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P05045 (LEC1_VIGUC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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

Names and origin

Protein namesRecommended name:
Seed lectin subunit I

Short name=SL

Cleaved into the following chain:

  1. Seed lectin subunit II
OrganismVigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
Taxonomic identifier3840 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

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. Has a high preference for GalNAc over Gal.

Subunit structure

Homotetramer.

Post-translational modification

Subunit II may arise from subunit I by proteolytic cleavage at the C-terminal end.

Sequence similarities

Belongs to the leguminous lectin family.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Lectin
Mannose-binding
   PTMGlycoprotein
   Technical term3D-structure
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 – 275253Seed lectin subunit I
PRO_0000017611
Chain23 – 265243Seed lectin subunit II
PRO_0000017612

Sites

Site265 – 2662Cleavage

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict61 – 677IPTPSSL → FPLRFPS in AAA33141. Ref.1
Sequence conflict821S → F in AAA33141. Ref.1
Sequence conflict1491F → L in AAA33141. Ref.1
Sequence conflict1991A → V in AAA33141. Ref.1
Sequence conflict2271S → G in AAA33141. Ref.1
Sequence conflict2541K → R in AAA33141. Ref.1
Sequence conflict2681S → R in AAA33141. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P05045 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: D313D73860661A83

FASTA27529,406
        10         20         30         40         50         60 
MASSTVSVVL SLFLLLLTQA NSANIQSFSF KNFNSPSFIL QGDATVSSGK LQLTKVKENG 

        70         80         90        100        110        120 
IPTPSSLGRA FYSSPIQIYD KSTGAVASWA TSFTVKISAP SKASFADGIA FALVPVGSEP 

       130        140        150        160        170        180 
RRNGGYLGVF DSDVYNNSAQ TVAVEFDTFS NSGWDPSMKH IGIDVNSIKS IATVSWDLAN 

       190        200        210        220        230        240 
GENAEILITY NAATSLLVAS LVHPSRRTSY ILSERVDITN ELPEYVSVGF SATTGLSEGY 

       250        260        270 
IETHDVLSWS FASKLPDDST AEPLDLASYL VRNVL 

« Hide

References

[1]"Primary structure of the Dolichos biflorus seed lectin."
Schnell D.J., Etzler M.E.
J. Biol. Chem. 262:7220-7225(1987) [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]"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 (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02721 mRNA. Translation: AAA33141.1.
M34270 Genomic DNA. Translation: AAA33143.1.
PIRA29572.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJQX-ray2.65A/B/C/D/E/F/G/H23-275[»]
1LU1X-ray2.60A23-275[»]
1LU2X-ray2.80A/B23-275[»]
ProteinModelPortalP05045.
SMRP05045. Positions 23-275.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00173. Adenine.

Protein family/group databases

Allergome3011. Dol b Agglutinin.

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

EvolutionaryTraceP05045.

Entry information

Entry nameLEC1_VIGUC
AccessionPrimary (citable) accession number: P05045
Secondary accession number(s): Q39666
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 83 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