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Q17005

- LYSC1_ANOGA

UniProt

Q17005 - LYSC1_ANOGA

Protein

Lysozyme c-1

Gene

AGAP007347

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.1 PublicationPROSITE-ProRule annotation

    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 sitei52 – 521PROSITE-ProRule annotation
    Active sitei69 – 691PROSITE-ProRule annotation

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    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

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme c-1 (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase
    Gene namesi
    ORF Names:AGAP007347
    OrganismiAnopheles gambiae (African malaria mosquito)
    Taxonomic identifieri7165 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
    ProteomesiUP000007062: Chromosome 2L

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 140120Lysozyme c-1PRO_0000018504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 139PROSITE-ProRule annotation
    Disulfide bondi47 ↔ 128PROSITE-ProRule annotation
    Disulfide bondi81 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi90 ↔ 108PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed in salivary glands and Malpighian tubules.1 Publication

    Developmental stagei

    Expressed at all developmental stages, highest expression is in the adult.1 Publication

    Inductioni

    By bacterial infection, expression significantly increases 6-12 hours post challenge with bacteria.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi7165.AGAP007347-PA.

    Structurei

    3D structure databases

    ProteinModelPortaliQ17005.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85133.
    HOGENOMiHOG000037357.
    InParanoidiQ4ZIL2.
    KOiK13915.
    OMAiGNGMNAW.
    OrthoDBiEOG7BW0M5.
    PhylomeDBiQ17005.

    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.

    Q17005-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVFSTVLLA IVACCAVAEA KTFGKCELAK ALANNGIAKA SLPDWVCLVQ    50
    NESAFSTSAT NKNKNGSTDY GIFQINNKYW CDSGYGSNDC KIACKNLLND 100
    DITDDIKCAK LIHKRHGFNA WYGWKNHCNG KKLPNVSSCF 140
    Length:140
    Mass (Da):15,338
    Last modified:May 16, 2006 - v2
    Checksum:iD30D604699316D24
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51S → F in AAC47326. (PubMed:8890741)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28809 Genomic DNA. Translation: AAC47326.1.
    DQ007317 mRNA. Translation: AAY24699.1.
    AAAB01008807 Genomic DNA. Translation: EAA45417.1.
    PIRiJC5003.
    RefSeqiXP_308481.1. XM_308481.3.

    Genome annotation databases

    EnsemblMetazoaiAGAP007347-RA; AGAP007347-PA; AGAP007347.
    GeneIDi1269831.
    KEGGiaga:AgaP_AGAP007347.
    VectorBaseiAGAP007347. Anopheles gambiae.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28809 Genomic DNA. Translation: AAC47326.1 .
    DQ007317 mRNA. Translation: AAY24699.1 .
    AAAB01008807 Genomic DNA. Translation: EAA45417.1 .
    PIRi JC5003.
    RefSeqi XP_308481.1. XM_308481.3.

    3D structure databases

    ProteinModelPortali Q17005.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7165.AGAP007347-PA.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai AGAP007347-RA ; AGAP007347-PA ; AGAP007347 .
    GeneIDi 1269831.
    KEGGi aga:AgaP_AGAP007347.
    VectorBasei AGAP007347. Anopheles gambiae.

    Organism-specific databases

    CTDi 1269831.

    Phylogenomic databases

    eggNOGi NOG85133.
    HOGENOMi HOG000037357.
    InParanoidi Q4ZIL2.
    KOi K13915.
    OMAi GNGMNAW.
    OrthoDBi EOG7BW0M5.
    PhylomeDBi Q17005.

    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. "Analysis of a lysozyme gene from the malaria vector mosquito, Anopheles gambiae."
      Kang D., Romans P., Lee J.Y.
      Gene 174:239-244(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characterization of the c-type lysozyme gene family in Anopheles gambiae."
      Li B., Calvo E., Marinotti O., James A.A., Paskewitz S.M.
      Gene 360:131-139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: Pinkeye.
    3. "The genome sequence of the malaria mosquito Anopheles gambiae."
      Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F.
      , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
      Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PEST.

    Entry informationi

    Entry nameiLYSC1_ANOGA
    AccessioniPrimary (citable) accession number: Q17005
    Secondary accession number(s): Q4ZIL2, Q7PF88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    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