ID   LECG_BOTPI              Reviewed;         135 AA.
AC   P0DL30;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=C-type lectin BPL;
DE            Short=CTL;
DE   AltName: Full=Galactose-specific lectin;
OS   Bothrops pirajai (Piraja's lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=113192;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOASSAY, AND INDUCTION.
RC   TISSUE=Venom;
RX   PubMed=15381156; DOI=10.1016/j.biocel.2004.06.003;
RA   Havt A., Toyama M.H., do Nascimento N.R., Toyama D.O., Nobre A.C.,
RA   Martins A.M., Barbosa P.S., Novello J.C., Boschero A.C., Carneiro E.M.,
RA   Fonteles M.C., Monteiro H.S.;
RT   "A new C-type animal lectin isolated from Bothrops pirajai is responsible
RT   for the snake venom major effects in the isolated kidney.";
RL   Int. J. Biochem. Cell Biol. 37:130-141(2005).
CC   -!- FUNCTION: Galactose-binding protein which recognizes specific
CC       carbohydrate structures and agglutinates a variety of animal cells by
CC       binding to cell-surface glycoproteins and glycolipids. Calcium-
CC       dependent lectin. Shows high hemagglutinating activity in the presence
CC       of human erythrocytes, which are agglutinated with a minimum
CC       hemagglutination concentration (MHC) of 2.5-0.35 ug/ml. Causes indirect
CC       nephrotoxicity. Causes reductions in perfusion pressures, renal
CC       vascular resistance, urinary flow, glomerular filtration rate, sodium,
CC       potassium and chloride tubular transport. Its effects may be caused by
CC       the release of inflammatory mediators. {ECO:0000269|PubMed:15381156}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- INDUCTION: Hemagglutination activity is inhibited by D-lactose
CC       (MIC=1.75 mM), D-galactose (MIC=0.75 mM) and D-raphinose (MIC=3.5 mM).
CC       Is not inhibited by D-glucose, D-sucrose, D-maltose, D-mannose, D-
CC       fructose, D-threalose, and methyl-manopyrosonide (PubMed:15381156).
CC       {ECO:0000269|PubMed:15381156}.
CC   -!- MISCELLANEOUS: Does not induce direct vasoactive effects in perfused
CC       arteriolar mesenteric bed, and does not potentiate bradykinin
CC       contraction in the ileum. {ECO:0000305|PubMed:15381156}.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC   -!- CAUTION: The same name has been given to a lectin from Bothropoides
CC       pauloensis (AC P86970). {ECO:0000305}.
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DR   AlphaFoldDB; P0DL30; -.
DR   SMR; P0DL30; -.
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 BPL"
FT                   /id="PRO_0000422308"
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"
FT   BINDING         104
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;  16117 MW;  0654FF326102FD61 CRC64;
     NNCPGDWLPM NGLCYKIFNE LKAWEDAEMF CRKYKPGCHL ASIHIYGESL EIAEYISDYH
     KGQAEVWIGL WDKKKDFSWE WTDRSCTDYL SWDKNQPDHY ENKEFCVELV SLTGYRLWED
     QVCESKNAFL CQCKF