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P08905

- LYZ2_MOUSE

UniProt

P08905 - LYZ2_MOUSE

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Protein
Lysozyme C-2
Gene
Lyz2, Lyz, Lyzs
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication

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 – 531 By similarity
Active sitei71 – 711 By similarity

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 Gram-negative bacterium Source: UniProtKB
  4. defense response to Gram-positive bacterium Source: UniProtKB
  5. defense response to bacterium Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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 Publication
Add
BLAST
Chaini19 – 148130Lysozyme C-2
PRO_0000018472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1461 Publication
Disulfide bondi48 ↔ 1341 Publication
Disulfide bondi83 ↔ 991 Publication
Disulfide bondi95 ↔ 1131 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP08905.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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

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