1016/j.biochi.2010.11.006;
RA   Earl S.T., Robson J., Trabi M., de Jersey J., Masci P.P., Lavin M.F.;
RT   "Characterisation of a mannose-binding C-type lectin from Oxyuranus
RT   scutellatus snake venom.";
RL   Biochimie 93:519-527(2011).
CC   -!- FUNCTION: Galactose-binding lectin that binds to and agglutinates
CC       erythrocytes in a calcium-dependent manner. {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; EF194744; ABP94089.1; -; mRNA.
DR   AlphaFoldDB; D2YVK1; -.
DR   SMR; D2YVK1; -.
DR   PRIDE; D2YVK1; -.
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; Hemagglutinin; Lectin; Metal-binding; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..158
FT                   /note="C-type lectin galactose-binding isoform"
FT                   /id="PRO_0000422552"
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   DISULFID        26..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        54..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        129..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   158 AA;  18567 MW;  10613408E9204C5D CRC64;
     MGRFLLVTLS LLVVAFSLNG ANNCCCPQDW LPKNGYCYKV FKDHKSWDDA EMFCRKLKPG
     CHLASLHSNA DAFDFSEYIT DYLTGHDHVW IGLRDTEKNY IWEWTDRSRT DFLPWKKDQP
     DHHNNDEFCV EIVSFTGYLQ WNDDSCTALR PFLCQCKH