LECG_BOTJR
ID LECG_BOTJR Reviewed; 159 AA.
AC P83519; Q6TRS6; Q7T228;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=C-type lectin BJcuL {ECO:0000303|PubMed:11478954, ECO:0000303|PubMed:28003128};
DE Short=CTL;
DE AltName: Full=Galactose-specific lectin;
DE AltName: Full=Snake venom galactoside-binding lectin {ECO:0000303|PubMed:28003128};
DE Short=SVgalL {ECO:0000303|PubMed:28003128};
DE Flags: Precursor;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15135412; DOI=10.1016/j.pep.2004.02.012;
RA Kassab B.H., de Carvalho D.D., Oliveira M.A., Baptista G.R., Pereira G.A.,
RA Novello J.C.;
RT "Cloning, expression, and structural analysis of recombinant BJcuL, a c-
RT type lectin from the Bothrops jararacussu snake venom.";
RL Protein Expr. Purif. 35:344-352(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-159.
RC TISSUE=Venom gland;
RX PubMed=15134836; DOI=10.1016/j.biochi.2004.02.002;
RA Kashima S., Roberto P.G., Soares A.M., Astolfi-Filho S., Pereira J.O.,
RA Giuliati S., Faria M. Jr., Xavier M.A.S., Fontes M.R.M., Giglio J.R.,
RA Franca S.C.;
RT "Analysis of Bothrops jararacussu venomous gland transcriptome focusing on
RT structural and functional aspects: I -- gene expression profile of highly
RT expressed phospholipases A2.";
RL Biochimie 86:211-219(2004).
RN [3]
RP PROTEIN SEQUENCE OF 25-159.
RC TISSUE=Venom;
RX PubMed=11902666; DOI=10.1023/a:1014131115951;
RA de Carvalho D.D., Marangoni S., Novello J.C.;
RT "Primary structure characterization of Bothrops jararacussu snake venom
RT lectin.";
RL J. Protein Chem. 21:43-50(2002).
RN [4]
RP PROTEIN SEQUENCE OF 25-44.
RC TISSUE=Venom;
RX PubMed=15994137; DOI=10.1016/j.jchromb.2005.04.018;
RA De-Simone S.G., Correa-Netto C., Antunes O.A., De-Alencastro R.B.,
RA Silva F.P. Jr.;
RT "Biochemical and molecular modeling analysis of the ability of two p-
RT aminobenzamidine-based sorbents to selectively purify serine proteases
RT (fibrinogenases) from snake venoms.";
RL J. Chromatogr. B 822:1-9(2005).
RN [5]
RP PROTEIN SEQUENCE OF 25-32, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP ACTIVITY REGULATION.
RC TISSUE=Venom;
RA de Carvalho D.D., Marangoni S., Oliveira B., Novello J.C.;
RT "Isolation and characterization of a new lectin from the venom of the snake
RT Bothrops jararacussu.";
RL Biochem. Mol. Biol. Int. 44:933-938(1998).
RN [6]
RP FUNCTION.
RX PubMed=10628348;
RA Pereira-Bittencourt M., de Carvalho D.D., Gagliardi A.R., Collins D.C.;
RT "The effect of a lectin from the venom of the snake, Bothrops jararacussu,
RT on tumor cell proliferation.";
RL Anticancer Res. 19:4023-4025(1999).
RN [7]
RP FUNCTION.
RX PubMed=11478954; DOI=10.1016/s0041-0101(01)00106-4;
RA de Carvalho D.D., Schmitmeier S., Novello J.C., Markland F.S.;
RT "Effect of BJcuL (a lectin from the venom of the snake Bothrops
RT jararacussu) on adhesion and growth of tumor and endothelial cells.";
RL Toxicon 39:1471-1476(2001).
RN [8]
RP FUNCTION.
RX PubMed=21266049; DOI=10.1186/1471-2172-12-10;
RA Elifio-Esposito S., Tomazeli L., Schwartz C., Gimenez A.P., Fugii G.M.,
RA Fernandes L.C., Zishler L.F., Stuelp-Campelo P.M., Moreno A.N.;
RT "Human neutrophil migration and activation by BJcuL, a galactose binding
RT lectin purified from Bothrops jararacussu venom.";
RL BMC Immunol. 12:10-10(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND BIOTECHNOLOGY.
RC TISSUE=Venom;
RX PubMed=25811661; DOI=10.1371/journal.pone.0120514;
RA Klein R.C., Fabres-Klein M.H., de Oliveira L.L., Feio R.N., Malouin F.,
RA Ribon A.O.;
RT "A C-type lectin from Bothrops jararacussu venom disrupts Staphylococcal
RT biofilms.";
RL PLoS ONE 10:E0120514-E0120514(2015).
RN [10]
RP FUNCTION, BIOASSAY, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=16309723; DOI=10.1016/j.toxicon.2005.08.012;
RA Panunto P.C., da Silva M.A., Linardi A., Buzin M.P., Melo S.E., Mello S.M.,
RA Prado-Franceschi J., Hyslop S.;
RT "Biological activities of a lectin from Bothrops jararacussu snake venom.";
RL Toxicon 47:21-31(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 26-159 (HOMODECAMER) IN COMPLEX
RP WITH AMINOGLYCOSIDE ANTIBIOTICS, FUNCTION, METAL-BINDING SITES, SUBUNIT,
RP DISULFIDE BOND, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=28003128; DOI=10.1016/j.toxicon.2016.12.007;
RA Sartim M.A., Pinheiro M.P., de Padua R.A.P., Sampaio S.V., Nonato M.C.;
RT "Structural and binding studies of a C-type galactose-binding lectin from
RT Bothrops jararacussu snake venom.";
RL Toxicon 126:59-69(2017).
CC -!- FUNCTION: Galactose-binding lectin 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. Also binds lactose and raffinose (PubMed:28003128).
CC Shows high hemagglutinating activity on mammalian erythrocytes (Ref.5,
CC PubMed:16309723). It also involved in immunological functions, since it
CC is able of inducing potent neutrophil activation (PubMed:21266049,
CC PubMed:16309723). In vivo, it causes edema and increases vascular
CC permeability after injection into mouse hind paws (10-100 ug/paw). In
CC anesthetized rats, it decreases the blood pressure by approximately
CC 15%, with a rapid return to the resting level (PubMed:16309723). Is an
CC effective inhibitor of cell growth in some cancer cell lines,
CC especially against renal and pancreatic cancer cell lines, human breast
CC and ovarian carcinoma, glioblastoma and a bovine brain microvascular
CC endothelial cell line (PubMed:10628348, PubMed:11478954).
CC {ECO:0000269|PubMed:10628348, ECO:0000269|PubMed:11478954,
CC ECO:0000269|PubMed:16309723, ECO:0000269|Ref.5}.
CC -!- ACTIVITY REGULATION: Hemagglutination activity is inhibited by lactose
CC (MIC=2.5 mM), galactose (MIC=10 mM), and raffinose (Ref.5,
CC PubMed:16309723, PubMed:28003128). Is very weakly or not inhibited by
CC gentamicin, kanamycin, glucose and sucrose (PubMed:16309723,
CC PubMed:28003128). {ECO:0000269|PubMed:16309723,
CC ECO:0000269|PubMed:28003128, ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Homodecamer of disulfide-linked dimers arranged in two 5-fold
CC symmetric pentamers (Ref.5, PubMed:28003128). Binds the gentamicin
CC group of aminoglycoside antibiotics at the dimeric interface near the
CC intermolecular disulfide bond (PubMed:28003128).
CC {ECO:0000269|PubMed:28003128, ECO:0000305|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.5}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.5}.
CC -!- BIOTECHNOLOGY: Can be used in the treatment of bovine mastitis, since
CC it is able to both inhibit bacterial biofilm growth, and disrupt
CC existing biofilm, without affecting bacterial cell viability.
CC {ECO:0000305|PubMed:25811661}.
CC -!- MISCELLANEOUS: The lectin (up to 200 microg/ml) does not aggregate
CC human platelet-rich plasma (PRP) or washed platelets (WP), nor does it
CC alter the aggregation induced by ADP in PRP or by thrombin in WP.
CC {ECO:0000305|PubMed:16309723}.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP42417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY388642; AAQ92957.1; -; mRNA.
DR EMBL; AY251283; AAP42417.1; ALT_INIT; mRNA.
DR PDB; 5F2Q; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J=25-159.
DR PDBsum; 5F2Q; -.
DR AlphaFoldDB; P83519; -.
DR SMR; P83519; -.
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:0030308; P:negative regulation of cell growth; TAS:UniProtKB.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hemagglutinin; Lectin; Metal-binding; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:11902666,
FT ECO:0000269|PubMed:15994137, ECO:0000269|Ref.5"
FT CHAIN 25..159
FT /note="C-type lectin BJcuL"
FT /evidence="ECO:0000269|PubMed:11902666"
FT /id="PRO_0000046643"
FT DOMAIN 34..156
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 120..122
FT /note="Galactose-binding"
FT /evidence="ECO:0000250|UniProtKB:P21963"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT SITE 103
FT /note="Binds aminoglycoside antibiotics (subunit E')"
FT /evidence="ECO:0000269|PubMed:28003128"
FT SITE 104
FT /note="Binds aminoglycoside antibiotics (subunit A and E')"
FT /evidence="ECO:0000269|PubMed:28003128"
FT SITE 105
FT /note="Binds aminoglycoside antibiotics (subunit A)"
FT /evidence="ECO:0000269|PubMed:28003128"
FT SITE 109
FT /note="Binds aminoglycoside antibiotics (subunit A)"
FT /evidence="ECO:0000269|PubMed:28003128"
FT SITE 111
FT /note="Binds aminoglycoside antibiotics (subunit A and E')"
FT /evidence="ECO:0000269|PubMed:28003128"
FT DISULFID 27..38
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT DISULFID 55..155
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT DISULFID 62..157
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT DISULFID 110
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:28003128"
FT DISULFID 130..147
FT /evidence="ECO:0000269|PubMed:28003128,
FT ECO:0007744|PDB:5F2Q"
FT CONFLICT 43
FT /note="N -> D (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="C -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="N -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="N -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Q -> H (in Ref. 1; AAQ92957)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="F -> LGTSSKG (in Ref. 1; AAQ92957)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:5F2Q"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5F2Q"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5F2Q"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5F2Q"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5F2Q"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:5F2Q"
SQ SEQUENCE 159 AA; 18653 MW; CA54B549F208D1D5 CRC64;
MGRFLFVASS ACWFVFLSLS GAKGNNCPQD WLPMNGLCYK IFNELKAWKD AEMFCRKYKP
GCHLASIHLY GESPEIAEYI SDYHKGQSEV WIGLCDKKKD FSWEWTDRSC TDYLSWDKNQ
PDHYQNKEFC VELVSNTGYR LWNDQVCESK NAFLCQCKF
