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P05105

- LYS_HYACE

UniProt

P05105 - LYS_HYACE

Protein

Lysozyme

Gene
N/A
Organism
Hyalophora cecropia (Cecropia moth)
Status
Reviewed - Annotation score: 4 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.

    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: 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 (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase
    OrganismiHyalophora cecropia (Cecropia moth)
    Taxonomic identifieri7123 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSaturniidaeSaturniinaeAttaciniHyalophora

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 139120LysozymePRO_0000018506Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi25 ↔ 139PROSITE-ProRule annotation
    Disulfide bondi46 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi81 ↔ 95PROSITE-ProRule annotation
    Disulfide bondi91 ↔ 109PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP05105.
    SMRiP05105. Positions 20-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

    P05105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKYVILLAV LAFALHCDAK RFTRCGLVQE LRRLGFDETL MSNWVCLVEN    50
    ESGRFTDKIG KVNKNGSRDY GLFQINDKYW CSKGTTPGKD CNVTCNQLLT 100
    DDISVAATCA KKIYKRHKFD AWYGWKNHCQ HGLPDISDC 139
    Length:139
    Mass (Da):15,877
    Last modified:May 1, 1992 - v2
    Checksum:iE8AF5C2CE561F641
    GO

    Sequence cautioni

    The sequence AAA29190.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA26542.1 differs from that shown. Reason: Erroneous initiation.

    Polymorphismi

    3 allelic variants of cecropia moth lysozyme have been found. The sequence shown is that of lysozyme 1.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341L → R in lysozyme-2.
    Natural varianti85 – 851T → S in lysozyme-2 and lysozyme-3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60914 Genomic DNA. Translation: AAA29189.1.
    X02765 mRNA. Translation: CAA26542.1. Different initiation.
    M34923 mRNA. Translation: AAA29190.1. Different initiation.
    PIRiA24649. LZWK.
    A38744.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60914 Genomic DNA. Translation: AAA29189.1 .
    X02765 mRNA. Translation: CAA26542.1 . Different initiation.
    M34923 mRNA. Translation: AAA29190.1 . Different initiation.
    PIRi A24649. LZWK.
    A38744.

    3D structure databases

    ProteinModelPortali P05105.
    SMRi P05105. Positions 20-139.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia."
      Sun S.-C., Aasling B., Faye I.
      J. Biol. Chem. 266:6644-6649(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia."
      Engstroem A., Xanthopoulos K.G., Boman H.G., Bennich H.
      EMBO J. 4:2119-2122(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 13-139.
    3. "On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia."
      Boman H.G., Faye I., von Hofsten P., Kockum K., Lee J.-Y., Xanthopoulos K.G., Bennich H., Engstroem A., Merrifield R.B., Andreu D.
      Dev. Comp. Immunol. 9:551-558(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 13-139.

    Entry informationi

    Entry nameiLYS_HYACE
    AccessioniPrimary (citable) accession number: P05105
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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