LECC1_CENTO
ID LECC1_CENTO Reviewed; 245 AA.
AC C0HJX1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Mannose/glucose-specific lectin {ECO:0000303|PubMed:26946944, ECO:0000303|Ref.2};
DE Short=CTL {ECO:0000303|PubMed:26946944, ECO:0000303|Ref.2};
OS Centrolobium tomentosum (Arariba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Centrolobium.
OX NCBI_TaxID=500182 {ECO:0000303|Ref.2};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-245 IN COMPLEX
RP WITH METHYL-DIMANNOSIDE; CALCIUM AND MANGANESE, FUNCTION, SUBUNIT,
RP DIMERIZATION, GLYCOSYLATION AT ASN-119, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:26946944};
RX PubMed=26946944; DOI=10.1016/j.abb.2016.03.001;
RA Almeida A.C., Osterne V.J., Santiago M.Q., Pinto-Junior V.R.,
RA Silva-Filho J.C., Lossio C.F., Faustino Nascimento F.L.,
RA Honorato Almeida R.P., Teixeira C.S., Leal R.B., Delatorre P.,
RA Matias Rocha B.A., Sampaio Assreuy A.M., Nascimento K.S., Cavada B.S.;
RT "Structural analysis of Centrolobium tomentosum seed lectin with
RT inflammatory activity.";
RL Arch. Biochem. Biophys. 596:73-83(2016).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 26-45; 137-163; 183-196 AND 214-232, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Seed {ECO:0000303|Ref.2};
RA Almeida A.C., Silva H.C., Pereira-Junior F.N., Cajazeiras J.B.,
RA Delatorre P., Nagano C.S., Nascimento K.S., Cavada B.S.;
RT "Purification and partial characterization of a new mannose/glucose-
RT specific lectin from Centrolobium tomentosum Guill. ex Benth seeds
RT exhibiting low toxicity on Artemia sp.";
RL Int. J. Ind. Med. Plants 47:1567-1577(2014).
CC -!- FUNCTION: Mannose/glucose-specific lectin that also binds derivatives
CC N-acetyl-D-glucosamine and alpha-methyl-D-mannopyranoside with even
CC higher affinity (Ref.2, PubMed:26946944). Has hemagglutinating activity
CC towards rabbit erythrocytes (Ref.2). Is toxic towards brine shrimp
CC A.nauplii (Ref.2). In rats, induces dose-dependent paw edema
CC (PubMed:26946944). {ECO:0000269|PubMed:26946944, ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7 for hemagglutinating activity. Activity drops
CC rapidly at lower or higher pH. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Thermostable. Retains hemagglutinating activity after incubation at
CC 70 degrees Celsius for 1 hour. At higher temperatures activity drops
CC drastically and is lost at 100 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26946944}.
CC -!- MASS SPECTROMETRY: Mass=27452; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.2};
CC -!- TOXIC DOSE: LD(50) is 33.56 ug/ml against A.nauplii.
CC {ECO:0000269|Ref.2}.
CC -!- MISCELLANEOUS: Hemagglutinating activity is not inhibited by D-
CC arabinose, D-fructose, D-fucose, D-galactose, D-xylose, alpha-methyl-D-
CC glactopyranoside, carrageenan, lactose or mucin. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 5EYX; X-ray; 2.25 A; A/B=1-245.
DR PDB; 5EYY; X-ray; 1.90 A; A/B=1-245.
DR PDBsum; 5EYX; -.
DR PDBsum; 5EYY; -.
DR AlphaFoldDB; C0HJX1; -.
DR SMR; C0HJX1; -.
DR UniLectin; C0HJX1; -.
DR iPTMnet; C0HJX1; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin;
KW Manganese; Mannose-binding; Metal-binding; Toxin.
FT CHAIN 1..245
FT /note="Mannose/glucose-specific lectin"
FT /id="PRO_0000436265"
FT BINDING 87
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 107
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 138
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 139
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 221
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 222
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT BINDING 223
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:26946944"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26946944"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:5EYY"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 66..79
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5EYY"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:5EYY"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5EYY"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5EYY"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5EYY"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5EYY"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 210..223
FT /evidence="ECO:0007829|PDB:5EYY"
FT STRAND 226..239
FT /evidence="ECO:0007829|PDB:5EYY"
SQ SEQUENCE 245 AA; 27063 MW; 91B68CEC309606C8 CRC64;
SDSLSFSFIN FDQDERNVIA QGDARLSGNN ILQLTRTDSD GTPVRSTVGR ILYSAQVRLW
EKSTNRVANF QTQFSFFLES PLSNPADGIA FFIAPPDTAI PSGSAGGLLG LFSPKTAQNE
SANQVLAVEF DTFYAQNSNT WDPNYPHIGI DVNSIKSAKT VRWERREGVT LNVLVTYNPS
TKTLDVVATY PDGQRYDLSV VVDVTTVLPE WVRVGFSAAS GEQFQTHNLE SWSFTSTLLY
TAQKE
