ID   LEC_BOTJA               Reviewed;         135 AA.
AC   Q9PRY7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=C-type lectin BjL;
DE            Short=CTL;
DE   AltName: Full=Galactoside-binding lectin BjL;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   PROTEIN SEQUENCE.
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-55, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=8311467; DOI=10.1006/abbi.1994.1043;
RA   Ozeki Y., Matsui T., Hamako J., Suzuki M., Fujimura Y., Yoshida E.,
RA   Nishida S., Titani K.;
RT   "C-type galactoside-binding lectin from Bothrops jararaca venom: comparison
RT   of its structure and function with those of botrocetin.";
RL   Arch. Biochem. Biophys. 308:306-310(1994).
CC   -!- FUNCTION: Lectin that shows calcium-dependent hemagglutination activity
CC       but does not induce platelet aggregation in the presence or absence of
CC       calcium ions and vWF. Does not inhibit platelet aggregation induced by
CC       botrocetin and vWF. {ECO:0000269|PubMed:8311467}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:8311467}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC   -!- CAUTION: The complete sequence of this protein comes from
CC       PubMed:17046438, but no sequencing method is described. {ECO:0000305}.
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DR   AlphaFoldDB; Q9PRY7; -.
DR   SMR; Q9PRY7; -.
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.
FT   CHAIN           1..135
FT                   /note="C-type lectin BjL"
FT                   /id="PRO_0000355253"
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                   /evidence="ECO:0000250"
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"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        31..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        38..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        106..123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   135 AA;  16148 MW;  7815038A4EB31205 CRC64;
     NNCPQDWLPM NGLCYKIFDE LKAWKDAEMF CRKYKPGCHL ASFHLYGESP EIAEYISDYH
     KGQAEVWIGL WDKKKDFSWE WTDRSCTDYL TWDKNQPDHY EGKEFCVELV SLTGYRLWND
     QVCESKNAFL CQCKF