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P08905 (LYZ2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C-2

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Lysozyme C type M
Gene names
Name:Lyz2
Synonyms:Lyz, Lyzs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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.

Subunit structure

Monomer. Ref.10

Subcellular location

Secreted.

Tissue specificity

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

Disruption phenotype

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5. Ref.10

Sequence caution

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.4
Chain19 – 148130Lysozyme C-2
PRO_0000018472

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond24 ↔ 146 Ref.10
Disulfide bond48 ↔ 134 Ref.10
Disulfide bond83 ↔ 99 Ref.10
Disulfide bond95 ↔ 113 Ref.10

Secondary structure

................................ 148
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08905 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 5C768DDCD8071BAF

FASTA14816,689
        10         20         30         40         50         60 
MKTLLTLGLL LLSVTAQAKV YERCEFARTL KRNGMAGYYG VSLADWVCLA QHESNYNTRA 

        70         80         90        100        110        120 
TNYNRGDQST DYGIFQINSR YWCNDGKTPR AVNACGINCS ALLQDDITAA IQCAKRVVRD 

       130        140 
PQGIRAWVAW RAHCQNRDLS QYIRNCGV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21050 expand/collapse EMBL AC list , 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.
CCDSCCDS48694.1.
PIRA31239.
RefSeqNP_059068.1. NM_017372.3.
UniGeneMm.45436.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVMNMR-A19-148[»]
ProteinModelPortalP08905.
SMRP08905. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08905. 4 interactions.
MINTMINT-4100851.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

MaxQBP08905.
PaxDbP08905.
PRIDEP08905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
GeneID17105.
KEGGmmu:17105.
UCSCuc007hda.1. mouse.

Organism-specific databases

CTD17105.
MGIMGI:96897. Lyz2.

Phylogenomic databases

eggNOGNOG85133.
GeneTreeENSGT00550000074398.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP08905.
KOK13915.
OMACLASWER.
OrthoDBEOG7BW0M5.
PhylomeDBP08905.
TreeFamTF324882.

Gene expression databases

BgeeP08905.
CleanExMM_LYZ2.
GenevestigatorP08905.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08905.
NextBio291248.
PROP08905.
SOURCESearch...

Entry information

Entry nameLYZ2_MOUSE
AccessionPrimary (citable) accession number: P08905
Secondary accession number(s): Q3TXG2 expand/collapse secondary AC list , Q3U5Q2, Q3U690, Q8VE78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries