LECC1_CENMI
ID LECC1_CENMI Reviewed; 247 AA.
AC C0HK20;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Mannose-specific lectin CML-2 {ECO:0000303|PubMed:26321423};
DE Contains:
DE RecName: Full=Mannose-specific lectin CML-1 {ECO:0000303|PubMed:26321423};
OS Centrolobium microchaete (Canarywood tree) (Centrolobium robustum var.
OS microchaete).
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=500177 {ECO:0000303|PubMed:26321423};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP GLYCOSYLATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:26321423};
RX PubMed=26321423; DOI=10.1016/j.ijbiomac.2015.08.059;
RA Vasconcelos M.A., Alves A.C., Carneiro R.F., Dias A.H., Martins F.W.,
RA Cajazeiras J.B., Nagano C.S., Teixeira E.H., Nascimento K.S., Cavada B.S.;
RT "Purification and primary structure of a novel mannose-specific lectin from
RT Centrolobium microchaete Mart seeds.";
RL Int. J. Biol. Macromol. 81:600-607(2015).
CC -!- FUNCTION: Mannose-specific lectin. Also binds alpha-methyl-D-mannoside,
CC D-glucose, N-acetyl-D-glucosamine and sucrose but not D-galactose, D-
CC arabinose, D-fructose, D-xylose, lactose or glycoproteins fetiun, PSM
CC and ovalbumin. Shows agglutinating activity towards rabbit
CC erythrocytes. {ECO:0000269|PubMed:26321423}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8 for hemagglutinating activity. Activity drops
CC rapidly at lower or higher pH. {ECO:0000269|PubMed:26321423};
CC Temperature dependence:
CC Thermostable. Retains hemagglutinating activity after incubation at
CC 50 degrees Celsius for 1 hour. At higher temperatures activity drops
CC drastically and is lost at 80 degrees Celsius.
CC {ECO:0000269|PubMed:26321423};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:26321423}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:26321423}.
CC -!- MASS SPECTROMETRY: [Mannose-specific lectin CML-1]: Mass=27224;
CC Mass_error=2; Method=Electrospray; Note=CML-1.;
CC Evidence={ECO:0000269|PubMed:26321423};
CC -!- MASS SPECTROMETRY: [Mannose-specific lectin CML-2]: Mass=27338;
CC Mass_error=2; Method=Electrospray; Note=CML-2.;
CC Evidence={ECO:0000269|PubMed:26321423};
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR AlphaFoldDB; C0HK20; -.
DR SMR; C0HK20; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Calcium; Direct protein sequencing; Glycoprotein; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..247
FT /note="Mannose-specific lectin CML-2"
FT /evidence="ECO:0000269|PubMed:26321423"
FT /id="PRO_0000437084"
FT CHAIN 1..246
FT /note="Mannose-specific lectin CML-1"
FT /evidence="ECO:0000269|PubMed:26321423"
FT /id="PRO_0000437085"
FT BINDING 87
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 107
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 138
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 139
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 221
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 222
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT BINDING 223
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:C0HJX1"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT UNSURE 75..76
FT /note="Assigned by comparison with orthologs"
FT /evidence="ECO:0000305|PubMed:26321423"
SQ SEQUENCE 247 AA; 27286 MW; 2ABFC1F025149B92 CRC64;
SDSLSFSFIN FDKDERNVIA QGDARLVGNN ILQLTRTDSN GSPVKSTVGR ILYVAQVRLW
EKSTNRVANF QSQFSFFLES PLSNPADGIA FFIAPPDTAI PSGSAGGLLG LFSPKTAQNE
SANQVLAVEF DTFYAQNSNT WDPNYPHIGI DVNSIKSAKT VRWERREGVT LNVLVTYNPS
TRTIDVVATY PDGQRYDLSV VVDVTTVLPE WVRVGFSAAS GEQFQTHNLE SWSFTSTLLY
TAQKENN
