LEC5_VIGUC
ID LEC5_VIGUC Reviewed; 275 AA.
AC P19588; Q39665;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Lectin DB58;
DE Contains:
DE RecName: Full=Lectin DB58 subunit alpha;
DE Contains:
DE RecName: Full=Lectin DB58 subunit beta;
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=2844781; DOI=10.1016/s0021-9258(18)68086-x;
RA Schnell D.J., Etzler M.E.;
RT "cDNA cloning, primary structure, and in vitro biosynthesis of the DB58
RT lectin from Dolichos biflorus.";
RL J. Biol. Chem. 263:14648-14653(1988).
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 PROTEIN SEQUENCE OF 255-275, AND PROTEOLYTIC PROCESSING.
RC TISSUE=Leaf, and Stem;
RX PubMed=8068657; DOI=10.1021/bi00198a049;
RA Etzler M.E.;
RT "Isolation and characterization of subunits of DB58, a lectin from the
RT stems and leaves of Dolichos biflorus.";
RL Biochemistry 33:9778-9783(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 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.
CC -!- SUBUNIT: Heterodimer, composed of an alpha and a beta subunit derived
CC from a single precursor.
CC -!- PTM: Leu-264 is missing in a major portion of the beta subunit,
CC suggesting an origin by sequential removal of amino acids rather than a
CC processing by endoproteolytic cleavage. {ECO:0000269|PubMed:8068657}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; M23216; AAA33142.1; -; mRNA.
DR EMBL; M34271; AAA33140.1; -; Genomic_DNA.
DR PIR; A31972; A31972.
DR PDB; 1G7Y; X-ray; 2.50 A; A/B/C/D/E/F=23-275.
DR PDB; 1LUL; X-ray; 3.30 A; A/B/C/D/E/F=23-275.
DR PDBsum; 1G7Y; -.
DR PDBsum; 1LUL; -.
DR AlphaFoldDB; P19588; -.
DR SMR; P19588; -.
DR UniLectin; P19588; -.
DR EvolutionaryTrace; P19588; -.
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; Direct protein sequencing; Glycoprotein; Lectin;
KW Mannose-binding; Signal.
FT SIGNAL 1..22
FT CHAIN 23..275
FT /note="Lectin DB58 subunit alpha"
FT /id="PRO_0000017613"
FT CHAIN 23..264
FT /note="Lectin DB58 subunit beta"
FT /id="PRO_0000017614"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 236..237
FT /note="LS -> FF (in Ref. 1; AAA33142)"
FT /evidence="ECO:0000305"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1LUL"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1LUL"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1LUL"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1LUL"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:1LUL"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:1LUL"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1LUL"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:1LUL"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:1LUL"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1LUL"
SQ SEQUENCE 275 AA; 29453 MW; 53D72ACB02EAE03F CRC64;
MASSTVSVVL SLFLLLLTQA YSADIQSFSF KNFNSSSFIL QGDATVSSSK LRLTKVKGNG
LPTLSSLGRA FYSSPIQIYD KSTGAVASWA TSFTANIFAP NKSSSADGIA FALVPVGSEP
KSNSGFLGVF DSDVYDNSAQ TVAVEFDTFS NTDWDPTSRH IGIDVNSIKS IRTASWGLAN
GQNAEILITY NAATSLLVAS LVHPSRRTSY IVSERVDITN ELPEYVSIGF SATTGLSEGY
TETHDVLSWS FASKLPDDST TEPLDIASYL VRNVL
