LEC2_COLES
ID LEC2_COLES Reviewed; 261 AA.
AC A5HMM7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Mannose-specific lectin 2 {ECO:0000305};
DE AltName: Full=Agglutinin {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 2 chain 1 {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 2 chain 2 {ECO:0000305};
DE Flags: Precursor;
OS Colocasia esculenta (Wild taro) (Arum esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC Colocasia.
OX NCBI_TaxID=4460;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nayak S.N., Bhat R., Krishnaraj P.U., Krishnamurthy K.,
RA Kuruvinashetti M.S.;
RT "Colocasia esculenta lectin gene.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 24-133 IN COMPLEX WITH
RP BETA-D-MANNOSE, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=27558840; DOI=10.1093/glycob/cww083;
RA Pereira P.R., Meagher J.L., Winter H.C., Goldstein I.J., Paschoalin V.M.,
RA Silva J.T., Stuckey J.A.;
RT "High-resolution crystal structures of Colocasia esculenta tarin lectin.";
RL Glycobiology 27:50-56(2017).
CC -!- FUNCTION: Mannose-specific lectin (PubMed:27558840). Shows
CC agglutinating activity towards erythrocytes from rabbit (By
CC similarity). {ECO:0000250|UniProtKB:R9RL27,
CC ECO:0000269|PubMed:27558840}.
CC -!- SUBUNIT: Forms heterotetramer of 2 chains 1 and 2 chains 2 arranged as
CC a dimer of chain 1 and chain 2 heterodimers.
CC {ECO:0000250|UniProtKB:R9RL27}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ32294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF541132; ABQ32294.1; ALT_SEQ; Genomic_DNA.
DR PDB; 5T1X; X-ray; 1.70 A; A/C/E/G=24-133.
DR PDB; 5T20; X-ray; 1.91 A; A/C/E/G/I/K/M/O=24-133.
DR PDBsum; 5T1X; -.
DR PDBsum; 5T20; -.
DR AlphaFoldDB; A5HMM7; -.
DR SMR; A5HMM7; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 2.
DR Gene3D; 2.90.10.10; -; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR SMART; SM00108; B_lectin; 2.
DR SUPFAM; SSF51110; SSF51110; 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hemagglutinin; Lectin; Mannose-binding;
KW Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..139
FT /note="Mannose-specific lectin 2 chain 1"
FT /id="PRO_5002683074"
FT CHAIN 140..261
FT /note="Mannose-specific lectin 2 chain 2"
FT /id="PRO_0000450779"
FT DOMAIN 26..131
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 145..252
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT MOTIF 51..59
FT /note="Carbohydrate-binding motif 1"
FT /evidence="ECO:0000305|PubMed:27558840"
FT MOTIF 170..178
FT /note="Carbohydrate-binding motif 2"
FT /evidence="ECO:0000305|PubMed:27558840"
FT BINDING 51..55
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT BINDING 59
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT BINDING 63
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:R9RL27"
FT BINDING 64
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT BINDING 170..174
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:R9RL27"
FT BINDING 178
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:Q39487"
FT BINDING 182..185
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:Q39487"
FT DISULFID 54..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|PubMed:27558840, ECO:0007744|PDB:5T1X,
FT ECO:0007744|PDB:5T20"
FT DISULFID 173..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ SEQUENCE 261 AA; 28743 MW; B514B8B232FBF76D CRC64;
MAKLLLFLLP AILGLLIPRS AVALGTNYLL SGQTLNTDGH LKNGDFDLVM QNDCNLVLYN
GNWQSNTANN GRDCKLTLTD YGELVIKNGD GSTVWRSRAK SVKGNYAAVL HPDGRLVVFG
PSVFKIDPWV PGLNSLRFRN IPFTDNLLFS GQVLYGDGRL TAKNHQLVMQ GDCNLVLYGG
KYGWQSNTHG NGEHCFLRLN HKGELIIKDD DFRTIWSSSS SSKQGDYVLI LQDDGFAVIY
GPAIWETSSK RSIADVGEDD G
