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P19588 (LEC5_VIGUC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1.

Subunit structure

Heterodimer, composed of an alpha and a beta subunit derived from a single precursor.

Post-translational modification

Leu-264 is missing in a major portion of the beta subunit, suggesting an origin by sequential removal of amino acids rather than a processing by endoproteolytic cleavage.

Sequence similarities

Belongs to the leguminous lectin family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Lectin
Mannose-binding
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionmannose binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 275253Lectin DB58 subunit alpha
PRO_0000017613
Chain23 – 264242Lectin DB58 subunit beta
PRO_0000017614

Amino acid modifications

Glycosylation341N-linked (GlcNAc...)
Glycosylation1011N-linked (GlcNAc...)

Experimental info

Sequence conflict236 – 2372LS → FF in AAA33142. Ref.1

Secondary structure

........................................ 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19588 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 53D72ACB02EAE03F

FASTA27529,453
        10         20         30         40         50         60 
MASSTVSVVL SLFLLLLTQA YSADIQSFSF KNFNSSSFIL QGDATVSSSK LRLTKVKGNG 

        70         80         90        100        110        120 
LPTLSSLGRA FYSSPIQIYD KSTGAVASWA TSFTANIFAP NKSSSADGIA FALVPVGSEP 

       130        140        150        160        170        180 
KSNSGFLGVF DSDVYDNSAQ TVAVEFDTFS NTDWDPTSRH IGIDVNSIKS IRTASWGLAN 

       190        200        210        220        230        240 
GQNAEILITY NAATSLLVAS LVHPSRRTSY IVSERVDITN ELPEYVSIGF SATTGLSEGY 

       250        260        270 
TETHDVLSWS FASKLPDDST TEPLDIASYL VRNVL 

« Hide

References

[1]"cDNA cloning, primary structure, and in vitro biosynthesis of the DB58 lectin from Dolichos biflorus."
Schnell D.J., Etzler M.E.
J. Biol. Chem. 263:14648-14653(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Two lectin genes differentially expressed in Dolichos biflorus differ primarily by a 116-base pair sequence in their 5' flanking regions."
Harada J.J., Spadoro-Tank J., Maxwell J.C., Schnell D.J., Etzler M.E.
J. Biol. Chem. 265:4997-5001(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and characterization of subunits of DB58, a lectin from the stems and leaves of Dolichos biflorus."
Etzler M.E.
Biochemistry 33:9778-9783(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 255-275, PROTEOLYTIC PROCESSING.
Tissue: Leaf and Stem.
[4]"Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus."
Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.-H., Strecker G., Imberty A., Fernandez E., Wyns L., Etzler M.E.
J. Mol. Biol. 286:1161-1177(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23216 mRNA. Translation: AAA33142.1.
M34271 Genomic DNA. Translation: AAA33140.1.
PIRA31972.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G7YX-ray2.50A/B/C/D/E/F23-275[»]
1LULX-ray3.30A/B/C/D/E/F23-275[»]
ProteinModelPortalP19588.
SMRP19588. Positions 23-275.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19588.

Entry information

Entry nameLEC5_VIGUC
AccessionPrimary (citable) accession number: P19588
Secondary accession number(s): Q39665
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references