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P00697

- LYSC1_RAT

UniProt

P00697 - LYSC1_RAT

Protein

Lysozyme C-1

Gene

Lyz1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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. In the intestine they may also have a digestive function.

    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 sitei71 – 711PROSITE-ProRule annotation

    GO - Molecular functioni

    1. hydrolase activity, acting on glycosyl bonds Source: RGD
    2. lysozyme activity Source: RGD

    GO - Biological processi

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

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

    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
    Gene namesi
    Name:Lyz1
    Synonyms:Lyz
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3026. Lyz.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. endoplasmic reticulum lumen Source: RGD
    3. extracellular region Source: UniProtKB-SubCell
    4. Golgi cis cisterna Source: RGD
    5. Golgi stack Source: RGD
    6. microvillus Source: RGD
    7. rough endoplasmic reticulum lumen Source: RGD
    8. secretory granule Source: RGD
    9. trans-Golgi network transport vesicle Source: RGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 148130Lysozyme C-1PRO_0000018484Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 146PROSITE-ProRule annotation
    Disulfide bondi48 ↔ 134PROSITE-ProRule annotation
    Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
    Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP00697.
    PRIDEiP00697.

    PTM databases

    PhosphoSiteiP00697.

    Expressioni

    Tissue specificityi

    Expressed in lung, small intestine and spleen.

    Gene expression databases

    GenevestigatoriP00697.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000007747.

    Structurei

    3D structure databases

    ProteinModelPortaliP00697.
    SMRiP00697. Positions 19-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85133.
    HOGENOMiHOG000037357.
    HOVERGENiHBG052297.
    InParanoidiP00697.
    PhylomeDBiP00697.

    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.

    P00697-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALLVLGFL LLSASVQAKI YERCQFARTL KRNGMSGYYG VSLADWVCLA    50
    QHESNYNTQA RNYNPGDQST DYGIFQINSR YWCNDGKTPR AKNACGIPCS 100
    ALLQDDITQA IQCAKRVVRD PQGIRAWVAW QRHCKNRDLS GYIRNCGV 148
    Length:148
    Mass (Da):16,729
    Last modified:October 1, 1994 - v2
    Checksum:i8E6E986539BD3EEE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201I → T AA sequence (PubMed:851497)Curated
    Sequence conflicti64 – 641N → D AA sequence (PubMed:851497)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12459 Genomic DNA. Translation: AAA41551.1.
    PIRiA40729. LZRT.
    UniGeneiRn.2283.

    Genome annotation databases

    UCSCiRGD:3026. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12459 Genomic DNA. Translation: AAA41551.1 .
    PIRi A40729. LZRT.
    UniGenei Rn.2283.

    3D structure databases

    ProteinModelPortali P00697.
    SMRi P00697. Positions 19-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000007747.

    Chemistry

    BindingDBi P00697.
    ChEMBLi CHEMBL2297.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    PTM databases

    PhosphoSitei P00697.

    Proteomic databases

    PaxDbi P00697.
    PRIDEi P00697.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:3026. rat.

    Organism-specific databases

    RGDi 3026. Lyz.

    Phylogenomic databases

    eggNOGi NOG85133.
    HOGENOMi HOG000037357.
    HOVERGENi HBG052297.
    InParanoidi P00697.
    PhylomeDBi P00697.

    Gene expression databases

    Genevestigatori P00697.

    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. "Evolution of rodent lysozymes: isolation and sequence of the rat lysozyme genes."
      Yeh T.C., Wilson A.C., Irwin D.M.
      Mol. Phylogenet. Evol. 2:65-75(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sprague-Dawley.
    2. Cited for: PROTEIN SEQUENCE OF 19-148.
      Strain: Wistar.

    Entry informationi

    Entry nameiLYSC1_RAT
    AccessioniPrimary (citable) accession number: P00697
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 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.
    Rat has two lysozymes, type 1 and type 2 of which only type 1 is expressed; type 2 being probably a pseudogene.

    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