CEA_COLES
ID CEA_COLES Reviewed; 264 AA.
AC R9RL27;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Mannose-specific lectin CEA {ECO:0000305};
DE AltName: Full=Agglutinin CEA {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin CEA chain 1 {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin CEA chain 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=CEA {ECO:0000303|Ref.1};
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, AND BIOTECHNOLOGY.
RX DOI=10.4236/ajps.2013.42A053;
RA Das A., Roy A., Hess D., Das S.;
RT "Characterization of a highly potent insecticidal lectin from Colocasia
RT esculenta tuber and cloning of its coding sequence.";
RL Am. J. Plant Sci. 4:408-416(2013).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 24-132 AND 140-250 IN COMPLEX
RP WITH BETA-D-MANNOSE, DISULFIDE BONDS, AND SUBUNIT.
RX DOI=10.4172/2168-958X.1000126;
RA Chattopadhyaya R., Biswas H., Sarkar A.;
RT "Crystal structure of Colocasia esculenta tuber agglutinin at 1.74 A
RT resolution and its quaternary interactions.";
RL J. Glycobiol. 6:1000126-1000126(2017).
CC -!- FUNCTION: Mannose-specific lectin (Ref.1). Shows agglutinating activity
CC towards erythrocytes from rabbit (Ref.1). Has insecticidal activity
CC against cotton aphids and other hemipteran insects (Ref.1).
CC {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Forms heterotetramer of 2 chains 1 and 2 chains 2 arranged as
CC a dimer of chain 1 and chain 2 heterodimers. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- BIOTECHNOLOGY: May be used as a potent insecticidal agent against
CC hemipteran insects. {ECO:0000305|Ref.1}.
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DR EMBL; JX435122; AGM50056.1; -; Genomic_DNA.
DR PDB; 5D5G; X-ray; 1.74 A; A/C=24-132, B/D=140-250.
DR PDB; 5D9Z; X-ray; 1.85 A; A=24-132, B=140-251.
DR PDBsum; 5D5G; -.
DR PDBsum; 5D9Z; -.
DR AlphaFoldDB; R9RL27; -.
DR SMR; R9RL27; -.
DR UniLectin; R9RL27; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; Magnesium;
KW Mannose-binding; Metal-binding; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..139
FT /note="Mannose-specific lectin CEA chain 1"
FT /id="PRO_5004489017"
FT CHAIN 140..264
FT /note="Mannose-specific lectin CEA chain 2"
FT /id="PRO_0000450780"
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|Ref.1"
FT MOTIF 170..178
FT /note="Carbohydrate-binding motif 2"
FT /evidence="ECO:0000305|Ref.1"
FT BINDING 51..55
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 59
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 63
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:5D9Z"
FT BINDING 64
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 170..174
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:5D9Z"
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|Ref.2, ECO:0007744|PDB:5D5G,
FT ECO:0007744|PDB:5D9Z"
FT DISULFID 173..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5D5G,
FT ECO:0007744|PDB:5D9Z"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5D5G"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:5D5G"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5D9Z"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5D5G"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5D9Z"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5D5G"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5D5G"
SQ SEQUENCE 264 AA; 29134 MW; 2FE83835FF5B7D60 CRC64;
MAKLLLFLLP AILGLLVPRS AVALGTNYLL SGQTLDREGH LKNGDFDLVM QDDCNLVLYN
GNWQSNTANK GRDCKLTLTD YGELVIKNGD GSTVWRSRAQ SVKGNYAAVV HPDGRLVVFG
PSVFKIDPWV PGLNSLRFRN IPFTNNLLFS GQVLYGDGRL TAKSHQLVMQ GDCNLVLYGG
KYGWQSNTHG NGEHCFLRLN HKGELIIKDD DFKTIWSSSS SSKHGDYVLI LRDDGFAVIY
GPAIWETSPQ AKEKMIGMVT AGKL
