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P08252

- CHI1_TOBAC

UniProt

P08252 - CHI1_TOBAC

Protein

Endochitinase A

Gene

CHN48

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Defense against chitin containing fungal pathogens.

    Catalytic activityi

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

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB-EC
    2. chitin binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-KW
    3. defense response Source: UniProtKB-KW
    4. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endochitinase A (EC:3.2.1.14)
    Short name:
    CHN-A
    Gene namesi
    Name:CHN48
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    Subcellular locationi

    Vacuole 1 Publication
    Note: Vacuolar and protoplast.

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 322299Endochitinase APRO_0000005330Add
    BLAST
    Propeptidei323 – 3297Removed in mature formPRO_0000005331

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 41PROSITE-ProRule annotation
    Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
    Disulfide bondi40 ↔ 54PROSITE-ProRule annotation
    Disulfide bondi59 ↔ 63PROSITE-ProRule annotation
    Modified residuei67 – 6714-hydroxyproline; partial1 Publication
    Modified residuei69 – 6914-hydroxyproline1 Publication
    Modified residuei71 – 7114-hydroxyproline1 Publication
    Modified residuei72 – 7214-hydroxyproline1 Publication
    Modified residuei74 – 7414-hydroxyproline1 Publication
    Modified residuei75 – 7514-hydroxyproline; partial1 Publication
    Disulfide bondi101 ↔ 163PROSITE-ProRule annotation
    Disulfide bondi175 ↔ 183PROSITE-ProRule annotation
    Disulfide bondi282 ↔ 314PROSITE-ProRule annotation

    Post-translational modificationi

    The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.

    Keywords - PTMi

    Disulfide bond, Hydroxylation

    Proteomic databases

    ProMEXiP08252.

    Expressioni

    Developmental stagei

    Expressed during flower formation.1 Publication

    Inductioni

    By ethylene.

    Structurei

    3D structure databases

    ProteinModelPortaliP08252.
    SMRiP08252. Positions 24-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 6542Chitin-binding type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.30.60.10. 1 hit.
    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.
    PRINTSiPR00451. CHITINBINDNG.
    ProDomiPD000609. Chitin_bd_1. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00270. ChtBD1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
    PS50941. CHIT_BIND_I_2. 1 hit.
    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.

    P08252-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLCKFTALS SLLFSLLLLS ASAEQCGSQA GGARCPSGLC CSKFGWCGNT    50
    NDYCGPGNCQ SQCPGGPTPT PPTPPGGGDL GSIISSSMFD QMLKHRNDNA 100
    CQGKGFYSYN AFINAARSFP GFGTSGDTTA RKREIAAFFA QTSHETTGGW 150
    ATAPDGPYAW GYCWLREQGS PGDYCTPSGQ WPCAPGRKYF GRGPIQISHN 200
    YNYGPCGRAI GVDLLNNPDL VATDPVISFK SALWFWMTPQ SPKPSCHDVI 250
    IGRWQPSAGD RAANRLPGFG VITNIINGGL ECGRGTDSRV QDRIGFYRRY 300
    CSILGVSPGD NLDCGNQRSF GNGLLVDTM 329
    Length:329
    Mass (Da):35,156
    Last modified:August 1, 1990 - v2
    Checksum:i3EC99D96E6C0114C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 786TPPGGG → HPTRC in AAB23374. (PubMed:2152343)Curated
    Sequence conflicti263 – 2631A → S in AAB23374. (PubMed:2152343)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16938 Genomic DNA. Translation: CAA34812.1.
    X16939 mRNA. Translation: CAA34813.1.
    S44869 mRNA. Translation: AAB23374.1.
    PIRiS08627.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16938 Genomic DNA. Translation: CAA34812.1 .
    X16939 mRNA. Translation: CAA34813.1 .
    S44869 mRNA. Translation: AAB23374.1 .
    PIRi S08627.

    3D structure databases

    ProteinModelPortali P08252.
    SMRi P08252. Positions 24-320.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    ProMEXi P08252.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.30.60.10. 1 hit.
    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.
    PRINTSi PR00451. CHITINBINDNG.
    ProDomi PD000609. Chitin_bd_1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEi PS00026. CHIT_BIND_I_1. 1 hit.
    PS50941. CHIT_BIND_I_2. 1 hit.
    PS00773. CHITINASE_19_1. 1 hit.
    PS00774. CHITINASE_19_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain."
      Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr.
      Plant Mol. Biol. 14:357-368(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: cv. Havana 425.
      Tissue: Leaf.
    2. "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation."
      Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R., Peacock W.J., Dennis E.S.
      Plant Cell 2:673-684(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
      Strain: cv. Samsun.
      Tissue: Flower bud.
    3. "A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole."
      Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.
      Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    4. "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins."
      Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.
      Science 257:655-657(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-67; PRO-69; PRO-71; PRO-72; PRO-74 AND PRO-75, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCHI1_TOBAC
    AccessioniPrimary (citable) accession number: P08252
    Secondary accession number(s): Q41180
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3