LECG_BOTPA
ID LECG_BOTPA Reviewed; 135 AA.
AC P86970;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=C-type lectin BpLec;
DE Short=BpL;
DE Short=CTL;
OS Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1042543;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Castanheira L.E., Richardson M., Borges M.H., Rodrigues V.M.;
RL Submitted (JUN-2011) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=23178369; DOI=10.1016/j.ijbiomac.2012.11.018;
RA Castanheira L.E., Nunes D.C., Cardoso T.M., Santos Pde S., Goulart L.R.,
RA Rodrigues R.S., Richardson M., Borges M.H., Yoneyama K.A., Rodrigues V.M.;
RT "Biochemical and functional characterization of a C-type lectin (BpLec)
RT from Bothrops pauloensis snake venom.";
RL Int. J. Biol. Macromol. 54:57-64(2013).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22480909; DOI=10.1016/j.jprot.2012.03.028;
RA Rodrigues R.S., Boldrini-Franca J., Fonseca F.P., de la Torre P.,
RA Henrique-Silva F., Sanz L., Calvete J.J., Rodrigues V.M.;
RT "Combined snake venomics and venom gland transcriptomic analysis of
RT Bothropoides pauloensis.";
RL J. Proteomics 75:2707-2720(2012).
CC -!- FUNCTION: This lectin displays hemagglutinating activity on dog
CC (128'000 HU/mg) and cat erythrocytes, that is inhibited by beta-
CC galactosides (D-galactose, D-lactose, and N-acetyl-D-galactosamine) and
CC EDTA. In addition, has been shown to hemagglutinate promastigote forms
CC of Leishmania amazonensis. Also inhibits Gram-positive (S.aureus ATCC
CC 25923) (MIC is 31.25 ug/ml) but not Gram-negative (E.coli ATCC 25922)
CC bacteria. Is a calcium-dependent lectin. {ECO:0000269|PubMed:23178369,
CC ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:23178369}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=16800; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23178369};
CC -!- MISCELLANEOUS: Does not agglutinate erythrocytes from horse, ox and
CC mouse at doses up to 800 ug/ml. {ECO:0000305|PubMed:23178369}.
CC -!- MISCELLANEOUS: Hemagglutinin activity is not inhibited by D-fructose,
CC D-maltose, D-mannose, and D-sucrose. {ECO:0000305|PubMed:23178369}.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC -!- CAUTION: The same name (BpL) has been given to a lectin from Bothrops
CC pirajai (AC P0DL30). {ECO:0000305}.
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DR AlphaFoldDB; P86970; -.
DR SMR; P86970; -.
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 GO; GO:0042742; P:defense response to bacterium; 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 Antibiotic; Antimicrobial; Calcium; Direct protein sequencing;
KW Disulfide bond; Hemagglutinin; Lectin; Metal-binding; Secreted.
FT CHAIN 1..135
FT /note="C-type lectin BpLec"
FT /id="PRO_0000412757"
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 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:0000250|UniProtKB:P21963,
FT 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"
FT UNSURE 62
FT /note="Assigned by comparison with orthologs"
FT UNSURE 63
FT /note="Assigned by comparison with orthologs"
FT UNSURE 135
FT /note="Assigned by comparison with orthologs"
SQ SEQUENCE 135 AA; 16223 MW; A517C69B27DAC893 CRC64;
NNCPQDWLPM NGLCYKIFDE LKAWKDAEMF CRKYKPGCHL ASIHLYGESP EIAEYISDYH
KGQSEVWIGL WDEKKDFSWE WTDRSCTDYL SWDKNQPDHY KNKEFCVELV SYTGYRLWND
QVCESKNAFL CQCKF
