ID   LECG_CRORU              Reviewed;         135 AA.
AC   P84987;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=C-type Lectin CRL;
DE            Short=CTL;
OS   Crotalus ruber ruber (Red diamond rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8736;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17251046; DOI=10.1016/j.cbpb.2006.11.022;
RA   Hamako J., Suzuki Y., Hayashi N., Kimura M., Ozeki Y., Hashimoto K.,
RA   Matsui T.;
RT   "Amino acid sequence and characterization of C-type lectin purified from
RT   the snake venom of Crotalus ruber.";
RL   Comp. Biochem. Physiol. 146B:299-306(2007).
CC   -!- FUNCTION: Beta-galactoside and N-acetylgalactosamine (GalNAc) specific
CC       C-type lectin. {ECO:0000269|PubMed:17251046}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:17251046}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17251046}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not induce platelet aggregation and does not
CC       inhibit platelet aggregation mediated by von Willebrand factor or
CC       fibrinogen with agonists. {ECO:0000305|PubMed:17251046}.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   AlphaFoldDB; P84987; -.
DR   SMR; P84987; -.
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; Lectin; Metal-binding;
KW   Secreted.
FT   CHAIN           1..135
FT                   /note="C-type Lectin CRL"
FT                   /id="PRO_0000263030"
FT   DOMAIN          10..132
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           96..98
FT                   /note="Galactose-binding"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P21963"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P21963"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P21963"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P21963"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000250|UniProtKB:P21963,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        31..131
FT                   /evidence="ECO:0000250|UniProtKB:P21963,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        38..133
FT                   /evidence="ECO:0000250|UniProtKB:P21963,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P21963,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        106..123
FT                   /evidence="ECO:0000250|UniProtKB:P21963,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   135 AA;  16274 MW;  052E6D0E5B782904 CRC64;
     NNCPLDWLPM NGLCYKIFNQ LKTWEDAEMF CRKYKPGCHL ASFHLYGESL EIAEYISDYH
     KGQDNVWIGL WDKKKDFSWE WTDRSCIDYL NWNKNQPDHY KNKEFCVELV SLSGYRLWND
     QVCESKDAFL CQCKF