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P19588

- LEC5_VIGUC

UniProt

P19588 - LEC5_VIGUC

Protein

Lectin DB58

Gene
N/A
Organism
Vigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

    Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1.

    GO - Molecular functioni

    1. mannose binding Source: UniProtKB-KW

    Keywords - Ligandi

    Calcium, Lectin, Mannose-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lectin DB58
    Cleaved into the following 2 chains:
    OrganismiVigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
    Taxonomic identifieri3840 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 275253Lectin DB58 subunit alphaPRO_0000017613Add
    BLAST
    Chaini23 – 264242Lectin DB58 subunit betaPRO_0000017614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)
    Glycosylationi101 – 1011N-linked (GlcNAc...)

    Post-translational modificationi

    Leu-264 is missing in a major portion of the beta subunit, suggesting an origin by sequential removal of amino acids rather than a processing by endoproteolytic cleavage.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Heterodimer, composed of an alpha and a beta subunit derived from a single precursor.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 318
    Beta strandi38 – 425
    Beta strandi48 – 525
    Beta strandi67 – 748
    Turni81 – 833
    Beta strandi88 – 969
    Helixi102 – 1043
    Beta strandi108 – 1158
    Turni127 – 1293
    Helixi137 – 1393
    Beta strandi142 – 1476
    Beta strandi160 – 16910
    Beta strandi171 – 1755
    Beta strandi182 – 19110
    Turni192 – 1954
    Beta strandi196 – 2038
    Helixi204 – 2063
    Beta strandi208 – 2158
    Helixi218 – 2214
    Beta strandi224 – 23310
    Beta strandi245 – 25511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G7YX-ray2.50A/B/C/D/E/F23-275[»]
    1LULX-ray3.30A/B/C/D/E/F23-275[»]
    ProteinModelPortaliP19588.
    SMRiP19588. Positions 23-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19588.

    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.

    P19588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSTVSVVL SLFLLLLTQA YSADIQSFSF KNFNSSSFIL QGDATVSSSK    50
    LRLTKVKGNG LPTLSSLGRA FYSSPIQIYD KSTGAVASWA TSFTANIFAP 100
    NKSSSADGIA FALVPVGSEP KSNSGFLGVF DSDVYDNSAQ TVAVEFDTFS 150
    NTDWDPTSRH IGIDVNSIKS IRTASWGLAN GQNAEILITY NAATSLLVAS 200
    LVHPSRRTSY IVSERVDITN ELPEYVSIGF SATTGLSEGY TETHDVLSWS 250
    FASKLPDDST TEPLDIASYL VRNVL 275
    Length:275
    Mass (Da):29,453
    Last modified:July 15, 1999 - v2
    Checksum:i53D72ACB02EAE03F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2372LS → FF in AAA33142. (PubMed:2844781)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23216 mRNA. Translation: AAA33142.1.
    M34271 Genomic DNA. Translation: AAA33140.1.
    PIRiA31972.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23216 mRNA. Translation: AAA33142.1 .
    M34271 Genomic DNA. Translation: AAA33140.1 .
    PIRi A31972.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G7Y X-ray 2.50 A/B/C/D/E/F 23-275 [» ]
    1LUL X-ray 3.30 A/B/C/D/E/F 23-275 [» ]
    ProteinModelPortali P19588.
    SMRi P19588. Positions 23-275.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P19588.

    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. "cDNA cloning, primary structure, and in vitro biosynthesis of the DB58 lectin from Dolichos biflorus."
      Schnell D.J., Etzler M.E.
      J. Biol. Chem. 263:14648-14653(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Two lectin genes differentially expressed in Dolichos biflorus differ primarily by a 116-base pair sequence in their 5' flanking regions."
      Harada J.J., Spadoro-Tank J., Maxwell J.C., Schnell D.J., Etzler M.E.
      J. Biol. Chem. 265:4997-5001(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Isolation and characterization of subunits of DB58, a lectin from the stems and leaves of Dolichos biflorus."
      Etzler M.E.
      Biochemistry 33:9778-9783(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 255-275, PROTEOLYTIC PROCESSING.
      Tissue: Leaf and Stem.
    4. "Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus."
      Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.-H., Strecker G., Imberty A., Fernandez E., Wyns L., Etzler M.E.
      J. Mol. Biol. 286:1161-1177(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).

    Entry informationi

    Entry nameiLEC5_VIGUC
    AccessioniPrimary (citable) accession number: P19588
    Secondary accession number(s): Q39665
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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