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P02867

- LEC_PEA

UniProt

P02867 - LEC_PEA

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Protein
Lectin
Gene
LECA, PSL1
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 – 1491Manganese By similarity
Metal bindingi151 – 1511Calcium By similarity
Metal bindingi151 – 1511Manganese By similarity
Metal bindingi153 – 1531Calcium; via carbonyl oxygen By similarity
Metal bindingi155 – 1551Calcium By similarity
Metal bindingi159 – 1591Calcium By similarity
Metal bindingi159 – 1591Manganese By similarity
Metal bindingi166 – 1661Manganese By 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 – 3030
Add
BLAST
Chaini31 – 217187Lectin beta chain
PRO_0000017623Add
BLAST
Chaini218 – 27558Lectin alpha chain
PRO_0000017624Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains.

Protein-protein interaction databases

MINTiMINT-1508409.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP02867.

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.

P02867-1 [UniParc]FASTAAdd to Basket

« Hide

MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF    50
QGDGYTTKEK LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV 100
INAPNSYNVA DGFTFFIAPV DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF 150
DTFYNAAWDP SNRDRHIGID VNSIKSVNTK SWKLQNGEEA NVVIAFNAAT 200
NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG FSATTGAEYA 250
AHEVLSWSFH SELSGTSSSK QAADA 275
Length:275
Mass (Da):30,270
Last modified:July 21, 1986 - v1
Checksum:iFD7BE8E00A811222
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

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 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. 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: February 19, 2014
This is version 102 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

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