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P81460

- CONA_CANLI

UniProt

P81460 - CONA_CANLI

Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia lineata (Beach bean) (Dolichos lineatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Glucose/D-mannose specific lectin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi8 – 81ManganeseBy similarity
    Metal bindingi10 – 101CalciumBy similarity
    Metal bindingi10 – 101ManganeseBy similarity
    Metal bindingi12 – 121Calcium; via carbonyl oxygenBy similarity
    Binding sitei12 – 121CarbohydrateBy similarity
    Metal bindingi14 – 141CalciumBy similarity
    Metal bindingi19 – 191CalciumBy similarity
    Metal bindingi19 – 191ManganeseBy similarity
    Metal bindingi24 – 241ManganeseBy similarity
    Metal bindingi208 – 2081CalciumBy similarity
    Binding sitei228 – 2281Carbohydrate; via amide nitrogenBy similarity

    GO - Molecular functioni

    1. mannose binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Concanavalin-A
    Short name:
    Con A
    OrganismiCanavalia lineata (Beach bean) (Dolichos lineatus)
    Taxonomic identifieri28957 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 237237Concanavalin-APRO_0000105087Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    237
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi15 – 173
    Beta strandi24 – 3310
    Beta strandi35 – 395
    Beta strandi46 – 5510
    Turni56 – 594
    Beta strandi60 – 667
    Beta strandi72 – 787
    Helixi81 – 833
    Beta strandi87 – 9610
    Beta strandi98 – 1003
    Beta strandi105 – 11612
    Beta strandi124 – 1329
    Beta strandi140 – 1445
    Beta strandi150 – 1523
    Beta strandi154 – 1574
    Turni161 – 1633
    Beta strandi170 – 1778
    Beta strandi187 – 19913
    Beta strandi203 – 2053
    Beta strandi209 – 2168
    Helixi227 – 2293
    Turni230 – 2323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CWMX-ray1.95A1-237[»]
    2CY6X-ray2.00A/D1-237[»]
    2CYFX-ray1.80A1-237[»]
    3SNMX-ray2.15A1-237[»]
    4DPNX-ray2.55A/D1-237[»]
    4I30X-ray1.89A1-237[»]
    ProteinModelPortaliP81460.
    SMRiP81460. Positions 1-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81460.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1002Carbohydrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the leguminous lectin family.Curated

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000985. Lectin_LegA_CS.
    IPR019825. Lectin_legB_Mn/Ca_BS.
    IPR001220. Legume_lectin_dom.
    [Graphical view]
    PfamiPF00139. Lectin_legB. 2 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
    PS00307. LECTIN_LEGUME_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81460-1 [UniParc]FASTAAdd to Basket

    « Hide

    ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA    50
    HIIYNSVGKR LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY 100
    KETNTILSWS FTSKLKSNST HETNALHFVF NQFSKDQKDL ILQGDATTGT 150
    DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK 200
    SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN 237
    Length:237
    Mass (Da):25,497
    Last modified:December 15, 1998 - v1
    Checksum:i2D31C2BD3D30D66A
    GO

    Sequence databases

    PIRiA59415.

    Cross-referencesi

    Sequence databases

    PIRi A59415.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CWM X-ray 1.95 A 1-237 [» ]
    2CY6 X-ray 2.00 A/D 1-237 [» ]
    2CYF X-ray 1.80 A 1-237 [» ]
    3SNM X-ray 2.15 A 1-237 [» ]
    4DPN X-ray 2.55 A/D 1-237 [» ]
    4I30 X-ray 1.89 A 1-237 [» ]
    ProteinModelPortali P81460.
    SMRi P81460. Positions 1-237.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P81460.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000985. Lectin_LegA_CS.
    IPR019825. Lectin_legB_Mn/Ca_BS.
    IPR001220. Legume_lectin_dom.
    [Graphical view ]
    Pfami PF00139. Lectin_legB. 2 hits.
    [Graphical view ]
    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 structures of concanavalin A-like lectins from seeds of two species of Canavalia."
      Fujimura S., Terada S., Jayavardhanan K.K., Panikkar K.R., Kimoto E.
      Phytochemistry 33:985-987(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiCONA_CANLI
    AccessioniPrimary (citable) accession number: P81460
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 81 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