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Lysozyme C-2 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Lysozyme C type M)

 LYZ2_MOUSE              Reviewed;         148 AA.
P08905; Q3TXG2; Q3U5Q2; Q3U690; Q8VE78;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
07-NOV-2018, entry version 167.
RecName: Full=Lysozyme C-2;
EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C;
AltName: Full=Lysozyme C type M;
Flags: Precursor;
Name=Lyz2; Synonyms=Lyz, Lyzs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3413093; DOI=10.1073/pnas.85.17.6232;
Cross M., Mangelsdorf I., Wedel A., Renkawitz R.;
"Mouse lysozyme M gene: isolation, characterization, and expression
studies.";
Proc. Natl. Acad. Sci. U.S.A. 85:6232-6236(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Pancreatic islet;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 19-78.
Riblet R.J.;
"Sequence studies of mouse lysozyme.";
(In) Osserman E.F., Canfield R.E., Beychok S. (eds.);
Lysozyme, pp.89-93, Academic Press, New York (1974).
[5]
DISRUPTION PHENOTYPE.
PubMed=12411294; DOI=10.1182/blood-2002-07-2319;
Ganz T., Gabayan V., Liao H.-I., Liu L., Oren A., Graf T., Cole A.M.;
"Increased inflammation in lysozyme M-deficient mice in response to
Micrococcus luteus and its peptidoglycan.";
Blood 101:2388-2392(2003).
[6]
DISRUPTION PHENOTYPE.
PubMed=14617511; DOI=10.1164/rccm.200305-669OC;
Markart P., Korfhagen T.R., Weaver T.E., Akinbi H.T.;
"Mouse lysozyme M is important in pulmonary host defense against
Klebsiella pneumoniae infection.";
Am. J. Respir. Crit. Care Med. 169:454-458(2004).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14977423; DOI=10.1042/BJ20031810;
Markart P., Faust N., Graf T., Na C.-L., Weaver T.E., Akinbi H.T.;
"Comparison of the microbicidal and muramidase activities of mouse
lysozyme M and P.";
Biochem. J. 380:385-392(2004).
[8]
DISRUPTION PHENOTYPE.
PubMed=15265906; DOI=10.4049/jimmunol.173.3.1763;
Sinha P., Chi H.H., Kim H.R., Clausen B.E., Pederson B., Sercarz E.E.,
Forster I., Moudgil K.D.;
"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.";
J. Immunol. 173:1763-1771(2004).
[9]
DISRUPTION PHENOTYPE.
PubMed=16204648; DOI=10.1189/jlb.0205073;
Cole A.M., Thapa D.R., Gabayan V., Liao H.-I., Liu L., Ganz T.;
"Decreased clearance of Pseudomonas aeruginosa from airways of mice
deficient in lysozyme M.";
J. Leukoc. Biol. 78:1081-1085(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
STRUCTURE BY NMR OF 19-148, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND DISULFIDE BONDS.
PubMed=12613666; DOI=10.1007/s000180300012;
Obita T., Ueda T., Imoto T.;
"Solution structure and activity of mouse lysozyme M.";
Cell. Mol. Life Sci. 60:176-184(2003).
-!- 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. {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:14977423}.
-!- 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.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5. {ECO:0000269|PubMed:12613666};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12613666}.
-!- 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.
{ECO:0000269|PubMed:12411294, ECO:0000269|PubMed:14617511,
ECO:0000269|PubMed:14977423, ECO:0000269|PubMed:15265906,
ECO:0000269|PubMed:16204648}.
-!- 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
-!- SEQUENCE CAUTION:
Sequence=BAE30022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE31835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE34954.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M21050; AAA39473.1; -; Genomic_DNA.
EMBL; M21047; AAA39473.1; JOINED; Genomic_DNA.
EMBL; M21048; AAA39473.1; JOINED; Genomic_DNA.
EMBL; M21049; AAA39473.1; JOINED; Genomic_DNA.
EMBL; AK148516; BAE28595.1; -; mRNA.
EMBL; AK150998; BAE30022.1; ALT_INIT; mRNA.
EMBL; AK153244; BAE31835.1; ALT_INIT; mRNA.
EMBL; AK153475; BAE32025.1; -; mRNA.
EMBL; AK159276; BAE34954.1; ALT_INIT; mRNA.
EMBL; AK159640; BAE35253.1; -; mRNA.
EMBL; BC002069; AAH02069.1; -; mRNA.
EMBL; BC019611; AAH19611.1; -; mRNA.
EMBL; BC054463; AAH54463.1; -; mRNA.
CCDS; CCDS48694.1; -.
PIR; A31239; A31239.
RefSeq; NP_059068.1; NM_017372.3.
UniGene; Mm.45436; -.
PDB; 1IVM; NMR; -; A=19-148.
PDBsum; 1IVM; -.
ProteinModelPortal; P08905; -.
SMR; P08905; -.
IntAct; P08905; 4.
MINT; P08905; -.
STRING; 10090.ENSMUSP00000089801; -.
CAZy; GH22; Glycoside Hydrolase Family 22.
iPTMnet; P08905; -.
PhosphoSitePlus; P08905; -.
MaxQB; P08905; -.
PaxDb; P08905; -.
PeptideAtlas; P08905; -.
PRIDE; P08905; -.
Ensembl; ENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
GeneID; 17105; -.
KEGG; mmu:17105; -.
UCSC; uc007hda.1; mouse.
CTD; 17105; -.
MGI; MGI:96897; Lyz2.
eggNOG; ENOG410IXGD; Eukaryota.
eggNOG; ENOG4111QHM; LUCA.
GeneTree; ENSGT00550000074398; -.
HOGENOM; HOG000037357; -.
HOVERGEN; HBG052297; -.
InParanoid; P08905; -.
KO; K13915; -.
OMA; KWESNYN; -.
OrthoDB; EOG091G0R9V; -.
PhylomeDB; P08905; -.
TreeFam; TF324882; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6803157; Antimicrobial peptides.
EvolutionaryTrace; P08905; -.
PRO; PR:P08905; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000069516; Expressed in 244 organ(s), highest expression level in stroma of bone marrow.
CleanEx; MM_LYZ2; -.
ExpressionAtlas; P08905; baseline and differential.
Genevisible; P08905; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0000137; C:Golgi cis cisterna; ISO:MGI.
GO; GO:0005795; C:Golgi stack; ISO:MGI.
GO; GO:0005902; C:microvillus; ISO:MGI.
GO; GO:0048237; C:rough endoplasmic reticulum lumen; ISO:MGI.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000974; Glyco_hydro_22_lys.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR030056; Lysozyme_C.
PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
Pfam; PF00062; Lys; 1.
PRINTS; PR00137; LYSOZYME.
PRINTS; PR00135; LYZLACT.
SMART; SM00263; LYZ1; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
1: Evidence at protein level;
3D-structure; Antimicrobial; Bacteriolytic enzyme; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
Milk protein; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|Ref.4}.
CHAIN 19 148 Lysozyme C-2.
/FTId=PRO_0000018472.
ACT_SITE 53 53 {ECO:0000255|PROSITE-ProRule:PRU00680}.
ACT_SITE 71 71 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 24 146 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:12613666}.
DISULFID 48 134 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:12613666}.
DISULFID 83 99 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:12613666}.
DISULFID 95 113 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:12613666}.
HELIX 23 33 {ECO:0000244|PDB:1IVM}.
STRAND 39 41 {ECO:0000244|PDB:1IVM}.
HELIX 43 53 {ECO:0000244|PDB:1IVM}.
STRAND 56 58 {ECO:0000244|PDB:1IVM}.
STRAND 61 64 {ECO:0000244|PDB:1IVM}.
HELIX 65 67 {ECO:0000244|PDB:1IVM}.
STRAND 69 72 {ECO:0000244|PDB:1IVM}.
TURN 73 76 {ECO:0000244|PDB:1IVM}.
TURN 79 81 {ECO:0000244|PDB:1IVM}.
STRAND 82 84 {ECO:0000244|PDB:1IVM}.
HELIX 99 102 {ECO:0000244|PDB:1IVM}.
STRAND 103 105 {ECO:0000244|PDB:1IVM}.
HELIX 108 118 {ECO:0000244|PDB:1IVM}.
STRAND 120 122 {ECO:0000244|PDB:1IVM}.
HELIX 124 126 {ECO:0000244|PDB:1IVM}.
HELIX 128 131 {ECO:0000244|PDB:1IVM}.
TURN 132 136 {ECO:0000244|PDB:1IVM}.
HELIX 140 143 {ECO:0000244|PDB:1IVM}.
SEQUENCE 148 AA; 16689 MW; 5C768DDCD8071BAF CRC64;
MKTLLTLGLL LLSVTAQAKV YERCEFARTL KRNGMAGYYG VSLADWVCLA QHESNYNTRA
TNYNRGDQST DYGIFQINSR YWCNDGKTPR AVNACGINCS ALLQDDITAA IQCAKRVVRD
PQGIRAWVAW RAHCQNRDLS QYIRNCGV


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