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P11218

- AGI_URTDI

UniProt

P11218 - AGI_URTDI

Protein

Lectin/endochitinase 1

Gene

UDA1

Organism
Urtica dioica (Great nettle) (Stinging nettle)
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 3 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.1 Publication

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241Substrate; via amide nitrogen
    Metal bindingi70 – 701Zinc 1; shared with dimeric partner
    Metal bindingi90 – 901Zinc 2; shared with dimeric partner

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB-EC
    2. chitin binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-KW
    3. defense response to fungus Source: UniProtKB-KW
    4. killing of cells of other organism Source: UniProtKB-KW
    5. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Fungicide, Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding, Lectin, Metal-binding, Zinc

    Protein family/group databases

    CAZyiCBM18. Carbohydrate-Binding Module Family 18.
    GH19. Glycoside Hydrolase Family 19.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lectin/endochitinase 1 (EC:3.2.1.14)
    Alternative name(s):
    Agglutinin
    UDA
    chia5.1.1
    Cleaved into the following chain:
    Gene namesi
    Name:UDA1
    OrganismiUrtica dioica (Great nettle) (Stinging nettle)
    Taxonomic identifieri3501 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesUrticaceaeUrtica

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 372349Lectin/endochitinase 1PRO_0000005266Add
    BLAST
    Chaini24 – 11289Lectin 1PRO_0000005267Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Pyrrolidone carboxylic acid
    Disulfide bondi26 ↔ 41
    Disulfide bondi35 ↔ 47
    Disulfide bondi40 ↔ 54
    Disulfide bondi58 ↔ 62
    Disulfide bondi72 ↔ 87
    Disulfide bondi81 ↔ 93
    Disulfide bondi86 ↔ 100
    Disulfide bondi105 ↔ 109
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically processed to yield a very small protein (8.5 kDa, 86 AA) containing only the two chitin-binding domains.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Expressioni

    Tissue specificityi

    Rhizomes and inflorescence with immature seeds.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Zinc favors dimerization. Active in the monomeric form but probably inactive in the dimeric form. The interaction with glycans on the mammalian TCR and MHC molecules of the T-cell and antigen-presenting cell, respectively, is inhibited by oligomers of GlcNAc.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    envQ757602EBI-8453649,EBI-8453491From a different organism.

    Protein-protein interaction databases

    IntActiP11218. 1 interaction.
    MINTiMINT-8414736.

    Structurei

    Secondary structure

    1
    372
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 304
    Helixi36 – 383
    Beta strandi40 – 423
    Beta strandi45 – 506
    Helixi51 – 544
    Beta strandi58 – 614
    Helixi63 – 653
    Helixi74 – 763
    Beta strandi85 – 884
    Beta strandi91 – 966
    Helixi97 – 1004
    Helixi102 – 1043
    Beta strandi105 – 1084

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EN2X-ray1.40A25-112[»]
    1ENMX-ray1.90A25-112[»]
    1IQBX-ray1.90A/B24-112[»]
    ProteinModelPortaliP11218.
    SMRiP11218. Positions 24-112, 132-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11218.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 6441Chitin-binding type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini69 – 11143Chitin-binding type-1 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 5312Substrate bindingAdd
    BLAST
    Regioni113 – 12816SpacerAdd
    BLAST
    Regioni129 – 372244ChitinaseAdd
    BLAST

    Sequence similaritiesi

    Contains 2 chitin-binding type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di3.30.60.10. 2 hits.
    InterProiIPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001060. Endochitinase. 1 hit.
    ProDomiPD000609. Chitin_bd_1. 2 hits.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00270. ChtBD1. 2 hits.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 2 hits.
    PROSITEiPS00026. CHIT_BIND_I_1. 2 hits.
    PS50941. CHIT_BIND_I_2. 2 hits.
    PS00773. CHITINASE_19_1. 1 hit.
    PS00774. CHITINASE_19_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11218-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMMRFLSAVV IMSSAMAVGL VSAQRCGSQG GGGTCPALWC CSIWGWCGDS    50
    EPYCGRTCEN KCWSGERSDH RCGAAVGNPP CGQDRCCSVH GWCGGGNDYC 100
    SGSKCQYRCS SSVRGPRVAL SGNSTANSIG NVVVTEPLFD QMFSHRKDCP 150
    SQGFYSYHSF LVAAESFPAF GTIGDVATRK REVAAFLAHI SQATSGERSD 200
    VENPHAWGLC HINTTTVTEN DFCTSSDWPC AAGKKYSPRG PIQLTHNFNY 250
    GLAGQAIGED LIQNPDLVEK DPIISFKTAL WFWMSQHDNK PSCHDIVLNA 300
    NSAANRIPNK GVIGNIISRA FGHDDFAVRS SSIGFYKRYC DMLGVSYGHD 350
    LKYWFDNTPS SEFQRIQMRV AA 372
    Length:372
    Mass (Da):40,542
    Last modified:December 1, 1992 - v3
    Checksum:i28E9A2312BF08FD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71S → A in AAD03614. (PubMed:10080699)Curated

    Mass spectrometryi

    Molecular mass is 9380 Da from positions 24 - 372. Determined by MALDI. 1 Publication
    Molecular mass is 9380.7±0.4 Da from positions 24 - 372. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87302 mRNA. Translation: AAA34219.1.
    AF059535 Genomic DNA. Translation: AAD03614.1.
    PIRiA44298. A42778.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87302 mRNA. Translation: AAA34219.1 .
    AF059535 Genomic DNA. Translation: AAD03614.1 .
    PIRi A44298. A42778.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EN2 X-ray 1.40 A 25-112 [» ]
    1ENM X-ray 1.90 A 25-112 [» ]
    1IQB X-ray 1.90 A/B 24-112 [» ]
    ProteinModelPortali P11218.
    SMRi P11218. Positions 24-112, 132-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11218. 1 interaction.
    MINTi MINT-8414736.

    Protein family/group databases

    CAZyi CBM18. Carbohydrate-Binding Module Family 18.
    GH19. Glycoside Hydrolase Family 19.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P11218.

    Family and domain databases

    Gene3Di 3.30.60.10. 2 hits.
    InterProi IPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001060. Endochitinase. 1 hit.
    ProDomi PD000609. Chitin_bd_1. 2 hits.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 2 hits.
    PROSITEi PS00026. CHIT_BIND_I_1. 2 hits.
    PS50941. CHIT_BIND_I_2. 2 hits.
    PS00773. CHITINASE_19_1. 1 hit.
    PS00774. CHITINASE_19_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase."
      Lerner D.R., Raikhel N.V.
      J. Biol. Chem. 267:11085-11091(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Erratum
      Lerner D.R., Raikhel N.V.
      J. Biol. Chem. 267:22694-22694(1992) [PubMed] [Europe PMC] [Abstract]
    3. "Characterization of Urtica dioica agglutinin isolectins and the encoding gene family."
      Does M.P., Ng D.K., Dekker H.L., Peumans W.J., Houterman P.M., Van Damme E.J., Cornelissen B.J.
      Plant Mol. Biol. 39:335-347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MASS SPECTROMETRY.
      Strain: cv. Weerselo.
    4. "The primary structure of stinging nettle (Urtica dioica) agglutinin. A two-domain member of the hevein family."
      Beintema J.J., Peumans W.J.
      FEBS Lett. 299:131-134(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-112.
    5. "Extensive homologies between lectins from non-leguminous plants."
      Chapot M.-P., Peumans W.J., Strosberg A.D.
      FEBS Lett. 195:231-234(1986)
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 24-54.
    6. "Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II."
      Saul F.A., Rovira P., Boulot G., van Damme E.J.M., Peumans W.J., Truffa-Bachi P., Bentley G.A.
      Structure 8:593-603(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 24-112 IN COMPLEX WITH TRI-ACETYLCHITOTRIOSE AND TETRA-ACETYLCHITOTETRAOSE, FUNCTION, INTERACTION WITH HUMAN TCR AND MHC, DISULFIDE BONDS.
    7. "Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site."
      Harata K., Schubert W.-D., Muraki M.
      Acta Crystallogr. D 57:1513-1517(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-112, SUBUNIT, ZINC BINDING, DISULFIDE BONDS.

    Entry informationi

    Entry nameiAGI_URTDI
    AccessioniPrimary (citable) accession number: P11218
    Secondary accession number(s): Q9SYR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3