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Q06283

- LYSC2_BOVIN

UniProt

Q06283 - LYSC2_BOVIN

Protein

Lysozyme C-2

Gene

LYZ2

Organism
Bos taurus (Bovine)
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 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

    Enzyme and pathway databases

    ReactomeiREACT_206540. Amyloids.

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C-2 (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    Gene namesi
    Name:LYZ2
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 5

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 147129Lysozyme C-2PRO_0000018455Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 1451 PublicationPROSITE-ProRule annotation
    Disulfide bondi48 ↔ 1331 PublicationPROSITE-ProRule annotation
    Disulfide bondi83 ↔ 991 PublicationPROSITE-ProRule annotation
    Disulfide bondi95 ↔ 1131 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Stomach-specific.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3210
    Helixi43 – 5412
    Beta strandi61 – 644
    Turni65 – 684
    Beta strandi69 – 724
    Turni73 – 764
    Turni79 – 813
    Beta strandi82 – 843
    Beta strandi88 – 903
    Beta strandi96 – 983
    Helixi99 – 1035
    Beta strandi104 – 1063
    Helixi108 – 12114
    Helixi123 – 1253
    Helixi127 – 1326
    Turni133 – 1353
    Helixi139 – 1424

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z2FX-ray1.50A19-147[»]
    ProteinModelPortaliQ06283.
    SMRiQ06283. Positions 19-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06283.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85133.
    GeneTreeiENSGT00550000074398.
    HOGENOMiHOG000037357.
    HOVERGENiHBG052297.
    InParanoidiQ06283.
    KOiK13915.
    OMAiSCELART.
    OrthoDBiEOG7BW0M5.
    TreeFamiTF324882.

    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.

    Q06283-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT    50
    KWESSYNTKA TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS 100
    ELMENDIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCTL 147
    Length:147
    Mass (Da):16,304
    Last modified:January 1, 1999 - v2
    Checksum:iB0A38B9ECE1E66BE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95098 Unassigned DNA. Translation: AAC37311.1.
    PIRiC34277. LZBO.
    RefSeqiNP_851342.1. NM_180999.1.
    UniGeneiBt.29367.

    Genome annotation databases

    EnsembliENSBTAT00000007924; ENSBTAP00000007924; ENSBTAG00000026088.
    GeneIDi280849.
    KEGGibta:280849.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95098 Unassigned DNA. Translation: AAC37311.1 .
    PIRi C34277. LZBO.
    RefSeqi NP_851342.1. NM_180999.1.
    UniGenei Bt.29367.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z2F X-ray 1.50 A 19-147 [» ]
    ProteinModelPortali Q06283.
    SMRi Q06283. 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...

    Genome annotation databases

    Ensembli ENSBTAT00000007924 ; ENSBTAP00000007924 ; ENSBTAG00000026088 .
    GeneIDi 280849.
    KEGGi bta:280849.

    Organism-specific databases

    CTDi 17105.

    Phylogenomic databases

    eggNOGi NOG85133.
    GeneTreei ENSGT00550000074398.
    HOGENOMi HOG000037357.
    HOVERGENi HBG052297.
    InParanoidi Q06283.
    KOi K13915.
    OMAi SCELART.
    OrthoDBi EOG7BW0M5.
    TreeFami TF324882.

    Enzyme and pathway databases

    Reactomei REACT_206540. Amyloids.

    Miscellaneous databases

    EvolutionaryTracei Q06283.
    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. "Characterization of the cow stomach lysozyme genes: repetitive DNA and concerted evolution."
      Irwin D.M., White R.T., Wilson A.C.
      J. Mol. Evol. 37:355-366(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "X-ray crystallography and structural stability of digestive lysozyme from cow stomach."
      Nonaka Y., Akieda D., Aizawa T., Watanabe N., Kamiya M., Kumaki Y., Mizuguchi M., Kikukawa T., Demura M., Kawano K.
      FEBS J. 276:2192-2200(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 19-147, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLYSC2_BOVIN
    AccessioniPrimary (citable) accession number: Q06283
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: January 1, 1999
    Last modified: October 1, 2014
    This is version 95 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3