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P08905

- LYZ2_MOUSE

UniProt

P08905 - LYZ2_MOUSE

Protein

Lysozyme C-2

Gene

Lyz2

Organism
Mus musculus (Mouse)
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. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.1 PublicationPROSITE-ProRule annotation

    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.

    pH dependencei

    Optimum pH is 5.1 Publication

    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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase, Milk protein

    Enzyme and pathway databases

    ReactomeiREACT_198563. 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
    Lysozyme C type M
    Gene namesi
    Name:Lyz2
    Synonyms:Lyz, Lyzs
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:96897. Lyz2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mice display increased inflammation in response to M.luteus infection, impaired digestion of M.luteus cell walls, decreased clearance of P.aeruginosa from infected airways, increased susceptibility to K.pneumoniae infection and increased bacterial burden and mortality following infection with various Gram-negative bacteria. Lyz2 is non-immunogenic in wild-type mice but is rendered immunogenic in mutants.5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 148130Lysozyme C-2PRO_0000018472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 1461 PublicationPROSITE-ProRule annotation
    Disulfide bondi48 ↔ 1341 PublicationPROSITE-ProRule annotation
    Disulfide bondi83 ↔ 991 PublicationPROSITE-ProRule annotation
    Disulfide bondi95 ↔ 1131 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP08905.
    PaxDbiP08905.
    PRIDEiP08905.

    Expressioni

    Tissue specificityi

    Expressed weakly in myeloblasts, moderately in immature macrophages, and strongly in both mature macrophages and macrophage-rich tissues.

    Gene expression databases

    BgeeiP08905.
    CleanExiMM_LYZ2.
    GenevestigatoriP08905.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP08905. 4 interactions.
    MINTiMINT-4100851.

    Structurei

    Secondary structure

    1
    148
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3311
    Beta strandi39 – 413
    Helixi43 – 5311
    Beta strandi56 – 583
    Beta strandi61 – 644
    Helixi65 – 673
    Beta strandi69 – 724
    Turni73 – 764
    Turni79 – 813
    Beta strandi82 – 843
    Helixi99 – 1024
    Beta strandi103 – 1053
    Helixi108 – 11811
    Beta strandi120 – 1223
    Helixi124 – 1263
    Helixi128 – 1314
    Turni132 – 1365
    Helixi140 – 1434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IVMNMR-A19-148[»]
    ProteinModelPortaliP08905.
    SMRiP08905. Positions 19-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08905.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85133.
    GeneTreeiENSGT00550000074398.
    HOGENOMiHOG000037357.
    HOVERGENiHBG052297.
    InParanoidiP08905.
    KOiK13915.
    OMAiCLASWER.
    OrthoDBiEOG7BW0M5.
    PhylomeDBiP08905.
    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.

    P08905-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTLLTLGLL LLSVTAQAKV YERCEFARTL KRNGMAGYYG VSLADWVCLA    50
    QHESNYNTRA TNYNRGDQST DYGIFQINSR YWCNDGKTPR AVNACGINCS 100
    ALLQDDITAA IQCAKRVVRD PQGIRAWVAW RAHCQNRDLS QYIRNCGV 148
    Length:148
    Mass (Da):16,689
    Last modified:November 1, 1990 - v2
    Checksum:i5C768DDCD8071BAF
    GO

    Sequence cautioni

    The sequence BAE30022.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE31835.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE34954.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21050
    , M21047, M21048, M21049 Genomic DNA. Translation: AAA39473.1.
    AK148516 mRNA. Translation: BAE28595.1.
    AK150998 mRNA. Translation: BAE30022.1. Different initiation.
    AK153244 mRNA. Translation: BAE31835.1. Different initiation.
    AK153475 mRNA. Translation: BAE32025.1.
    AK159276 mRNA. Translation: BAE34954.1. Different initiation.
    AK159640 mRNA. Translation: BAE35253.1.
    BC002069 mRNA. Translation: AAH02069.1.
    BC019611 mRNA. Translation: AAH19611.1.
    BC054463 mRNA. Translation: AAH54463.1.
    CCDSiCCDS48694.1.
    PIRiA31239.
    RefSeqiNP_059068.1. NM_017372.3.
    UniGeneiMm.45436.

    Genome annotation databases

    EnsembliENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
    GeneIDi17105.
    KEGGimmu:17105.
    UCSCiuc007hda.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21050
    , M21047 , M21048 , M21049 Genomic DNA. Translation: AAA39473.1 .
    AK148516 mRNA. Translation: BAE28595.1 .
    AK150998 mRNA. Translation: BAE30022.1 . Different initiation.
    AK153244 mRNA. Translation: BAE31835.1 . Different initiation.
    AK153475 mRNA. Translation: BAE32025.1 .
    AK159276 mRNA. Translation: BAE34954.1 . Different initiation.
    AK159640 mRNA. Translation: BAE35253.1 .
    BC002069 mRNA. Translation: AAH02069.1 .
    BC019611 mRNA. Translation: AAH19611.1 .
    BC054463 mRNA. Translation: AAH54463.1 .
    CCDSi CCDS48694.1.
    PIRi A31239.
    RefSeqi NP_059068.1. NM_017372.3.
    UniGenei Mm.45436.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IVM NMR - A 19-148 [» ]
    ProteinModelPortali P08905.
    SMRi P08905. Positions 19-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08905. 4 interactions.
    MINTi MINT-4100851.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    MaxQBi P08905.
    PaxDbi P08905.
    PRIDEi P08905.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092163 ; ENSMUSP00000089801 ; ENSMUSG00000069516 .
    GeneIDi 17105.
    KEGGi mmu:17105.
    UCSCi uc007hda.1. mouse.

    Organism-specific databases

    CTDi 17105.
    MGIi MGI:96897. Lyz2.

    Phylogenomic databases

    eggNOGi NOG85133.
    GeneTreei ENSGT00550000074398.
    HOGENOMi HOG000037357.
    HOVERGENi HBG052297.
    InParanoidi P08905.
    KOi K13915.
    OMAi CLASWER.
    OrthoDBi EOG7BW0M5.
    PhylomeDBi P08905.
    TreeFami TF324882.

    Enzyme and pathway databases

    Reactomei REACT_198563. Amyloids.

    Miscellaneous databases

    EvolutionaryTracei P08905.
    NextBioi 291248.
    PROi P08905.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08905.
    CleanExi MM_LYZ2.
    Genevestigatori P08905.

    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. "Mouse lysozyme M gene: isolation, characterization, and expression studies."
      Cross M., Mangelsdorf I., Wedel A., Renkawitz R.
      Proc. Natl. Acad. Sci. U.S.A. 85:6232-6236(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage and Pancreatic islet.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N and FVB/N-3.
      Tissue: Mammary tumor.
    4. "Sequence studies of mouse lysozyme."
      Riblet R.J.
      (In) Osserman E.F., Canfield R.E., Beychok S. (eds.); Lysozyme, pp.89-93, Academic Press, New York (1974)
      Cited for: PROTEIN SEQUENCE OF 19-78.
    5. "Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan."
      Ganz T., Gabayan V., Liao H.-I., Liu L., Oren A., Graf T., Cole A.M.
      Blood 101:2388-2392(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    6. "Mouse lysozyme M is important in pulmonary host defense against Klebsiella pneumoniae infection."
      Markart P., Korfhagen T.R., Weaver T.E., Akinbi H.T.
      Am. J. Respir. Crit. Care Med. 169:454-458(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Comparison of the microbicidal and muramidase activities of mouse lysozyme M and P."
      Markart P., Faust N., Graf T., Na C.-L., Weaver T.E., Akinbi H.T.
      Biochem. J. 380:385-392(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Mouse lysozyme-M knockout mice reveal how the self-determinant hierarchy shapes the T cell repertoire against this circulating self antigen in wild-type mice."
      Sinha P., Chi H.H., Kim H.R., Clausen B.E., Pederson B., Sercarz E.E., Forster I., Moudgil K.D.
      J. Immunol. 173:1763-1771(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    9. "Decreased clearance of Pseudomonas aeruginosa from airways of mice deficient in lysozyme M."
      Cole A.M., Thapa D.R., Gabayan V., Liao H.-I., Liu L., Ganz T.
      J. Leukoc. Biol. 78:1081-1085(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Solution structure and activity of mouse lysozyme M."
      Obita T., Ueda T., Imoto T.
      Cell. Mol. Life Sci. 60:176-184(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 19-148, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLYZ2_MOUSE
    AccessioniPrimary (citable) accession number: P08905
    Secondary accession number(s): Q3TXG2
    , Q3U5Q2, Q3U690, Q8VE78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 136 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3