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P02867

- LEC_PEA

UniProt

P02867 - LEC_PEA

Protein

Lectin

Gene

LECA

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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 – 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.
    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.
    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

    Experimental Info

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

    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...
    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 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: October 1, 2014
    This is version 103 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