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P37161

- LYSX_DROME

UniProt

P37161 - LYSX_DROME

Protein

Lysozyme X

Gene

LysX

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 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. May be involved in the clearance of bacteria from the larval gut before metamorphosis.

    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 X (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase X
    Gene namesi
    Name:LysX
    ORF Names:CG9120
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0004431. LysX.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 142123Lysozyme XPRO_0000018516Add
    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

    PaxDbiP37161.
    PRIDEiP37161.

    Expressioni

    Tissue specificityi

    Found in the midgut.

    Developmental stagei

    Rises dramatically in the late third instar, then decreases gradually during the pupal stages. Low expression is found in adults.

    Gene expression databases

    BgeeiP37161.

    Interactioni

    Protein-protein interaction databases

    BioGridi63669. 1 interaction.
    DIPiDIP-24095N.
    MINTiMINT-1674138.
    STRINGi7227.FBpp0072533.

    Structurei

    3D structure databases

    ProteinModelPortaliP37161.
    SMRiP37161. Positions 20-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG281116.
    GeneTreeiENSGT00550000074398.
    InParanoidiP37161.
    KOiK01185.
    OMAiQGMDGYR.
    OrthoDBiEOG7BW0M5.
    PhylomeDBiP37161.

    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.

    P37161-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRALLGICVL ALVTPAVLGR TMDRCSLARE MANMGVSRDQ LSKWACIAEH    50
    ESSYRTGVVG PPNTDGSNDY GIFQINDMYW CQPSSGKFSH NGCDVSCNAL 100
    LTDDIKSSVR CALKVLGQQG WSAWSTWHYC SGYLPPIDDC FV 142
    Length:142
    Mass (Da):15,591
    Last modified:December 1, 2000 - v2
    Checksum:i2A48035364B995BC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61G → T in strain: G140. 1 Publication
    Natural varianti78 – 781M → L in strain: Canton-S, G02, G130 and G140. 1 Publication
    Natural varianti94 – 941D → G in strain: G130 and G140. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM412869 Genomic DNA. Translation: CAL85492.1.
    AM412870 Genomic DNA. Translation: CAL85493.1.
    AM412871 Genomic DNA. Translation: CAL85494.1.
    AM412872 Genomic DNA. Translation: CAL85495.1.
    AE014296 Genomic DNA. Translation: AAF47445.1.
    AY119081 mRNA. Translation: AAM50941.1.
    Z22224 mRNA. Translation: CAA80226.1.
    PIRiS41580.
    RefSeqiNP_523881.1. NM_079157.2.
    UniGeneiDm.19201.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072637; FBpp0072533; FBgn0004431.
    GeneIDi38122.
    KEGGidme:Dmel_CG9120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM412869 Genomic DNA. Translation: CAL85492.1 .
    AM412870 Genomic DNA. Translation: CAL85493.1 .
    AM412871 Genomic DNA. Translation: CAL85494.1 .
    AM412872 Genomic DNA. Translation: CAL85495.1 .
    AE014296 Genomic DNA. Translation: AAF47445.1 .
    AY119081 mRNA. Translation: AAM50941.1 .
    Z22224 mRNA. Translation: CAA80226.1 .
    PIRi S41580.
    RefSeqi NP_523881.1. NM_079157.2.
    UniGenei Dm.19201.

    3D structure databases

    ProteinModelPortali P37161.
    SMRi P37161. Positions 20-141.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63669. 1 interaction.
    DIPi DIP-24095N.
    MINTi MINT-1674138.
    STRINGi 7227.FBpp0072533.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PaxDbi P37161.
    PRIDEi P37161.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072637 ; FBpp0072533 ; FBgn0004431 .
    GeneIDi 38122.
    KEGGi dme:Dmel_CG9120.

    Organism-specific databases

    CTDi 38122.
    FlyBasei FBgn0004431. LysX.

    Phylogenomic databases

    eggNOGi NOG281116.
    GeneTreei ENSGT00550000074398.
    InParanoidi P37161.
    KOi K01185.
    OMAi QGMDGYR.
    OrthoDBi EOG7BW0M5.
    PhylomeDBi P37161.

    Enzyme and pathway databases

    Reactomei REACT_180705. Amyloids.

    Miscellaneous databases

    GenomeRNAii 38122.
    NextBioi 807080.

    Gene expression databases

    Bgeei P37161.

    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. "A screen for immunity genes evolving under positive selection in Drosophila."
      Jiggins F.M., Kim K.W.
      J. Evol. Biol. 20:965-970(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-6; LEU-78 AND GLY-94.
      Strain: G02, G130, G140 and G28.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Larva and Pupae.
    5. "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 [MRNA] OF 62-142.
      Strain: Canton-S.

    Entry informationi

    Entry nameiLYSX_DROME
    AccessioniPrimary (citable) accession number: P37161
    Secondary accession number(s): A4V9W9
    , A4V9X0, A4V9X1, A4V9X2, Q9W0K1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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