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CONA_CANBR
ID   CONA_CANBR              Reviewed;         237 AA.
AC   P55915;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Concanavalin-Br;
DE            Short=Con Br;
OS   Canavalia brasiliensis (Brazilian jack bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX   NCBI_TaxID=61861;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RA   Grangeiro T.B.;
RL   Thesis (1996), Universidade Federale do Ceara, Brazil.
RN   [2]
RP   FUNCTION.
RX   PubMed=1398779; DOI=10.3109/08820139209069369;
RA   Barral-Netto M., Santos S.B., Barral A., Moreira L.I., Santos C.F.,
RA   Moreira R.A., Oliveira J.T., Cavada B.S.;
RT   "Human lymphocyte stimulation by legume lectins from the Diocleae tribe.";
RL   Immunol. Invest. 21:297-303(1992).
RN   [3]
RP   FUNCTION, AND CALCIUM-BINDING.
RX   PubMed=7524287; DOI=10.1007/bf02001905;
RA   Gomes J.C., Ferreira R.R., Cavada B.S., Moreira R.A., Oliveira J.T.;
RT   "Histamine release induced by glucose (mannose)-specific lectins isolated
RT   from Brazilian beans. Comparison with concanavalin A.";
RL   Agents Actions 41:132-135(1994).
RN   [4]
RP   FUNCTION, AND CALCIUM-BINDING.
RX   PubMed=8891754; DOI=10.1007/bf02252314;
RA   Ferreira R.R., Cavada B.S., Moreira R.A., Oliveira J.T., Gomes J.C.;
RT   "Characteristics of the histamine release from hamster cheek pouch mast
RT   cells stimulated by lectins from Brazilian beans and concanavalin A.";
RL   Inflamm. Res. 45:442-447(1996).
RN   [5]
RP   FUNCTION.
RX   PubMed=18472821; DOI=10.1080/09629359791695;
RA   Assreuy A.M., Shibuya M.D., Martins G.J., De Souza M.L., Cavada B.S.,
RA   Moreira R.A., Oliveira J.T., Ribeiro R.A., Flores C.A.;
RT   "Anti-inflammatory effect of glucose-mannose binding lectins isolated from
RT   Brazilian beans.";
RL   Mediators Inflamm. 6:201-210(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=9575151; DOI=10.1074/jbc.273.20.12082;
RA   Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., de Sousa F.A.M.,
RA   Oscarson S., Brewer C.F.;
RT   "Diocleinae lectins are a group of proteins with conserved binding sites
RT   for the core trimannoside of asparagine-linked oligosaccharides and
RT   differential specificities for complex carbohydrates.";
RL   J. Biol. Chem. 273:12082-12088(1998).
RN   [7]
RP   MANGANESE-BINDING.
RX   PubMed=10694401; DOI=10.1021/bi992102b;
RA   Lee H.C., Goroncy A.K., Peisach J., Cavada B.S., Grangeiro T.B.,
RA   Ramos M.V., Sampaio A.H., Dam T.K., Brewer C.F.;
RT   "Demonstration of a conserved histidine and two water ligands at the Mn2+
RT   site in Diocleinae lectins by pulsed EPR spectroscopy.";
RL   Biochemistry 39:2340-2346(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=10747944; DOI=10.1074/jbc.m000670200;
RA   Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., Ceccatto V.M.,
RA   de Sousa F.A., Oscarson S., Brewer C.F.;
RT   "Thermodynamic binding studies of lectins from the diocleinae subtribe to
RT   deoxy analogs of the core trimannoside of asparagine-linked
RT   oligosaccharides.";
RL   J. Biol. Chem. 275:16119-16126(2000).
RN   [9]
RP   FUNCTION, AND TOXIC DOSE.
RX   PubMed=19765980; DOI=10.1016/j.biortech.2009.07.062;
RA   dos Santos A.F., Cavada B.S., da Rocha B.A., do Nascimento K.S.,
RA   Sant'Ana A.E.;
RT   "Toxicity of some glucose/mannose-binding lectins to Biomphalaria glabrata
RT   and Artemia salina.";
RL   Bioresour. Technol. 101:794-798(2010).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=9094437; DOI=10.1016/s0014-5793(97)00137-3;
RA   Sanz-Aparicio J., Hermoso J., Grangeiro T.B., Calvete J.J., Cavada B.S.;
RT   "The crystal structure of Canavalia brasiliensis lectin suggests a
RT   correlation between its quaternary conformation and its distinct biological
RT   properties from Concanavalin A.";
RL   FEBS Lett. 405:114-118(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE.
RX   PubMed=10506175; DOI=10.1074/jbc.274.41.29188;
RA   Bouckaert J., Hamelryck T.W., Wyns L., Loris R.;
RT   "The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-
RT   6)Man(alpha1-O)Me in complex with concanavalin A.";
RL   J. Biol. Chem. 274:29188-29195(1999).
CC   -!- FUNCTION: Glucose/D-mannose specific lectin. Has anti-inflammatory
CC       activity in rats. Induces histamine release in mast cells from hamster
CC       and rat. Induces lymphocyte proliferation and IFNG production. Shows
CC       toxicity against the aquatic snail B.glabrata at concentrations higher
CC       than 20 ug/ml. {ECO:0000269|PubMed:10747944,
CC       ECO:0000269|PubMed:1398779, ECO:0000269|PubMed:18472821,
CC       ECO:0000269|PubMed:19765980, ECO:0000269|PubMed:7524287,
CC       ECO:0000269|PubMed:8891754, ECO:0000269|PubMed:9575151}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10506175}.
CC   -!- TOXIC DOSE: LD(50) is 15.4 ug/ml against the brine shrimp A.salina.
CC       {ECO:0000269|PubMed:19765980}.
CC   -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC       and one calcium ion. The metal ions are essential for the saccharide-
CC       binding and cell-agglutinating activities.
CC   -!- MISCELLANEOUS: Is being tested as a molluscicide with potential
CC       application in controlling schistosomiasis. The causative agent of
CC       schistosomiasis depends on freshwater snails of the genus Biomphalaria
CC       as hosts during its larval stages.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   PDB; 1AZD; X-ray; 3.00 A; A/B/C/D=1-237.
DR   PDB; 1QDC; X-ray; 2.00 A; A/B/C/D=1-237.
DR   PDB; 1QDO; X-ray; 2.80 A; A/B/C/D=1-237.
DR   PDB; 2CYF; X-ray; 1.80 A; A/C=1-237.
DR   PDB; 3JU9; X-ray; 2.10 A; A=1-237.
DR   PDB; 4H55; X-ray; 2.07 A; A=1-237.
DR   PDB; 4P14; X-ray; 2.00 A; A=1-237.
DR   PDB; 4PCR; X-ray; 2.15 A; A/D=1-237.
DR   PDB; 5YGM; X-ray; 1.60 A; A=1-237.
DR   PDB; 6VB8; X-ray; 2.20 A; A=1-237.
DR   PDBsum; 1AZD; -.
DR   PDBsum; 1QDC; -.
DR   PDBsum; 1QDO; -.
DR   PDBsum; 2CYF; -.
DR   PDBsum; 3JU9; -.
DR   PDBsum; 4H55; -.
DR   PDBsum; 4P14; -.
DR   PDBsum; 4PCR; -.
DR   PDBsum; 5YGM; -.
DR   PDBsum; 6VB8; -.
DR   AlphaFoldDB; P55915; -.
DR   SMR; P55915; -.
DR   UniLectin; P55915; -.
DR   PRIDE; P55915; -.
DR   EvolutionaryTrace; P55915; -.
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; IPR000985; Lectin_LegA_CS.
DR   InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 2.
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; Lectin; Manganese;
KW   Mannose-binding; Metal-binding; Toxin.
FT   CHAIN           1..237
FT                   /note="Concanavalin-Br"
FT                   /id="PRO_0000105085"
FT   BINDING         8
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         12
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000269|PubMed:10506175"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         19
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         24
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         34
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..100
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000269|PubMed:10506175"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          24..33
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          46..55
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   TURN            56..59
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1QDO"
FT   STRAND          73..78
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          87..96
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          105..121
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:4H55"
FT   STRAND          170..177
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          186..198
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   STRAND          209..215
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:5YGM"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:5YGM"
SQ   SEQUENCE   237 AA;  25568 MW;  4D62F2113A36C38F CRC64;
     ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
     LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY KETNTILSWS FTSKLKSNST
     HETNALHFMF NQFSKDQKDL ILQGDATTGT EGNLRLTRVS SNGSPQGSSV GRALFYAPVH
     IWESSAVVAS FEATFTFLIK SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
 
 
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