LEC1_VIGUC
ID LEC1_VIGUC Reviewed; 275 AA.
AC P05045; Q39666;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Seed lectin subunit I;
DE Short=SL;
DE Contains:
DE RecName: Full=Seed lectin subunit II;
DE Flags: Precursor;
OS Vigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus).
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; Vigna.
OX NCBI_TaxID=3840;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3584113; DOI=10.1016/s0021-9258(18)48226-9;
RA Schnell D.J., Etzler M.E.;
RT "Primary structure of the Dolichos biflorus seed lectin.";
RL J. Biol. Chem. 262:7220-7225(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2318879; DOI=10.1016/s0021-9258(19)34074-8;
RA Harada J.J., Spadoro-Tank J., Maxwell J.C., Schnell D.J., Etzler M.E.;
RT "Two lectin genes differentially expressed in Dolichos biflorus differ
RT primarily by a 116-base pair sequence in their 5' flanking regions.";
RL J. Biol. Chem. 265:4997-5001(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10047489; DOI=10.1006/jmbi.1998.2534;
RA Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.-H., Strecker G.,
RA Imberty A., Fernandez E., Wyns L., Etzler M.E.;
RT "Carbohydrate binding, quaternary structure and a novel hydrophobic binding
RT site in two legume lectin oligomers from Dolichos biflorus.";
RL J. Mol. Biol. 286:1161-1177(1999).
CC -!- FUNCTION: Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the
CC carbohydrates galactose, glucosamine, mannose, and fucose. It
CC agglutinates erythrocytes of blood group A1. Has a high preference for
CC GalNAc over Gal.
CC -!- SUBUNIT: Homotetramer.
CC -!- PTM: Subunit II may arise from subunit I by proteolytic cleavage at the
CC C-terminal end.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02721; AAA33141.1; -; mRNA.
DR EMBL; M34270; AAA33143.1; -; Genomic_DNA.
DR PIR; A29572; A29572.
DR PDB; 1BJQ; X-ray; 2.65 A; A/B/C/D/E/F/G/H=23-275.
DR PDB; 1LU1; X-ray; 2.60 A; A=23-275.
DR PDB; 1LU2; X-ray; 2.80 A; A/B=23-275.
DR PDBsum; 1BJQ; -.
DR PDBsum; 1LU1; -.
DR PDBsum; 1LU2; -.
DR AlphaFoldDB; P05045; -.
DR SMR; P05045; -.
DR Allergome; 3011; Dol b Agglutinin.
DR UniLectin; P05045; -.
DR EvolutionaryTrace; P05045; -.
DR GO; GO:0005537; F:mannose 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; Glycoprotein; Lectin; Mannose-binding; Signal.
FT SIGNAL 1..22
FT CHAIN 23..275
FT /note="Seed lectin subunit I"
FT /id="PRO_0000017611"
FT CHAIN 23..265
FT /note="Seed lectin subunit II"
FT /id="PRO_0000017612"
FT SITE 265..266
FT /note="Cleavage"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 61..67
FT /note="IPTPSSL -> FPLRFPS (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="S -> F (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="F -> L (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> V (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> G (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="K -> R (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> R (in Ref. 1; AAA33141)"
FT /evidence="ECO:0000305"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1LU1"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1LU1"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1LU1"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1LU1"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1LU1"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1LU1"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1LU1"
SQ SEQUENCE 275 AA; 29406 MW; D313D73860661A83 CRC64;
MASSTVSVVL SLFLLLLTQA NSANIQSFSF KNFNSPSFIL QGDATVSSGK LQLTKVKENG
IPTPSSLGRA FYSSPIQIYD KSTGAVASWA TSFTVKISAP SKASFADGIA FALVPVGSEP
RRNGGYLGVF DSDVYNNSAQ TVAVEFDTFS NSGWDPSMKH IGIDVNSIKS IATVSWDLAN
GENAEILITY NAATSLLVAS LVHPSRRTSY ILSERVDITN ELPEYVSVGF SATTGLSEGY
IETHDVLSWS FASKLPDDST AEPLDLASYL VRNVL
