LEC2_ULEEU
ID LEC2_ULEEU Reviewed; 249 AA.
AC P22973;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Anti-H(O) lectin 2;
DE AltName: Full=Anti-H(O) lectin II;
DE AltName: Full=UEA-II;
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, AND GLYCOSYLATION AT ASN-245.
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 1-36.
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: Di-N-acetylchitobiose specific lectin.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; JX0163; JX0163.
DR PDB; 1QNW; X-ray; 2.35 A; A/B/C/D=1-245.
DR PDBsum; 1QNW; -.
DR AlphaFoldDB; P22973; -.
DR SMR; P22973; -.
DR UniLectin; P22973; -.
DR iPTMnet; P22973; -.
DR EvolutionaryTrace; P22973; -.
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..249
FT /note="Anti-H(O) lectin 2"
FT /id="PRO_0000105112"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1869520"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1869520"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1QNW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1QNW"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1QNW"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1QNW"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1QNW"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1QNW"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1QNW"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:1QNW"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1QNW"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:1QNW"
SQ SEQUENCE 249 AA; 26928 MW; DFA7FEFCC4A7A64E CRC64;
NLSDDLSFNF DKFVPNQKNI IFQGDASVST KGVLEVTKVS KPTTRSIGRA LYAAPIQIWD
SITGKVASFA TSFSFVVKDE PDEKIDGVDG LAFFLAPANS QIPSGSSAGM FGLFCSSNDS
KSSNQIIAVE FDSYFGKTYN PWDPDFKHIG IDVNSIKSIK TVKDDWRNGE VADVVITYRA
PTKSLTVSLS YPSDGTSNIV TASSVDLKAI LPEWVSVGFS GGVGNAAKFD HDVLSWYFTS
NLEANQSQT
