LEC1_ULEEU
ID LEC1_ULEEU Reviewed; 243 AA.
AC P22972;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Anti-H(O) lectin 1;
DE AltName: Full=Anti-H(O) lectin I;
DE AltName: Full=UEA-I;
OS Ulex europaeus (Furze).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Ulex.
OX NCBI_TaxID=3902;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=1869520; DOI=10.1093/oxfordjournals.jbchem.a123435;
RA Konami Y., Yamamoto K., Osawa T.;
RT "The primary structures of two types of the Ulex europeus seed lectin.";
RL J. Biochem. 109:650-658(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-34.
RX PubMed=1859632; DOI=10.1515/bchm3.1991.372.1.95;
RA Konami Y., Yamamoto K., Osawa T.;
RT "Purification and characterization of a new type lactose-binding Ulex
RT europaeus lectin by affinity chromatography.";
RL Biol. Chem. Hoppe-Seyler 372:95-102(1991).
CC -!- FUNCTION: L-fucose specific lectin.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; JX0162; JX0162.
DR PDB; 1FX5; X-ray; 2.20 A; A/B=1-242.
DR PDB; 1JXN; X-ray; 2.30 A; A/B/C/D=1-243.
DR PDBsum; 1FX5; -.
DR PDBsum; 1JXN; -.
DR AlphaFoldDB; P22972; -.
DR SMR; P22972; -.
DR UniLectin; P22972; -.
DR iPTMnet; P22972; -.
DR EvolutionaryTrace; P22972; -.
DR GO; GO:0030246; F:carbohydrate 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 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin;
KW Manganese; Metal-binding.
FT CHAIN 1..243
FT /note="Anti-H(O) lectin 1"
FT /id="PRO_0000105111"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1869520"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1869520"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:1FX5"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 67..80
FT /evidence="ECO:0007829|PDB:1FX5"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1FX5"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1FX5"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1FX5"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1FX5"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1FX5"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:1FX5"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1FX5"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1FX5"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:1FX5"
FT STRAND 225..239
FT /evidence="ECO:0007829|PDB:1FX5"
SQ SEQUENCE 243 AA; 26670 MW; 74F2D74A8A2CF8E1 CRC64;
SDDLSFKFKN FSQNGKDLSF QGDASVIETG VLQLNKVGNN LPDETGGIAR YIAPIHIWNC
NTGEVASFIT SFSFFMETSA NPKAATDGLT FFLAPPDSPL RRAGGYFGLF EDTKDNDSSY
QTVAVEFDTI GSPVNFDDPG FPHIGIDVNR VKSINAERWN KRYGLNNVAN VEIIYEASSK
TLTASLTYPS DQTSISVTSI VDLKEILPEW VSVGFSGGTY IGRQATHEVL NWYFTSNLIN
TNS
