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P05045

- LEC1_VIGUC

UniProt

P05045 - LEC1_VIGUC

Protein

Seed lectin subunit I

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 84 (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. Has a high preference for GalNAc over Gal.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei265 – 2662Cleavage

    GO - Molecular functioni

    1. mannose binding Source: UniProtKB-KW

    Keywords - Ligandi

    Calcium, Lectin, Mannose-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Seed lectin subunit I
    Short name:
    SL
    Cleaved into the following chain:
    OrganismiVigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus)
    Taxonomic identifieri3840 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

    Pathology & Biotechi

    Protein family/group databases

    Allergomei3011. Dol b Agglutinin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 275253Seed lectin subunit IPRO_0000017611Add
    BLAST
    Chaini23 – 265243Seed lectin subunit IIPRO_0000017612Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Subunit II may arise from subunit I by proteolytic cleavage at the C-terminal end.

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 329
    Helixi35 – 373
    Beta strandi38 – 425
    Beta strandi45 – 473
    Beta strandi50 – 523
    Beta strandi67 – 748
    Turni81 – 844
    Beta strandi88 – 969
    Beta strandi107 – 1159
    Helixi124 – 1263
    Turni127 – 1293
    Helixi137 – 1393
    Beta strandi142 – 1476
    Turni152 – 1543
    Beta strandi160 – 16910
    Beta strandi171 – 1755
    Beta strandi184 – 1918
    Turni192 – 1954
    Beta strandi196 – 2027
    Helixi204 – 2063
    Beta strandi209 – 2157
    Helixi218 – 2214
    Beta strandi224 – 23411
    Beta strandi245 – 25511
    Beta strandi257 – 2593
    Helixi266 – 2738

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BJQX-ray2.65A/B/C/D/E/F/G/H23-275[»]
    1LU1X-ray2.60A23-275[»]
    1LU2X-ray2.80A/B23-275[»]
    ProteinModelPortaliP05045.
    SMRiP05045. Positions 23-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05045.

    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.

    P05045-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSTVSVVL SLFLLLLTQA NSANIQSFSF KNFNSPSFIL QGDATVSSGK    50
    LQLTKVKENG IPTPSSLGRA FYSSPIQIYD KSTGAVASWA TSFTVKISAP 100
    SKASFADGIA FALVPVGSEP RRNGGYLGVF DSDVYNNSAQ TVAVEFDTFS 150
    NSGWDPSMKH IGIDVNSIKS IATVSWDLAN GENAEILITY NAATSLLVAS 200
    LVHPSRRTSY ILSERVDITN ELPEYVSVGF SATTGLSEGY IETHDVLSWS 250
    FASKLPDDST AEPLDLASYL VRNVL 275
    Length:275
    Mass (Da):29,406
    Last modified:July 15, 1999 - v2
    Checksum:iD313D73860661A83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 677IPTPSSL → FPLRFPS in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti82 – 821S → F in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti149 – 1491F → L in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti199 – 1991A → V in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti227 – 2271S → G in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti254 – 2541K → R in AAA33141. (PubMed:3584113)Curated
    Sequence conflicti268 – 2681S → R in AAA33141. (PubMed:3584113)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02721 mRNA. Translation: AAA33141.1.
    M34270 Genomic DNA. Translation: AAA33143.1.
    PIRiA29572.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02721 mRNA. Translation: AAA33141.1 .
    M34270 Genomic DNA. Translation: AAA33143.1 .
    PIRi A29572.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BJQ X-ray 2.65 A/B/C/D/E/F/G/H 23-275 [» ]
    1LU1 X-ray 2.60 A 23-275 [» ]
    1LU2 X-ray 2.80 A/B 23-275 [» ]
    ProteinModelPortali P05045.
    SMRi P05045. Positions 23-275.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00173. Adenine.

    Protein family/group databases

    Allergomei 3011. Dol b Agglutinin.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P05045.

    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. "Primary structure of the Dolichos biflorus seed lectin."
      Schnell D.J., Etzler M.E.
      J. Biol. Chem. 262:7220-7225(1987) [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. "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 (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiLEC1_VIGUC
    AccessioniPrimary (citable) accession number: P05045
    Secondary accession number(s): Q39666
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 84 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

    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