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P21226

- CHI2_PEA

UniProt

P21226 - CHI2_PEA

Protein

Endochitinase A2

Gene

CHI2

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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 A2 (EC:3.2.1.14)
    Gene namesi
    Name:CHI2
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 309289Endochitinase A2PRO_0000005308Add
    BLAST
    Propeptidei310 – 32415Removed in mature formBy similarityPRO_0000005309Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 38PROSITE-ProRule annotation
    Disulfide bondi32 ↔ 44PROSITE-ProRule annotation
    Disulfide bondi37 ↔ 51PROSITE-ProRule annotation
    Disulfide bondi55 ↔ 59PROSITE-ProRule annotation
    Disulfide bondi151 ↔ 170PROSITE-ProRule annotation
    Disulfide bondi269 ↔ 301PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    By infection with the fungal pathogen Ascochyta pisi.

    Structurei

    3D structure databases

    ProteinModelPortaliP21226.
    SMRiP21226. Positions 21-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 6141Chitin-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.
    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.

    P21226-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKLRIPILL VLFIVSCCSA EQCGTQAGGA LCPGGLCCSK FGWCGSTSEY    50
    CGDGCQSQCS GSSGGGTLSS LISGDTFNNM LKHRNDNACQ GKPFYTYDAF 100
    LSAAKAFPNF ANKGDTATKK REIAAFLGQT SHETTGGWPT APDGPYAWGY 150
    CFLREQNPST YCQASSEFPC ASGKQYYGRG PIQISWNYNY GQCGRAIGVD 200
    LLNNPDLVAT DPVISFKTAL WFWMTPQSPK PSCHDVITGG WTPSSADRAA 250
    GRLPGYGTVT NIINGGLECG RGQDSRVQDR IGFYKRYCDI FGIGYGDNLD 300
    CYSQRPFGSS LPLSSILLDT VAAA 324
    Length:324
    Mass (Da):34,678
    Last modified:October 1, 1996 - v2
    Checksum:i540F0DA5EC1DC2FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37876 Genomic DNA. Translation: AAA75196.1.
    PIRiS56694.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37876 Genomic DNA. Translation: AAA75196.1 .
    PIRi S56694.

    3D structure databases

    ProteinModelPortali P21226.
    SMRi P21226. Positions 21-307.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    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.
    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. "Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan."
      Chang M.M., Horovitz D., Culley D., Hadwiger L.A.
      Plant Mol. Biol. 28:105-111(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Alcan.
    2. "Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi."
      Vad K., Mikkelsen J.D., Collinge D.B.
      Planta 184:24-29(1991)
      Cited for: PROTEIN SEQUENCE OF 21-36.
      Strain: cv. Birte.
      Tissue: Leaf.

    Entry informationi

    Entry nameiCHI2_PEA
    AccessioniPrimary (citable) accession number: P21226
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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