LEC1_COLES
ID LEC1_COLES Reviewed; 267 AA.
AC Q39487;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mannose-specific lectin 1 {ECO:0000305};
DE AltName: Full=Agglutinin {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 1 chain 1 {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 1 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 [MRNA], AND PROTEIN SEQUENCE OF 27-36 AND 143-152.
RC TISSUE=Tuber;
RX PubMed=8251188; DOI=10.1266/jjg.68.229;
RA Hirai M., Nakamura K., Imai T., Sato T.;
RT "cDNAs encoding for storage proteins in the tubers of taro (Colocasia
RT esculenta Schott).";
RL Jpn. J. Genet. 68:229-236(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-135 AND 143-253, AND DISULFIDE
RP BONDS.
RX PubMed=27262515; DOI=10.1016/j.ijbiomac.2016.05.048;
RA Vajravijayan S., Pletnev S., Pletnev V.Z., Nandhagopal N., Gunasekaran K.;
RT "Structural analysis of beta-prism lectin from Colocasia esculenta (L.) S
RT chott.";
RL Int. J. Biol. Macromol. 91:518-523(2016).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 143-251 IN COMPLEX WITH
RP BETA-D-MANNOSE, DISULFIDE BONDS, FUNCTION, AND SUBUNIT.
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:0000269|PubMed:27558840}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03722.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D16173; BAA03722.1; ALT_FRAME; mRNA.
DR PDB; 5J76; X-ray; 2.10 A; A=27-135, B=143-253.
DR PDB; 5T1X; X-ray; 1.70 A; B/D/F/H=143-251.
DR PDB; 5T20; X-ray; 1.91 A; B/D/F/H/J/L/N/P=143-251.
DR PDBsum; 5J76; -.
DR PDBsum; 5T1X; -.
DR PDBsum; 5T20; -.
DR AlphaFoldDB; Q39487; -.
DR SMR; Q39487; -.
DR UniLectin; Q39487; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Direct protein sequencing; Disulfide bond; Hemagglutinin;
KW Lectin; Mannose-binding; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8251188"
FT CHAIN 27..143
FT /note="Mannose-specific lectin 1 chain 1"
FT /id="PRO_0000450777"
FT CHAIN 144..267
FT /note="Mannose-specific lectin 1 chain 2"
FT /id="PRO_0000450778"
FT DOMAIN 29..134
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 148..255
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT MOTIF 54..62
FT /note="Carbohydrate-binding motif 1"
FT /evidence="ECO:0000305|PubMed:27262515"
FT MOTIF 173..181
FT /note="Carbohydrate-binding motif 2"
FT /evidence="ECO:0000305|PubMed:27262515"
FT BINDING 54..58
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 62
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 66
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:R9RL27"
FT BINDING 67
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 173..177
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT BINDING 181
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT BINDING 185..188
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000269|PubMed:27558840,
FT ECO:0007744|PDB:5T20"
FT DISULFID 57..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|PubMed:27262515, ECO:0007744|PDB:5J76"
FT DISULFID 176..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|PubMed:27262515, ECO:0007744|PDB:5J76"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5J76"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5J76"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5J76"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5J76"
SQ SEQUENCE 267 AA; 29317 MW; DBF4E89D25F3D3E0 CRC64;
MAKLLLFLLP AILGLLVPPR SWSAVALGTN YLLSGQTLET EGHLKNGDFD LVMQDDCNLV
LYNGNWQSNT ANKGRDCKLT LTDHGELVIN NGDGSTVWRS GAQSVKGDYA AVVHPEGRLV
VFSPSVFKID PSVPGLNSLR FRNIPFTNNL LFSGQVLYGD GRLTAKNHQL VMQGDCNLVL
YGGKYGWQSN THGNGEHCFL RLNHKGELII EDDDFKTIWS SSYSSKQGDY VLILRDDGVA
VIYGPAIWET SPQAKEKMIG MVTAGKL
