LYZ1_MOUSE
ID LYZ1_MOUSE Reviewed; 148 AA.
AC P17897;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Lysozyme C-1;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE AltName: Full=Lysozyme C type P;
DE Flags: Precursor;
GN Name=Lyz1; Synonyms=Lzp-s;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=2336377; DOI=10.1093/nar/18.7.1911;
RA Cortopassi G.A., Wilson A.C.;
RT "Recent origin of the P lysozyme gene in mice.";
RL Nucleic Acids Res. 18:1911-1911(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
RX PubMed=2323338; DOI=10.1002/j.1460-2075.1990.tb08237.x;
RA Cross M., Renkawitz R.;
RT "Repetitive sequence involvement in the duplication and divergence of mouse
RT lysozyme genes.";
RL EMBO J. 9:1283-1288(1990).
RN [4]
RP PROTEIN SEQUENCE OF 69-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP FUNCTION.
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).
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. Lyz1 is active against
CC a range of Gram-positive and Gram-negative bacteria. Less effective
CC than Lyz2 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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed strongly only in small intestine.
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}.
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DR EMBL; X51547; CAA35922.1; -; mRNA.
DR EMBL; BC061129; AAH61129.1; -; mRNA.
DR CCDS; CCDS48695.1; -.
DR PIR; S09229; S09229.
DR RefSeq; NP_038618.1; NM_013590.4.
DR AlphaFoldDB; P17897; -.
DR SMR; P17897; -.
DR BioGRID; 201260; 9.
DR IntAct; P17897; 1.
DR MINT; P17897; -.
DR STRING; 10090.ENSMUSP00000089800; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PhosphoSitePlus; P17897; -.
DR jPOST; P17897; -.
DR MaxQB; P17897; -.
DR PaxDb; P17897; -.
DR PeptideAtlas; P17897; -.
DR PRIDE; P17897; -.
DR ProteomicsDB; 292134; -.
DR DNASU; 17110; -.
DR Ensembl; ENSMUST00000092162; ENSMUSP00000089800; ENSMUSG00000069515.
DR GeneID; 17110; -.
DR KEGG; mmu:17110; -.
DR UCSC; uc007hdc.2; mouse.
DR CTD; 17110; -.
DR MGI; MGI:96902; Lyz1.
DR VEuPathDB; HostDB:ENSMUSG00000069515; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P17897; -.
DR OMA; QCKLART; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P17897; -.
DR TreeFam; TF324882; -.
DR BioGRID-ORCS; 17110; 0 hits in 74 CRISPR screens.
DR PRO; PR:P17897; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P17897; protein.
DR Bgee; ENSMUSG00000069515; Expressed in ileum and 38 other tissues.
DR ExpressionAtlas; P17897; baseline and differential.
DR Genevisible; P17897; 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; ISO:MGI.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
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 Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..148
FT /note="Lysozyme C-1"
FT /id="PRO_0000018473"
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 DISULFID 48..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 95..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 148 AA; 16794 MW; D849A9D02A49EDE6 CRC64;
MKALLTLGLL LLSVTAQAKV YNRCELARIL KRNGMDGYRG VKLADWVCLA QHESNYNTRA
TNYNRGDRST DYGIFQINSR YWCNDGKTPR SKNACGINCS ALLQDDITAA IQCAKRVVRD
PQGIRAWVAW RTQCQNRDLS QYIRNCGV
