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P02872 (LECG_ARAHY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. 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:
Galactose-binding lectin
Alternative name(s):
Agglutinin
PNA
OrganismArachis hypogaea (Peanut)
Taxonomic identifier3818 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeDalbergieaeArachis

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

D-galactose specific lectin.

Subunit structure

Homotetramer.

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

Sequence similarities

Belongs to the leguminous lectin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.2
Chain24 – 273250Galactose-binding lectin
PRO_0000017583

Sites

Metal binding1441Manganese
Metal binding1461Calcium
Metal binding1461Manganese
Metal binding1481Calcium; via carbonyl oxygen
Metal binding1501Calcium
Metal binding1551Calcium
Metal binding1551Manganese
Metal binding1601Manganese

Natural variations

Natural variant1151E → V in minor form.
Natural variant1721K → A in minor form.
Natural variant1851K → I in minor form.
Natural variant235 – 2362LG → RA in minor form.

Secondary structure

.............................................. 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02872 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 05A0B1A8FAC7B159

FASTA27329,325
        10         20         30         40         50         60 
MKPFCVFLTF FLLLAASSKK VDSAETVSFN FNSFSEGNPA INFQGDVTVL SNGNIQLTNL 

        70         80         90        100        110        120 
NKVNSVGRVL YAMPVRIWSS ATGNVASFLT SFSFEMKDIK DYDPADGIIF FIAPEDTQIP 

       130        140        150        160        170        180 
AGSIGGGTLG VSDTKGAGHF VGVEFDTYSN SEYNDPPTDH VGIDVNSVDS VKTVPWNSVS 

       190        200        210        220        230        240 
GAVVKVTVIY DSSTKTLSVA VTNDNGDITT IAQVVDLKAK LPERVKFGFS ASGSLGGRQI 

       250        260        270 
HLIRSWSFTS TLITTTRRSI DNNEKKIMNM ASA 

« Hide

References

[1]"Cloning, sequence analysis and expression in Escherichia coli of the cDNA encoding a precursor of peanut agglutinin."
Rodriguez-Arango E., Arango R., Adar R., Galili G., Sharon N.
FEBS Lett. 307:185-189(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Seed.
[2]"The amino acid sequence of peanut agglutinin."
Young N.M., Johnston R.A.Z., Watson D.C.
Eur. J. Biochem. 196:631-637(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-273.
Tissue: Seed.
[3]"Sequence studies of peanut agglutinin."
Lauwereys M., Foriers A., Sharon N., Strosberg A.D.
FEBS Lett. 181:241-244(1985)
Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
Strain: cv. Shulamit.
[4]"Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex."
Banerjee R., Das K., Ravishankar R., Suguna K., Surolia A., Vijayan M.
J. Mol. Biol. 259:281-296(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[5]"Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins."
Ravishankar R., Suguna K., Surolia A., Vijayan M.
Acta Crystallogr. D 55:1375-1382(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S42352 mRNA. Translation: AAB22817.1.
PIRLNNPG. A03364.
S24044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZWX-ray2.70A/B/C/D24-255[»]
1CIWX-ray2.70A/B/C/D24-259[»]
1CQ9X-ray3.50A/B/C/D24-259[»]
1CR7X-ray2.60A/B/C/D/E/F/G/H24-259[»]
1QF3X-ray2.80A/B/C/D24-259[»]
1RIRX-ray2.90A/B/C/D24-259[»]
1RITX-ray2.85A/B/C/D24-259[»]
1V6IX-ray2.15A/B/C/D24-255[»]
1V6JX-ray2.90A/B/C/D24-255[»]
1V6KX-ray2.40A/B/C/D24-255[»]
1V6LX-ray2.50A/B/C/D24-255[»]
1V6MX-ray2.70A/B/C/D/E/F/G/H24-255[»]
1V6NX-ray3.50A/B/C/D/E/F/G/H24-255[»]
1V6OX-ray3.00A/B/C/D/E/F/G/H24-255[»]
2DH1X-ray7.65A/B/C/D24-259[»]
2DV9X-ray2.48A/B/C/D24-259[»]
2DVAX-ray2.20A/B/C/D24-259[»]
2DVBX-ray2.25A/B/C/D24-259[»]
2DVDX-ray2.25A/B/C/D24-259[»]
2DVFX-ray2.74A/B/C/D24-259[»]
2DVGX-ray2.78A/B/C/D24-259[»]
2PELX-ray2.25A/B/C/D24-259[»]
2TEPX-ray2.50A/B/C/D24-259[»]
ProteinModelPortalP02872.
SMRP02872. Positions 24-255.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1050. Ara h 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

EvolutionaryTraceP02872.

Entry information

Entry nameLECG_ARAHY
AccessionPrimary (citable) accession number: P02872
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 101 of the entry and version 3 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