ID   LYSC_MACMU              Reviewed;         148 AA.
AC   P30201;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYZ;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=1960739; DOI=10.1007/bf02103133;
RA   Swanson K.W., Irwin D.M., Wilson A.C.;
RT   "Stomach lysozyme gene of the langur monkey: tests for convergence and
RT   positive selection.";
RL   J. Mol. Evol. 33:418-425(1991).
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.
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 {ECO:0000250}.
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; X60236; CAA42796.1; -; mRNA.
DR   RefSeq; NP_001095203.1; NM_001101733.1.
DR   AlphaFoldDB; P30201; -.
DR   SMR; P30201; -.
DR   STRING; 9544.ENSMMUP00000047515; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 9544-ENSMMUP00000011770; -.
DR   Ensembl; ENSMMUT00000056068.2; ENSMMUP00000047515.1; ENSMMUG00000008987.4.
DR   GeneID; 718361; -.
DR   KEGG; mcc:718361; -.
DR   CTD; 4069; -.
DR   VEuPathDB; HostDB:ENSMMUG00000008987; -.
DR   VGNC; VGNC:74466; LYZ.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000153832; -.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; P30201; -.
DR   OMA; NACNIKC; -.
DR   OrthoDB; 5344399at2759; -.
DR   TreeFam; TF324882; -.
DR   Proteomes; UP000006718; Chromosome 11.
DR   Bgee; ENSMMUG00000008987; Expressed in olfactory segment of nasal mucosa and 23 other cell types or tissues.
DR   ExpressionAtlas; P30201; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF28; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Milk protein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..148
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000018470"
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;  16408 MW;  AF4EE1B3A33F4765 CRC64;
     MKAVIILGLV LLSVTVQGKI FERCELARTL KRLGLDGYRG ISLANWVCLA KWESNYNTQA
     TNYNPGDQST DYGIFQINSH YWCNNGKTPG AVNACHISCN ALLQDNIADA VTCAKRVVSD
     PQGIRAWVAW RNHCQNRDVS QYVQGCGV
//