Reviewed, UniProtKB/Swiss-Prot P08905 (LYZ2_MOUSE)

Names and origin

Protein names

Recommended name:
    Lysozyme C-2
    EC=3.2.1.17
Alternative name(s):
    Lysozyme C type M
    1,4-beta-N-acetylmuramidase C

Gene names

Name:	Lyz2
Synonyms:	Lyz, Lyzs

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
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.7 Ref.5 Ref.6 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.

Ontologies

Keywords
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase Milk protein
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to Gram-negative bacterium Ref.7 Inferred from direct assay. Source: UniProtKB defense response to Gram-positive bacterium Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	lysozyme activity Ref.5 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.4

Chain

19 – 148

130

Lysozyme C-2

PRO_0000018472

Sites

Active site

53

1

By similarity

Active site

71

1

By similarity

Amino acid modifications

Disulfide bond

24 ↔ 146

Ref.10

Disulfide bond

48 ↔ 134

Ref.10

Disulfide bond

83 ↔ 99

Ref.10

Disulfide bond

95 ↔ 113

Ref.10

Secondary structure

1

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148

Helix Strand Turn

Details...

Helix

23 – 33

11

Beta strand

39 – 41

3

Helix

43 – 53

11

Beta strand

56 – 58

3

Beta strand

61 – 64

4

Helix

65 – 67

3

Beta strand

69 – 72

4

Turn

73 – 76

4

Turn

79 – 81

3

Beta strand

82 – 84

3

Helix

99 – 102

4

Beta strand

103 – 105

3

Helix

108 – 118

11

Beta strand

120 – 122

3

Helix

124 – 126

3

Helix

128 – 131

4

Turn

132 – 136

5

Helix

140 – 143

4

Sequences

	Sequence		Length	Mass (Da)
	P08905-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: 5C768DDCD8071BAF	FASTA	148	16,689
	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

References

	« Hide 'large scale' referencesShow '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: 3413093] [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: 16141072] [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: 15489334] [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: 12411294] [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: 14617511] [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: 14977423] [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: 15265906] [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: 16204648] [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: 12613666] [Abstract] Cited for: STRUCTURE BY NMR OF 19-148, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00107952.

PIR

A31239.

RefSeq

NP_059068.1.

UniGene

Mm.45436

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IVM	NMR	-	A	19-148	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Genome annotation databases

Ensembl

ENSMUSG00000069516. Mus musculus. [Contig view]

GeneID

17105.

KEGG

mmu:17105.

Organism-specific databases

MGI

MGI:96897. Lyz2.

Phylogenomic databases

HOVERGEN

P08905.

Enzyme and pathway databases

BRENDA

3.2.1.17. 244.

Gene expression databases

ArrayExpress

P08905.

Bgee

P08905.

CleanEx

MM_LYZ2.

GermOnline

ENSMUSG00000069516. Mus musculus.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

291248.

SOURCE

Search...

Entry information

Entry name

LYZ2_MOUSE

Accession

Primary (citable) accession number: P08905
Secondary accession number(s): Q3TXG2 , Q3U5Q2, Q3U690, Q8VE78

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)