LYZ2_MOUSE
ID LYZ2_MOUSE Reviewed; 148 AA.
AC P08905; Q3TXG2; Q3U5Q2; Q3U690; Q8VE78;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Lysozyme C-2;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE AltName: Full=Lysozyme C type M;
DE Flags: Precursor;
GN Name=Lyz2; Synonyms=Lyz, Lyzs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3413093; DOI=10.1073/pnas.85.17.6232;
RA Cross M., Mangelsdorf I., Wedel A., Renkawitz R.;
RT "Mouse lysozyme M gene: isolation, characterization, and expression
RT studies.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6232-6236(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Pancreatic islet;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 19-78.
RA Riblet R.J.;
RT "Sequence studies of mouse lysozyme.";
RL (In) Osserman E.F., Canfield R.E., Beychok S. (eds.);
RL Lysozyme, pp.89-93, Academic Press, New York (1974).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12411294; DOI=10.1182/blood-2002-07-2319;
RA Ganz T., Gabayan V., Liao H.-I., Liu L., Oren A., Graf T., Cole A.M.;
RT "Increased inflammation in lysozyme M-deficient mice in response to
RT Micrococcus luteus and its peptidoglycan.";
RL Blood 101:2388-2392(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14617511; DOI=10.1164/rccm.200305-669oc;
RA Markart P., Korfhagen T.R., Weaver T.E., Akinbi H.T.;
RT "Mouse lysozyme M is important in pulmonary host defense against Klebsiella
RT pneumoniae infection.";
RL Am. J. Respir. Crit. Care Med. 169:454-458(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14977423; DOI=10.1042/bj20031810;
RA Markart P., Faust N., Graf T., Na C.-L., Weaver T.E., Akinbi H.T.;
RT "Comparison of the microbicidal and muramidase activities of mouse lysozyme
RT M and P.";
RL Biochem. J. 380:385-392(2004).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=15265906; DOI=10.4049/jimmunol.173.3.1763;
RA Sinha P., Chi H.H., Kim H.R., Clausen B.E., Pederson B., Sercarz E.E.,
RA Forster I., Moudgil K.D.;
RT "Mouse lysozyme-M knockout mice reveal how the self-determinant hierarchy
RT shapes the T cell repertoire against this circulating self antigen in wild-
RT type mice.";
RL J. Immunol. 173:1763-1771(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=16204648; DOI=10.1189/jlb.0205073;
RA Cole A.M., Thapa D.R., Gabayan V., Liao H.-I., Liu L., Ganz T.;
RT "Decreased clearance of Pseudomonas aeruginosa from airways of mice
RT deficient in lysozyme M.";
RL J. Leukoc. Biol. 78:1081-1085(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP STRUCTURE BY NMR OF 19-148, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=12613666; DOI=10.1007/s000180300012;
RA Obita T., Ueda T., Imoto T.;
RT "Solution structure and activity of mouse lysozyme M.";
RL Cell. Mol. Life Sci. 60:176-184(2003).
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents. Lyz2 is active against
CC a range of Gram-positive and Gram-negative bacteria. More effective
CC than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally
CC effective in killing Gram-positive bacteria. {ECO:0000255|PROSITE-
CC ProRule:PRU00680, ECO:0000269|PubMed:14977423}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:12613666};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12613666}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed weakly in myeloblasts, moderately in
CC immature macrophages, and strongly in both mature macrophages and
CC macrophage-rich tissues.
CC -!- DISRUPTION PHENOTYPE: Mice display increased inflammation in response
CC to M.luteus infection, impaired digestion of M.luteus cell walls,
CC decreased clearance of P.aeruginosa from infected airways, increased
CC susceptibility to K.pneumoniae infection and increased bacterial burden
CC and mortality following infection with various Gram-negative bacteria.
CC Lyz2 is non-immunogenic in wild-type mice but is rendered immunogenic
CC in mutants. {ECO:0000269|PubMed:12411294, ECO:0000269|PubMed:14617511,
CC ECO:0000269|PubMed:14977423, ECO:0000269|PubMed:15265906,
CC ECO:0000269|PubMed:16204648}.
CC -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC transglycosylation; it shows also a slight esterase activity. It acts
CC rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC and slowly on chitin oligosaccharides.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE30022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE34954.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M21050; AAA39473.1; -; Genomic_DNA.
DR EMBL; M21047; AAA39473.1; JOINED; Genomic_DNA.
DR EMBL; M21048; AAA39473.1; JOINED; Genomic_DNA.
DR EMBL; M21049; AAA39473.1; JOINED; Genomic_DNA.
DR EMBL; AK148516; BAE28595.1; -; mRNA.
DR EMBL; AK150998; BAE30022.1; ALT_INIT; mRNA.
DR EMBL; AK153244; BAE31835.1; ALT_INIT; mRNA.
DR EMBL; AK153475; BAE32025.1; -; mRNA.
DR EMBL; AK159276; BAE34954.1; ALT_INIT; mRNA.
DR EMBL; AK159640; BAE35253.1; -; mRNA.
DR EMBL; BC002069; AAH02069.1; -; mRNA.
DR EMBL; BC019611; AAH19611.1; -; mRNA.
DR EMBL; BC054463; AAH54463.1; -; mRNA.
DR CCDS; CCDS48694.1; -.
DR PIR; A31239; A31239.
DR RefSeq; NP_059068.1; NM_017372.3.
DR PDB; 1IVM; NMR; -; A=19-148.
DR PDBsum; 1IVM; -.
DR AlphaFoldDB; P08905; -.
DR SMR; P08905; -.
DR IntAct; P08905; 3.
DR STRING; 10090.ENSMUSP00000089801; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR iPTMnet; P08905; -.
DR PhosphoSitePlus; P08905; -.
DR jPOST; P08905; -.
DR MaxQB; P08905; -.
DR PaxDb; P08905; -.
DR PeptideAtlas; P08905; -.
DR PRIDE; P08905; -.
DR ProteomicsDB; 292156; -.
DR DNASU; 17105; -.
DR Ensembl; ENSMUST00000092163; ENSMUSP00000089801; ENSMUSG00000069516.
DR GeneID; 17105; -.
DR KEGG; mmu:17105; -.
DR UCSC; uc007hda.1; mouse.
DR CTD; 17105; -.
DR MGI; MGI:96897; Lyz2.
DR VEuPathDB; HostDB:ENSMUSG00000069516; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P08905; -.
DR OMA; WVAWKAH; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P08905; -.
DR TreeFam; TF324882; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 17105; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lyz2; mouse.
DR EvolutionaryTrace; P08905; -.
DR PRO; PR:P08905; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P08905; protein.
DR Bgee; ENSMUSG00000069516; Expressed in stroma of bone marrow and 224 other tissues.
DR ExpressionAtlas; P08905; baseline and differential.
DR Genevisible; P08905; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0000137; C:Golgi cis cisterna; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0048237; C:rough endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR030056; Lysozyme_C.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Milk protein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 19..148
FT /note="Lysozyme C-2"
FT /id="PRO_0000018472"
FT DOMAIN 19..148
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:12613666"
FT DISULFID 48..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:12613666"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:12613666"
FT DISULFID 95..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:12613666"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1IVM"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1IVM"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1IVM"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1IVM"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:1IVM"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1IVM"
SQ SEQUENCE 148 AA; 16689 MW; 5C768DDCD8071BAF CRC64;
MKTLLTLGLL LLSVTAQAKV YERCEFARTL KRNGMAGYYG VSLADWVCLA QHESNYNTRA
TNYNRGDQST DYGIFQINSR YWCNDGKTPR AVNACGINCS ALLQDDITAA IQCAKRVVRD
PQGIRAWVAW RAHCQNRDLS QYIRNCGV
