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P29615

- LYSP_DROME

UniProt

P29615 - LYSP_DROME

Protein

Lysozyme P

Gene

LysP

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food.2 Publications

    Catalytic activityi

    Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei51 – 511PROSITE-ProRule annotation
    Active sitei69 – 691PROSITE-ProRule annotation

    GO - Molecular functioni

    1. lysozyme activity Source: FlyBase

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_180705. Amyloids.

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme P (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase P
    Gene namesi
    Name:LysP
    ORF Names:CG9116
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0004429. LysP.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 141123Lysozyme PPRO_0000018514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi25 ↔ 140PROSITE-ProRule annotation
    Disulfide bondi46 ↔ 130PROSITE-ProRule annotation
    Disulfide bondi81 ↔ 97PROSITE-ProRule annotation
    Disulfide bondi93 ↔ 111PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP29615.

    Expressioni

    Tissue specificityi

    Salivary gland.2 Publications

    Developmental stagei

    Only expressed in adults.2 Publications

    Gene expression databases

    BgeeiP29615.

    Structurei

    3D structure databases

    ProteinModelPortaliP29615.
    SMRiP29615. Positions 20-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85133.
    GeneTreeiENSGT00550000074398.
    InParanoidiP29615.
    KOiK13915.
    OMAiWESSFNT.
    OrthoDBiEOG7BW0M5.
    PhylomeDBiP29615.

    Family and domain databases

    InterProiIPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00062. Lys. 1 hit.
    [Graphical view]
    PRINTSiPR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTiSM00263. LYZ1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29615-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAFLVICAL TLTAVATQAR TMDRCSLARE MSKLGVPRDQ LAKWTCIAQH    50
    ESSFRTGVVG PANSNGSNDY GIFQINNKYW CKPADGRFSY NECGLSCNAL 100
    LTDDITNSVK CARKIQRQQG WTAWSTWKYC SGSLPSINSC F 141
    Length:141
    Mass (Da):15,648
    Last modified:April 1, 1993 - v1
    Checksum:i4D7C51B018FD5417
    GO

    Sequence cautioni

    The sequence ABK57077.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58383 Genomic DNA. Translation: CAA41273.1.
    AE014296 Genomic DNA. Translation: AAF47452.1.
    BT023249 mRNA. Translation: AAY55665.1.
    BT029420 mRNA. Translation: ABK57077.1. Different initiation.
    PIRiS20915.
    RefSeqiNP_476828.1. NM_057480.5.
    UniGeneiDm.24595.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072633; FBpp0072529; FBgn0004429.
    GeneIDi38129.
    KEGGidme:Dmel_CG9116.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58383 Genomic DNA. Translation: CAA41273.1 .
    AE014296 Genomic DNA. Translation: AAF47452.1 .
    BT023249 mRNA. Translation: AAY55665.1 .
    BT029420 mRNA. Translation: ABK57077.1 . Different initiation.
    PIRi S20915.
    RefSeqi NP_476828.1. NM_057480.5.
    UniGenei Dm.24595.

    3D structure databases

    ProteinModelPortali P29615.
    SMRi P29615. Positions 20-141.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PRIDEi P29615.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072633 ; FBpp0072529 ; FBgn0004429 .
    GeneIDi 38129.
    KEGGi dme:Dmel_CG9116.

    Organism-specific databases

    CTDi 38129.
    FlyBasei FBgn0004429. LysP.

    Phylogenomic databases

    eggNOGi NOG85133.
    GeneTreei ENSGT00550000074398.
    InParanoidi P29615.
    KOi K13915.
    OMAi WESSFNT.
    OrthoDBi EOG7BW0M5.
    PhylomeDBi P29615.

    Enzyme and pathway databases

    Reactomei REACT_180705. Amyloids.

    Miscellaneous databases

    GenomeRNAii 38129.
    NextBioi 807110.

    Gene expression databases

    Bgeei P29615.

    Family and domain databases

    InterProi IPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00062. Lys. 1 hit.
    [Graphical view ]
    PRINTSi PR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTi SM00263. LYZ1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands."
      Kylsten P., Kimbrell D.A., Daffre S., Samakovlis C., Hultmark D.
      Mol. Gen. Genet. 232:335-343(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
    2. "The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract."
      Daffre S., Kylsten P., Samakovlis C., Hultmark D.
      Mol. Gen. Genet. 242:152-162(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.

    Entry informationi

    Entry nameiLYSP_DROME
    AccessioniPrimary (citable) accession number: P29615
    Secondary accession number(s): A0JQ50, Q4V3V7, Q9W0J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3