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P02876

- AGI2_WHEAT

UniProt

P02876 - AGI2_WHEAT

Protein

Agglutinin isolectin 2

Gene
N/A
Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin.

    GO - Molecular functioni

    1. chitin binding Source: UniProtKB-KW

    Keywords - Ligandi

    Chitin-binding, Lectin

    Protein family/group databases

    CAZyiCBM18. Carbohydrate-Binding Module Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Agglutinin isolectin 2
    Alternative name(s):
    Isolectin D
    WGA2
    OrganismiTriticum aestivum (Wheat)
    Taxonomic identifieri4565 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
    ProteomesiUP000019116: Unplaced

    Organism-specific databases

    GrameneiP02876.

    Pathology & Biotechi

    Protein family/group databases

    Allergomei650. Tri a 18.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 198171Agglutinin isolectin 2PRO_0000005257Add
    BLAST
    Propeptidei199 – 21315PRO_0000005258Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi30 ↔ 451 PublicationPROSITE-ProRule annotation
    Disulfide bondi39 ↔ 511 PublicationPROSITE-ProRule annotation
    Disulfide bondi44 ↔ 581 PublicationPROSITE-ProRule annotation
    Disulfide bondi62 ↔ 671 PublicationPROSITE-ProRule annotation
    Disulfide bondi73 ↔ 881 PublicationPROSITE-ProRule annotation
    Disulfide bondi82 ↔ 941 PublicationPROSITE-ProRule annotation
    Disulfide bondi87 ↔ 1011 PublicationPROSITE-ProRule annotation
    Disulfide bondi105 ↔ 1101 PublicationPROSITE-ProRule annotation
    Disulfide bondi116 ↔ 1311 PublicationPROSITE-ProRule annotation
    Disulfide bondi125 ↔ 1371 PublicationPROSITE-ProRule annotation
    Disulfide bondi130 ↔ 1441 PublicationPROSITE-ProRule annotation
    Disulfide bondi148 ↔ 1531 PublicationPROSITE-ProRule annotation
    Disulfide bondi159 ↔ 1741 PublicationPROSITE-ProRule annotation
    Disulfide bondi168 ↔ 1801 PublicationPROSITE-ProRule annotation
    Disulfide bondi173 ↔ 1871 PublicationPROSITE-ProRule annotation
    Disulfide bondi191 ↔ 1961 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Interactioni

    Subunit structurei

    Homodimer, u-shaped.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 344
    Helixi40 – 423
    Helixi55 – 584
    Beta strandi64 – 663
    Helixi74 – 774
    Helixi83 – 853
    Beta strandi92 – 954
    Helixi98 – 1014
    Beta strandi107 – 1093
    Helixi118 – 1203
    Helixi126 – 1283
    Beta strandi135 – 1384
    Helixi141 – 1444
    Beta strandi150 – 1523
    Helixi161 – 1633
    Helixi169 – 1713
    Beta strandi173 – 1753
    Turni176 – 1783
    Beta strandi179 – 1813
    Helixi184 – 1874
    Beta strandi193 – 1953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WGCX-ray2.20A/B29-198[»]
    9WGAX-ray1.80A/B29-198[»]
    ProteinModelPortaliP02876.
    SMRiP02876. Positions 28-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02876.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6942Chitin-binding type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 11243Chitin-binding type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 15543Chitin-binding type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 19843Chitin-binding type-1 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 393Substrate bindingBy similarity
    Regioni89 – 10012Substrate bindingBy similarityAdd
    BLAST
    Regioni141 – 1422Substrate binding

    Sequence similaritiesi

    Contains 4 chitin-binding type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di3.30.60.10. 4 hits.
    InterProiIPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    [Graphical view]
    PfamiPF00187. Chitin_bind_1. 4 hits.
    [Graphical view]
    PRINTSiPR00451. CHITINBINDNG.
    ProDomiPD000609. Chitin_bd_1. 3 hits.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00270. ChtBD1. 4 hits.
    [Graphical view]
    SUPFAMiSSF57016. SSF57016. 4 hits.
    PROSITEiPS00026. CHIT_BIND_I_1. 4 hits.
    PS50941. CHIT_BIND_I_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02876-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKMMSTMAL TLGAAVFLAF AAATAQAQRC GEQGSNMECP NNLCCSQYGY    50
    CGMGGDYCGK GCQNGACWTS KRCGSQAGGA TCPNNHCCSQ YGHCGFGAEY 100
    CGAGCQGGPC RADIKCGSQS GGKLCPNNLC CSQWGFCGLG SEFCGGGCQS 150
    GACSTDKPCG KDAGGRVCTN NYCCSKWGSC GIGPGYCGAG CQSGGCDAVF 200
    AGAITANSTL LAE 213
    Length:213
    Mass (Da):21,356
    Last modified:November 1, 1990 - v3
    Checksum:iF656A5C9277148AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641N → D AA sequence (PubMed:6546522)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25537 mRNA. Translation: AAA34258.1.
    PIRiS09624. AEWT2.
    UniGeneiTa.147.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25537 mRNA. Translation: AAA34258.1 .
    PIRi S09624. AEWT2.
    UniGenei Ta.147.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WGC X-ray 2.20 A/B 29-198 [» ]
    9WGA X-ray 1.80 A/B 29-198 [» ]
    ProteinModelPortali P02876.
    SMRi P02876. Positions 28-198.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 650. Tri a 18.
    CAZyi CBM18. Carbohydrate-Binding Module Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P02876.

    Miscellaneous databases

    EvolutionaryTracei P02876.
    PROi P02876.

    Family and domain databases

    Gene3Di 3.30.60.10. 4 hits.
    InterProi IPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    [Graphical view ]
    Pfami PF00187. Chitin_bind_1. 4 hits.
    [Graphical view ]
    PRINTSi PR00451. CHITINBINDNG.
    ProDomi PD000609. Chitin_bd_1. 3 hits.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57016. SSF57016. 4 hits.
    PROSITEi PS00026. CHIT_BIND_I_1. 4 hits.
    PS50941. CHIT_BIND_I_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D."
      Smith J.J., Raikhel N.V.
      Plant Mol. Biol. 13:601-603(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Primary structure of wheat germ agglutinin isolectin 2. Peptide order deduced from X-ray structure."
      Wright C.S., Gavilanes F., Peterson D.L.
      Biochemistry 23:280-287(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-198.
      Tissue: Germ.
    3. "Sequence variability in three wheat germ agglutinin isolectins: products of multiple genes in polyploid wheat."
      Wright C.S., Raikhel N.V.
      J. Mol. Evol. 28:327-336(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 68; 136; 161 AND 177.
    4. "The crystal structure of wheat germ agglutinin at 2.2-A resolution."
      Wright C.S.
      J. Mol. Biol. 111:439-457(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    5. "Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8-A resolution."
      Wright C.S.
      J. Mol. Biol. 194:501-529(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    6. Erratum
      Wright C.S.
      J. Mol. Biol. 199:239-239(1988)

    Entry informationi

    Entry nameiAGI2_WHEAT
    AccessioniPrimary (citable) accession number: P02876
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The 4 sites proposed for binding to carbohydrates (N-acetyl-D-glucosamine) of receptor molecules are on the surface of the agglutinin molecule.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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