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Q9TUN1

- LYSC3_SHEEP

UniProt

Q9TUN1 - LYSC3_SHEEP

Protein

Lysozyme C-3

Gene
N/A
Organism
Ovis aries (Sheep)
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 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-3 (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    OrganismiOvis aries (Sheep)
    Taxonomic identifieri9940 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
    ProteomesiUP000002356: Unplaced

    Subcellular locationi

    Secreted By similarity

    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 – 1818By similarityAdd
    BLAST
    Chaini19 – 147129Lysozyme C-3PRO_0000018489Add
    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

    Expressed in stomach.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TUN1.
    SMRiQ9TUN1. 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.

    Q9TUN1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALVILGLL FLSVAVQGKV FERCELARTL KKLGLDDYKG VSLANWLCLS    50
    KWESGYNTKA TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS 100
    ALMENDIEKA VACAKHIVSE QGITAWVAWK SHCRVHDVSS YVEGCKL 147
    Length:147
    Mass (Da):16,265
    Last modified:May 1, 2000 - v1
    Checksum:i09601329F793EBD9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170559
    , AF170556, AF170557, AF170558 Genomic DNA. Translation: AAD51637.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170559
    , AF170556 , AF170557 , AF170558 Genomic DNA. Translation: AAD51637.1 .

    3D structure databases

    ProteinModelPortali Q9TUN1.
    SMRi Q9TUN1. Positions 19-147.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    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. "Mosaic evolution of ruminant stomach lysozyme genes."
      Wen Y., Irwin D.M.
      Mol. Phylogenet. Evol. 13:474-482(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiLYSC3_SHEEP
    AccessioniPrimary (citable) accession number: Q9TUN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 63 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.

    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