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P02866

- CONA_CANEN

UniProt

P02866 - CONA_CANEN

Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    D-mannose specific lectin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi119 – 1191CalciumBy similarity
    Binding sitei119 – 1191Carbohydrate
    Binding sitei139 – 1391Carbohydrate; via amide nitrogen
    Sitei148 – 1492Cleavage
    Sitei163 – 1642Cleavage
    Metal bindingi171 – 1711Manganese
    Metal bindingi173 – 1731Calcium1 Publication
    Metal bindingi173 – 1731Manganese
    Metal bindingi175 – 1751Calcium; via carbonyl oxygen1 Publication
    Metal bindingi177 – 1771Calcium1 Publication
    Metal bindingi182 – 1821Calcium1 Publication
    Metal bindingi182 – 1821Manganese
    Metal bindingi187 – 1871Manganese
    Sitei281 – 2822Cleavage

    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
    Cleaved into the following chain:
    OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
    Taxonomic identifieri3823 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 148119Concanavalin-APRO_0000017577Add
    BLAST
    Propeptidei149 – 163151 PublicationPRO_0000017578Add
    BLAST
    Chaini164 – 281118Concanavalin, 1st partPRO_0000017579Add
    BLAST
    Propeptidei282 – 2909PRO_0000017580

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi152 – 1521N-linked (GlcNAc...)

    Post-translational modificationi

    The mature chain consists of residues 164-281 followed by 30-148. To form a mature chain the precursor undergoes further post-translational modification after removal of the signal sequence; cleavage after Asn at positions 148, 163, and 281 is followed by transposition and ligation (By formation of a new peptide bond) of residues 164-281 and 30-148.

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP02866. 109 interactions.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 325
    Beta strandi34 – 429
    Beta strandi51 – 555
    Helixi61 – 633
    Beta strandi64 – 685
    Turni72 – 743
    Beta strandi81 – 888
    Beta strandi97 – 10913
    Beta strandi113 – 1164
    Beta strandi120 – 1267
    Helixi138 – 1403
    Turni141 – 1433
    Beta strandi167 – 1737
    Helixi178 – 1803
    Beta strandi187 – 19610
    Beta strandi198 – 2025
    Beta strandi210 – 2189
    Turni219 – 2224
    Beta strandi223 – 2297
    Beta strandi231 – 2333
    Beta strandi236 – 2416
    Helixi244 – 2463
    Beta strandi250 – 25910
    Beta strandi261 – 2633
    Beta strandi268 – 28114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1APNX-ray2.50A/B28-148[»]
    1BXHX-ray2.75A/B/C/D148-164[»]
    1C57neutron diffraction2.40A148-164[»]
    1CESX-ray2.70A/B28-148[»]
    1CJPX-ray2.78A/B/C/D30-148[»]
    1CN1X-ray3.20A/B30-281[»]
    1CONX-ray2.00A28-148[»]
    1CVNX-ray2.30A/B/C/D30-148[»]
    1DQ0X-ray1.70A28-148[»]
    1DQ1X-ray2.15A28-148[»]
    1DQ2X-ray2.05A/B28-148[»]
    1DQ4X-ray2.90A/B28-148[»]
    1DQ5X-ray2.00A28-148[»]
    1DQ6X-ray1.90A28-148[»]
    1ENQX-ray2.50A/B/C/D30-148[»]
    1ENRX-ray1.83A28-148[»]
    1ENSX-ray2.80A/B30-148[»]
    1GICX-ray2.00A/B28-148[»]
    1GKBX-ray1.56A/B148-164[»]
    1HQWX-ray2.40A30-148[»]
    1I3HX-ray1.20A28-148[»]
    1JBCX-ray1.15A28-148[»]
    1JN2X-ray1.90P28-148[»]
    1JOJX-ray3.00A/B/C/D28-148[»]
    1JUIX-ray2.75A/B/C/D28-148[»]
    1JW6X-ray1.93A28-148[»]
    1JYCX-ray2.75A/B/C/D28-148[»]
    1JYIX-ray2.75A/B/C/D28-148[»]
    1NLSX-ray0.94A28-148[»]
    1NXDX-ray1.901/2/3/4148-164[»]
    1ONAX-ray2.35A/B/C/D30-148[»]
    1QGLX-ray2.66A/B30-148[»]
    1QNYX-ray1.80A28-148[»]
    1SCRX-ray2.00A28-148[»]
    1SCSX-ray1.60A28-148[»]
    1TEIX-ray2.70A/B/C/D/E/F/G/H28-148[»]
    1VALX-ray3.00A/B/C/D30-148[»]
    1VAMX-ray2.75A/B/C/D30-148[»]
    1XQNneutron diffraction2.50A28-148[»]
    2CNAX-ray2.00A28-148[»]
    2CTVX-ray1.95A28-148[»]
    2ENRX-ray2.35A28-148[»]
    2UU8X-ray0.94A148-164[»]
    2YZ4neutron diffraction2.20A28-148[»]
    3CNAX-ray2.40A30-281[»]
    3D4KX-ray1.80A/B/C/D148-164[»]
    3ENRX-ray2.40A/B148-164[»]
    3NWKX-ray2.09A/B/C/D148-164[»]
    5CNAX-ray2.00A/B/C/D28-148[»]
    ProteinModelPortaliP02866.
    SMRiP02866. Positions 28-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02866.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni262 – 2632Carbohydrate binding

    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.

    P02866-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD    50
    LILQGDATTG TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA 100
    SFEATFTFLI KSPDSHPADG IAFFISNIDS SIPSGSTGRL LGLFPDANVI 150
    RNSTTIDFNA AYNADTIVAV ELDTYPNTDI GDPSYPHIGI DIKSVRSKKT 200
    AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY DVDLDNVLPE 250
    WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV 290
    Length:290
    Mass (Da):31,480
    Last modified:October 3, 2003 - v2
    Checksum:i0F2F7DBBCF547E42
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331E → Q AA sequence (PubMed:1112814)Curated
    Sequence conflicti35 – 351N → D AA sequence (PubMed:1112814)Curated
    Sequence conflicti62 – 621D → E in CAA25787. (PubMed:3965973)Curated
    Sequence conflicti66 – 661E → R in CAA25787. (PubMed:3965973)Curated
    Sequence conflicti77 – 771Q → E AA sequence (PubMed:1112814)Curated
    Sequence conflicti98 – 1014VVAS → TVSA AA sequence (PubMed:1112814)Curated
    Sequence conflicti107 – 1071T → A AA sequence (PubMed:1112814)Curated
    Sequence conflicti207 – 2071N → D AA sequence (PubMed:1112813)Curated
    Sequence conflicti245 – 2462DN → ND AA sequence (PubMed:1112813)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01632 mRNA. Translation: CAA25787.1.
    AF308777 mRNA. Translation: AAL09432.1.
    PIRiA03357. CVJBP.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual
    Functional Glycomics Gateway - Glycan Binding

    Con A (Canavalia ensiformis)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01632 mRNA. Translation: CAA25787.1 .
    AF308777 mRNA. Translation: AAL09432.1 .
    PIRi A03357. CVJBP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1APN X-ray 2.50 A/B 28-148 [» ]
    1BXH X-ray 2.75 A/B/C/D 148-164 [» ]
    1C57 neutron diffraction 2.40 A 148-164 [» ]
    1CES X-ray 2.70 A/B 28-148 [» ]
    1CJP X-ray 2.78 A/B/C/D 30-148 [» ]
    1CN1 X-ray 3.20 A/B 30-281 [» ]
    1CON X-ray 2.00 A 28-148 [» ]
    1CVN X-ray 2.30 A/B/C/D 30-148 [» ]
    1DQ0 X-ray 1.70 A 28-148 [» ]
    1DQ1 X-ray 2.15 A 28-148 [» ]
    1DQ2 X-ray 2.05 A/B 28-148 [» ]
    1DQ4 X-ray 2.90 A/B 28-148 [» ]
    1DQ5 X-ray 2.00 A 28-148 [» ]
    1DQ6 X-ray 1.90 A 28-148 [» ]
    1ENQ X-ray 2.50 A/B/C/D 30-148 [» ]
    1ENR X-ray 1.83 A 28-148 [» ]
    1ENS X-ray 2.80 A/B 30-148 [» ]
    1GIC X-ray 2.00 A/B 28-148 [» ]
    1GKB X-ray 1.56 A/B 148-164 [» ]
    1HQW X-ray 2.40 A 30-148 [» ]
    1I3H X-ray 1.20 A 28-148 [» ]
    1JBC X-ray 1.15 A 28-148 [» ]
    1JN2 X-ray 1.90 P 28-148 [» ]
    1JOJ X-ray 3.00 A/B/C/D 28-148 [» ]
    1JUI X-ray 2.75 A/B/C/D 28-148 [» ]
    1JW6 X-ray 1.93 A 28-148 [» ]
    1JYC X-ray 2.75 A/B/C/D 28-148 [» ]
    1JYI X-ray 2.75 A/B/C/D 28-148 [» ]
    1NLS X-ray 0.94 A 28-148 [» ]
    1NXD X-ray 1.90 1/2/3/4 148-164 [» ]
    1ONA X-ray 2.35 A/B/C/D 30-148 [» ]
    1QGL X-ray 2.66 A/B 30-148 [» ]
    1QNY X-ray 1.80 A 28-148 [» ]
    1SCR X-ray 2.00 A 28-148 [» ]
    1SCS X-ray 1.60 A 28-148 [» ]
    1TEI X-ray 2.70 A/B/C/D/E/F/G/H 28-148 [» ]
    1VAL X-ray 3.00 A/B/C/D 30-148 [» ]
    1VAM X-ray 2.75 A/B/C/D 30-148 [» ]
    1XQN neutron diffraction 2.50 A 28-148 [» ]
    2CNA X-ray 2.00 A 28-148 [» ]
    2CTV X-ray 1.95 A 28-148 [» ]
    2ENR X-ray 2.35 A 28-148 [» ]
    2UU8 X-ray 0.94 A 148-164 [» ]
    2YZ4 neutron diffraction 2.20 A 28-148 [» ]
    3CNA X-ray 2.40 A 30-281 [» ]
    3D4K X-ray 1.80 A/B/C/D 148-164 [» ]
    3ENR X-ray 2.40 A/B 148-164 [» ]
    3NWK X-ray 2.09 A/B/C/D 148-164 [» ]
    5CNA X-ray 2.00 A/B/C/D 28-148 [» ]
    ProteinModelPortali P02866.
    SMRi P02866. Positions 28-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02866. 109 interactions.

    Chemistry

    BindingDBi P02866.
    ChEMBLi CHEMBL5820.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P02866.

    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. "Polypeptide ligation occurs during post-translational modification of concanavalin A."
      Carrington D.M., Auffret A., Hanke D.E.
      Nature 313:64-67(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Ramis C., Gomord V.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. U-02.
    3. "The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3."
      Cunningham B.A., Wang J.L., Waxdal M.J., Edelman G.M.
      J. Biol. Chem. 250:1503-1512(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-148.
    4. "The covalent and three-dimensional structural of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2."
      Wang J.L., Cunningham B.A., Waxdal M.J., Edelman G.M.
      J. Biol. Chem. 250:1490-1502(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 164-281.
    5. "Structure of concanavalin A at 2.4-A resolution."
      Hardman K.D., Ainsworth C.F.
      Biochemistry 11:4910-4919(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    6. "The covalent and three-dimensional structure of concanavalin A. III. Structure of the monomer and its interactions with metals and saccharides."
      Becker J.W., Reeke G.N. Jr., Wang J.L., Cunningham B.A., Edelman G.M.
      J. Biol. Chem. 250:1513-1524(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    7. "The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure."
      Reeke G.N. Jr., Becker J.W., Edelman G.M.
      J. Biol. Chem. 250:1525-1547(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    8. "The structure of the saccharide-binding site of concanavalin A."
      Derewenda Z., Yariv J., Helliwell J.R., Kalb A.J., Dodson E.J., Papiz M.Z., Wan T., Campbell J.
      EMBO J. 8:2189-2193(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 164-290 IN COMPLEX WITH METHYL-ALPHA-D-MANNOPYRANOSIDE; CALCIUM AND MANGANESE IONS, SUBUNIT.
    9. "Atomic resolution structure of concanavalin A at 120 K."
      Parkin S., Rupp B., Hope H.
      Acta Crystallogr. D 52:1161-1168(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
    10. "The structural features of concanavalin A governing non-proline peptide isomerization."
      Bouckaert J., Dewallef Y., Poortmans F., Wyns L., Loris R.
      J. Biol. Chem. 275:19778-19787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

    Entry informationi

    Entry nameiCONA_CANEN
    AccessioniPrimary (citable) accession number: P02866
    Secondary accession number(s): Q947H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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