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P02872

- LECG_ARAHY

UniProt

P02872 - LECG_ARAHY

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Protein
Galactose-binding lectin
Gene
N/A
Organism
Arachis hypogaea (Peanut)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

D-galactose specific lectin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi144 – 1441Manganese
Metal bindingi146 – 1461Calcium
Metal bindingi146 – 1461Manganese
Metal bindingi148 – 1481Calcium; via carbonyl oxygen
Metal bindingi150 – 1501Calcium
Metal bindingi155 – 1551Calcium
Metal bindingi155 – 1551Manganese
Metal bindingi160 – 1601Manganese

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Galactose-binding lectin
Alternative name(s):
Agglutinin
PNA
OrganismiArachis hypogaea (Peanut)
Taxonomic identifieri3818 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeDalbergieaeArachis

Pathology & Biotechi

Protein family/group databases

Allergomei1050. Ara h Agglutinin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 273250Galactose-binding lectin
PRO_0000017583Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 339
Beta strandi41 – 466
Beta strandi51 – 533
Beta strandi60 – 645
Beta strandi66 – 738
Turni80 – 823
Beta strandi87 – 9711
Beta strandi100 – 1034
Beta strandi107 – 1148
Helixi126 – 1283
Turni129 – 1313
Beta strandi136 – 14611
Helixi151 – 1533
Beta strandi160 – 16910
Beta strandi171 – 1755
Beta strandi183 – 1919
Turni192 – 1954
Beta strandi196 – 2027
Beta strandi204 – 2063
Beta strandi208 – 2147
Helixi217 – 2204
Beta strandi223 – 23210
Beta strandi235 – 2373
Beta strandi240 – 25213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP02872.
SMRiP02872. Positions 24-255.

Miscellaneous databases

EvolutionaryTraceiP02872.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. 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]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02872-1 [UniParc]FASTAAdd to Basket

« Hide

MKPFCVFLTF FLLLAASSKK VDSAETVSFN FNSFSEGNPA INFQGDVTVL    50
SNGNIQLTNL NKVNSVGRVL YAMPVRIWSS ATGNVASFLT SFSFEMKDIK 100
DYDPADGIIF FIAPEDTQIP AGSIGGGTLG VSDTKGAGHF VGVEFDTYSN 150
SEYNDPPTDH VGIDVNSVDS VKTVPWNSVS GAVVKVTVIY DSSTKTLSVA 200
VTNDNGDITT IAQVVDLKAK LPERVKFGFS ASGSLGGRQI HLIRSWSFTS 250
TLITTTRRSI DNNEKKIMNM ASA 273
Length:273
Mass (Da):29,325
Last modified:October 1, 1996 - v3
Checksum:i05A0B1A8FAC7B159
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151E → V in minor form.
Natural varianti172 – 1721K → A in minor form.
Natural varianti185 – 1851K → I in minor form.
Natural varianti235 – 2362LG → RA in minor form.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S42352 mRNA. Translation: AAB22817.1.
PIRiA03364. LNNPG.
S24044.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S42352 mRNA. Translation: AAB22817.1 .
PIRi A03364. LNNPG.
S24044.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BZW X-ray 2.70 A/B/C/D 24-255 [» ]
1CIW X-ray 2.70 A/B/C/D 24-259 [» ]
1CQ9 X-ray 3.50 A/B/C/D 24-259 [» ]
1CR7 X-ray 2.60 A/B/C/D/E/F/G/H 24-259 [» ]
1QF3 X-ray 2.80 A/B/C/D 24-259 [» ]
1RIR X-ray 2.90 A/B/C/D 24-259 [» ]
1RIT X-ray 2.85 A/B/C/D 24-259 [» ]
1V6I X-ray 2.15 A/B/C/D 24-255 [» ]
1V6J X-ray 2.90 A/B/C/D 24-255 [» ]
1V6K X-ray 2.40 A/B/C/D 24-255 [» ]
1V6L X-ray 2.50 A/B/C/D 24-255 [» ]
1V6M X-ray 2.70 A/B/C/D/E/F/G/H 24-255 [» ]
1V6N X-ray 3.50 A/B/C/D/E/F/G/H 24-255 [» ]
1V6O X-ray 3.00 A/B/C/D/E/F/G/H 24-255 [» ]
2DH1 X-ray 7.65 A/B/C/D 24-259 [» ]
2DV9 X-ray 2.48 A/B/C/D 24-259 [» ]
2DVA X-ray 2.20 A/B/C/D 24-259 [» ]
2DVB X-ray 2.25 A/B/C/D 24-259 [» ]
2DVD X-ray 2.25 A/B/C/D 24-259 [» ]
2DVF X-ray 2.74 A/B/C/D 24-259 [» ]
2DVG X-ray 2.78 A/B/C/D 24-259 [» ]
2PEL X-ray 2.25 A/B/C/D 24-259 [» ]
2TEP X-ray 2.50 A/B/C/D 24-259 [» ]
ProteinModelPortali P02872.
SMRi P02872. Positions 24-255.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 1050. Ara h Agglutinin.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02872.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. 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 ]
Pfami PF00139. Lectin_legB. 1 hit.
[Graphical view ]
PIRSFi PIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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).

Entry informationi

Entry nameiLECG_ARAHY
AccessioniPrimary (citable) accession number: P02872
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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