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P02867

- LEC_PEA

UniProt

P02867 - LEC_PEA

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Protein

Lectin

Gene

LECA

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

D-mannose specific lectin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi149 – 1491ManganeseBy similarity
Metal bindingi151 – 1511CalciumBy similarity
Metal bindingi151 – 1511ManganeseBy similarity
Metal bindingi153 – 1531Calcium; via carbonyl oxygenBy similarity
Metal bindingi155 – 1551CalciumBy similarity
Metal bindingi159 – 1591CalciumBy similarity
Metal bindingi159 – 1591ManganeseBy similarity
Metal bindingi166 – 1661ManganeseBy similarity

GO - Molecular functioni

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

Keywords - Ligandi

Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin
Cleaved into the following 2 chains:
Gene namesi
Name:LECA
Synonyms:PSL1
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Pathology & Biotechi

Protein family/group databases

Allergomei8818. Pis s Agglutinin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Add
BLAST
Chaini31 – 217187Lectin beta chainPRO_0000017623Add
BLAST
Chaini218 – 27558Lectin alpha chainPRO_0000017624Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Protein-protein interaction databases

MINTiMINT-1508409.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 409Combined sources
Beta strandi48 – 525Combined sources
Beta strandi55 – 573Combined sources
Beta strandi58 – 647Combined sources
Beta strandi71 – 788Combined sources
Turni85 – 873Combined sources
Beta strandi92 – 10211Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi112 – 1198Combined sources
Helixi128 – 1303Combined sources
Turni131 – 1333Combined sources
Helixi141 – 1433Combined sources
Beta strandi146 – 1516Combined sources
Turni156 – 1583Combined sources
Beta strandi166 – 17510Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi190 – 1978Combined sources
Turni198 – 2014Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi219 – 2268Combined sources
Helixi229 – 2324Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 26313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQPX-ray2.10A/C31-211[»]
B/D218-264[»]
1HKDX-ray2.09A/C31-211[»]
B/D218-269[»]
1OFSX-ray1.80A/C31-217[»]
B/D218-265[»]
1RINX-ray2.60A/C31-210[»]
B/D218-266[»]
2BQPX-ray1.90A/B31-264[»]
2LTNX-ray1.70A/C31-211[»]
B/D218-269[»]
ProteinModelPortaliP02867.
SMRiP02867. Positions 31-266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02867.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
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.

P02867-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF
60 70 80 90 100
QGDGYTTKEK LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV
110 120 130 140 150
INAPNSYNVA DGFTFFIAPV DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF
160 170 180 190 200
DTFYNAAWDP SNRDRHIGID VNSIKSVNTK SWKLQNGEEA NVVIAFNAAT
210 220 230 240 250
NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG FSATTGAEYA
260 270
AHEVLSWSFH SELSGTSSSK QAADA
Length:275
Mass (Da):30,270
Last modified:July 21, 1986 - v1
Checksum:iFD7BE8E00A811222
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691Missing1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00440 Genomic DNA. Translation: CAA68497.1.
M18160 mRNA. Translation: AAA33676.1.
J01254 mRNA. No translation available.
X66368 Genomic DNA. Translation: CAA47011.1.
PIRiA26844. LNPM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00440 Genomic DNA. Translation: CAA68497.1 .
M18160 mRNA. Translation: AAA33676.1 .
J01254 mRNA. No translation available.
X66368 Genomic DNA. Translation: CAA47011.1 .
PIRi A26844. LNPM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQP X-ray 2.10 A/C 31-211 [» ]
B/D 218-264 [» ]
1HKD X-ray 2.09 A/C 31-211 [» ]
B/D 218-269 [» ]
1OFS X-ray 1.80 A/C 31-217 [» ]
B/D 218-265 [» ]
1RIN X-ray 2.60 A/C 31-210 [» ]
B/D 218-266 [» ]
2BQP X-ray 1.90 A/B 31-264 [» ]
2LTN X-ray 1.70 A/C 31-211 [» ]
B/D 218-269 [» ]
ProteinModelPortali P02867.
SMRi P02867. Positions 31-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1508409.

Protein family/group databases

Allergomei 8818. Pis s Agglutinin.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02867.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Feltham First.
    Tissue: Seed.
  2. "The pea lectin gene family contains only one functional gene."
    Kaminski P.A., Buffard D., Strosberg A.D.
    Plant Mol. Biol. 9:497-507(1987)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The biosynthesis and primary structure of pea seed lectin."
    Higgins T.J.V., Chandler P.M., Zurawski G., Button S.C., Spencer D.
    J. Biol. Chem. 258:9544-9549(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. P1/G086.
  4. de Pater B.S., Pham K.T., Katagiri F., Chua N.H., Kijne J.W.
    Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Feltham First.
  5. "The complete amino acid sequence of the alpha-subunit of pea lectin, Pisum sativum."
    Richardson C., Behnke W.D., Freisheim J.H., Blumenthal K.M.
    Biochim. Biophys. Acta 537:310-319(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 218-271.
  6. "The crystal structure of pea lectin at 3.0-A resolution."
    Einspahr H., Parks E.H., Suguna K., Subramanian E., Suddath F.L.
    J. Biol. Chem. 261:16518-16527(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  7. "X-ray crystal structure of a pea lectin-trimannoside complex at 2.6-A resolution."
    Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P.
    J. Biol. Chem. 268:10126-10132(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  8. "The structure of the pea lectin-D-mannopyranose complex at a 2.1 A resolution."
    Ruzeinikov S.N., Mikhailova I.Y., Tsygannik I.N., Pangborn W., Duax W., Pletnev V.Z.
    Russ. J. Bioorg. Chem. 24:277-279(1998)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  9. "Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity."
    van Eijsden R.R., Hoedemaeker F.J., Diaz C.L., Lugtenberg B.J.J., de Pater B.S., Kijne J.W.
    Plant Mol. Biol. 20:1049-1058(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiLEC_PEA
AccessioniPrimary (citable) accession number: P02867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 105 of the entry and version 1 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