P08905 (LYZ2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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
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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase Milk protein
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 Inferred from direct assay Ref.7. Source: UniProtKB defense response to Gram-positive bacterium Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lysozyme activity Inferred from direct assay Ref.5. 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 [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] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_017372.3.

UniGene

Mm.45436.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P08905.

SMR

P08905. Positions 19-148.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08905. 3 interactions.

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PaxDb

P08905.

PRIDE

P08905.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.

GeneID

17105.

KEGG

mmu:17105.

UCSC

uc007hdc.2. mouse.

Organism-specific databases

CTD

17105.

MGI

MGI:96897. Lyz2.

Phylogenomic databases

eggNOG

NOG85133.

GeneTree

ENSGT00550000074398.

HOGENOM

HOG000037357.

HOVERGEN

HBG052297.

InParanoid

P08905.

KO

K13915.

OMA

CNALLQD.

OrthoDB

EOG48KRCP.

Gene expression databases

Bgee

P08905.

CleanEx

MM_LYZ2.

Genevestigator

P08905.

GermOnline

ENSMUSG00000069516. Mus musculus.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P08905.

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:	April 3, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program