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P00705

- LYSC1_ANAPL

UniProt

P00705 - LYSC1_ANAPL

Protein

Lysozyme C-1

Gene
N/A
Organism
Anas platyrhynchos (Domestic duck) (Anas boschas)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein 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 sitei53 – 531PROSITE-ProRule annotation
    Active sitei70 – 701PROSITE-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 C
    OrganismiAnas platyrhynchos (Domestic duck) (Anas boschas)
    Taxonomic identifieri8839 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas
    ProteomesiUP000016666: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 147129Lysozyme C-1PRO_0000018494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 1451 PublicationPROSITE-ProRule annotation
    Disulfide bondi48 ↔ 1331 PublicationPROSITE-ProRule annotation
    Disulfide bondi82 ↔ 981 PublicationPROSITE-ProRule annotation
    Disulfide bondi94 ↔ 1121 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP00705.

    Structurei

    3D structure databases

    ProteinModelPortaliP00705.
    SMRiP00705. Positions 19-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG052297.

    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.

    P00705-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALLTLVFC LLPLAAQGKV YSRCELAAAM KRLGLDNYRG YSLGNWVCAA    50
    NYESGFNTQA TNRNTDGSTD YGILQINSRW WCDNGKTPRS KNACGIPCSV 100
    LLRSDITEAV RCAKRIVSDG DGMNAWVAWR NRCRGTDVSK WIRGCRL 147
    Length:147
    Mass (Da):16,363
    Last modified:July 21, 1986 - v1
    Checksum:iB0F2B6A9F7DA3978
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431L → I in DL3.
    Natural varianti55 – 551G → S in DL1 and lysozyme II.
    Natural varianti75 – 751Q → E in lysozyme II.
    Natural varianti89 – 891R → G in DL1 and lysozyme II.
    Natural varianti97 – 971P → R in DL3.

    Sequence databases

    PIRiD92574. LZDK.

    Cross-referencesi

    Sequence databases

    PIRi D92574. LZDK.

    3D structure databases

    ProteinModelPortali P00705.
    SMRi P00705. Positions 19-147.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PRIDEi P00705.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    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. "Evolutionary shift in the site of cleavage of prelysozyme."
      Weisman L.S., Krummel B.M., Wilson A.C.
      J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18.
      Strain: Pekin breed.
    2. "Chemical and immunological properties and amino acid sequences of three lysozymes from Peking-duck egg white."
      Kondo K., Fujio H., Amano T.
      J. Biochem. 91:571-587(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-147 (DL-1; DL-2 AND DL-3).
      Strain: Pekin breed.
    3. "Multiple forms of duck-egg white lysozyme. Primary structure of two duck lysozymes."
      Hermann J., Jolles J., Jolles P.
      Eur. J. Biochem. 24:12-17(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-147 (LYSOZYME II).
    4. "The disulfide bridges of duck egg-white lysozyme II."
      Hermann J., Jolles J., Jolles P.
      Arch. Biochem. Biophys. 158:355-358(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    5. "Multiple lysozymes of duck egg white."
      Prager E.M., Wilson A.C.
      J. Biol. Chem. 246:523-530(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C.
      Strain: Pekin breed.

    Entry informationi

    Entry nameiLYSC1_ANAPL
    AccessioniPrimary (citable) accession number: P00705
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
    The sequence of the DL-2 variant of lysozyme C from Pekin duck is shown. As only one lysozyme, or any combination of 2 lysozymes, but never all 3, occurred in one egg, the existence of 3 alleles at one locus has been suggested.
    The amino acid compositions of DL-1, DL-2, and DL-3 are identical with those of lysozymes A, B, and C, respectively. DL-1 and DL-2 are electrophoretically and immunologically indistinguishable from lysozymes A and B, respectively.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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