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P04421

- LYSC_BOVIN

UniProt

P04421 - LYSC_BOVIN

Protein

Lysozyme C

Gene

LYZ1

Organism
Bos taurus (Bovine)
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.

    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. 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
    4. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Keywords - Biological processi

    Digestion

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    Gene namesi
    Name:LYZ1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 147129Lysozyme CPRO_0000018453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 145PROSITE-ProRule annotation
    Disulfide bondi48 ↔ 133PROSITE-ProRule annotation
    Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
    Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Stomach-specific.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000007924.

    Structurei

    3D structure databases

    ProteinModelPortaliP04421.
    SMRiP04421. 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.
    InParanoidiP04421.
    KOiK01185.
    K13915.

    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.

    P04421-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT    50
    KWESSYNTKA TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCR 100
    ELMENDIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCTL 147
    Length:147
    Mass (Da):16,373
    Last modified:October 1, 1989 - v2
    Checksum:iC678E7EECE1E66BF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → T in isozyme 2A.
    Natural varianti5 – 51V → I in isozyme 1 and isozyme 3.
    Natural varianti17 – 171Q → K in isozyme 2C.
    Natural varianti45 – 451N → S in isozyme 2D.
    Natural varianti66 – 661S → G in isozyme 1.
    Natural varianti106 – 1061D → E in isozyme 1.
    Natural varianti116 – 1161H → Q in isozyme 1.
    Natural varianti143 – 1431E → Q in isozyme 3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26246 mRNA. Translation: AAA30627.1.
    M26245 mRNA. Translation: AAA30626.1.
    M26242 mRNA. Translation: AAA30632.1.
    M26241 mRNA. Translation: AAA30628.1.
    M26243 mRNA. Translation: AAA30629.1.
    M26244 mRNA. Translation: AAA30630.1.
    M26240 mRNA. Translation: AAA30631.1.
    RefSeqiNP_001073808.1. NM_001080339.1.
    NP_776529.1. NM_174104.2.
    NP_851342.1. NM_180999.1.
    UniGeneiBt.29367.
    Bt.80498.
    Bt.89770.

    Genome annotation databases

    GeneIDi280849.
    281289.
    781349.
    KEGGibta:280849.
    bta:281289.
    bta:781349.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26246 mRNA. Translation: AAA30627.1 .
    M26245 mRNA. Translation: AAA30626.1 .
    M26242 mRNA. Translation: AAA30632.1 .
    M26241 mRNA. Translation: AAA30628.1 .
    M26243 mRNA. Translation: AAA30629.1 .
    M26244 mRNA. Translation: AAA30630.1 .
    M26240 mRNA. Translation: AAA30631.1 .
    RefSeqi NP_001073808.1. NM_001080339.1.
    NP_776529.1. NM_174104.2.
    NP_851342.1. NM_180999.1.
    UniGenei Bt.29367.
    Bt.80498.
    Bt.89770.

    3D structure databases

    ProteinModelPortali P04421.
    SMRi P04421. Positions 19-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000007924.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 280849.
    281289.
    781349.
    KEGGi bta:280849.
    bta:281289.
    bta:781349.

    Organism-specific databases

    CTDi 17105.
    281289.

    Phylogenomic databases

    HOVERGENi HBG052297.
    InParanoidi P04421.
    KOi K01185.
    K13915.

    Miscellaneous databases

    NextBioi 20804997.

    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. "Multiple cDNA sequences and the evolution of bovine stomach lysozyme."
      Irwin D.M., Wilson A.C.
      J. Biol. Chem. 264:11387-11393(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes."
      Jolles P., Schoentgen F., Jolles J., Dobson D.E., Prager E.M., Wilson A.C.
      J. Biol. Chem. 259:11617-11625(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-147 (2B).
    3. Cited for: SEQUENCE REVISION TO 116 (2B).

    Entry informationi

    Entry nameiLYSC_BOVIN
    AccessioniPrimary (citable) accession number: P04421
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 108 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.
    The ruminant gastric lysozymes, which digest symbiotic bacteria coming with cud from the rumen, are much more resistant to inactivation by pepsin than are other lysozymes.
    Three non-allelic lysozymes C are present in the gastric mucosa of cattle.
    The sequence of isozyme 2B is shown.

    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