LEC_SOYBN
ID LEC_SOYBN Reviewed; 285 AA.
AC P05046;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lectin;
DE AltName: Full=Agglutinin;
DE AltName: Full=SBA;
DE Flags: Precursor;
GN Name=LE1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6313203; DOI=10.1016/0092-8674(83)90560-3;
RA Vodkin L.O., Rhodes P.R., Goldberg R.B.;
RT "cA lectin gene insertion has the structural features of a transposable
RT element.";
RL Cell 34:1023-1031(1983).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=7711015; DOI=10.1021/bi00015a004;
RA Dessen A., Gupta D., Sabesan S., Brewer C.F., Sacchettini J.C.;
RT "X-ray crystal structure of the soybean agglutinin cross-linked with a
RT biantennary analog of the blood group I carbohydrate antigen.";
RL Biochemistry 34:4933-4942(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS).
RX PubMed=9398234; DOI=10.1021/bi971828+;
RA Olsen L.R., Dessen A., Gupta D., Sabesan S., Sacchettini J.C., Brewer C.F.;
RT "X-ray crystallographic studies of unique cross-linked lattices between
RT four isomeric biantennary oligosaccharides and soybean agglutinin.";
RL Biochemistry 36:15073-15080(1997).
CC -!- FUNCTION: Binds GalNAc and galactose.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; K00821; AAA33983.1; -; Genomic_DNA.
DR PIR; S27365; S27365.
DR RefSeq; XP_003518800.1; XM_003518752.3.
DR PDB; 1G9F; X-ray; 2.50 A; A=33-285.
DR PDB; 1SBD; X-ray; 2.52 A; A=33-285.
DR PDB; 1SBE; X-ray; 2.80 A; A=33-285.
DR PDB; 1SBF; X-ray; 2.43 A; A=33-285.
DR PDB; 2SBA; X-ray; 2.60 A; A=33-285.
DR PDB; 4D69; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=33-285.
DR PDBsum; 1G9F; -.
DR PDBsum; 1SBD; -.
DR PDBsum; 1SBE; -.
DR PDBsum; 1SBF; -.
DR PDBsum; 2SBA; -.
DR PDBsum; 4D69; -.
DR AlphaFoldDB; P05046; -.
DR SMR; P05046; -.
DR IntAct; P05046; 1.
DR STRING; 3847.GLYMA02G01590.1; -.
DR ChEMBL; CHEMBL1649056; -.
DR Allergome; 1429; Gly m Agglutinin.
DR UniLectin; P05046; -.
DR GlyConnect; 333; 5 N-Linked glycans.
DR PRIDE; P05046; -.
DR EnsemblPlants; KRH69220; KRH69220; GLYMA_02G012600.
DR Gramene; KRH69220; KRH69220; GLYMA_02G012600.
DR eggNOG; ENOG502QTX3; Eukaryota.
DR HOGENOM; CLU_000288_62_2_1; -.
DR InParanoid; P05046; -.
DR OMA; YNESHDI; -.
DR OrthoDB; 1377709at2759; -.
DR EvolutionaryTrace; P05046; -.
DR PRO; PR:P05046; -.
DR Proteomes; UP000008827; Chromosome 2.
DR Genevisible; P05046; GM.
DR GO; GO:0030246; F:carbohydrate 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; Glycoprotein; Lectin; Reference proteome; Signal.
FT SIGNAL 1..32
FT CHAIN 33..285
FT /note="Lectin"
FT /id="PRO_0000017647"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2SBA"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1SBD"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1SBF"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:1SBF"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1SBE"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:1SBF"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1SBF"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4D69"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 167..179
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1SBF"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:1SBF"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1SBF"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 234..244
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1SBF"
FT STRAND 252..264
FT /evidence="ECO:0007829|PDB:1SBF"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:1G9F"
SQ SEQUENCE 285 AA; 30928 MW; B3704533C9315C52 CRC64;
MATSKLKTQN VVVSLSLTLT LVLVLLTSKA NSAETVSFSW NKFVPKQPNM ILQGDAIVTS
SGKLQLNKVD ENGTPKPSSL GRALYSTPIH IWDKETGSVA SFAASFNFTF YAPDTKRLAD
GLAFFLAPID TKPQTHAGYL GLFNENESGD QVVAVEFDTF RNSWDPPNPH IGINVNSIRS
IKTTSWDLAN NKVAKVLITY DASTSLLVAS LVYPSQRTSN ILSDVVDLKT SLPEWVRIGF
SAATGLDIPG ESHDVLSWSF ASNLPHASSN IDPLDLTSFV LHEAI
