ID   LYSCK_SHEEP             Reviewed;         130 AA.
AC   P80190;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Lysozyme C, kidney isozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Kidney;
RX   PubMed=8477739; DOI=10.1111/j.1432-1033.1993.tb17805.x;
RA   Ito Y., Yamada H., Nakamura M., Yoshikawa A., Ueda T., Imoto T.;
RT   "The primary structures and properties of non-stomach lysozymes of sheep
RT   and cow, and implication for functional divergence of lysozyme.";
RL   Eur. J. Biochem. 213:649-658(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-63.
RX   PubMed=7563116; DOI=10.1007/bf01215177;
RA   Irwin D.M.;
RT   "Evolution of the bovine lysozyme gene family: changes in gene expression
RT   and reversion of function.";
RL   J. Mol. Evol. 41:299-312(1995).
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.
CC   -!- MISCELLANEOUS: The sequence shown here is a non-stomach isozyme.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; U19473; AAA85547.1; -; Genomic_DNA.
DR   PIR; S32465; S32465.
DR   AlphaFoldDB; P80190; -.
DR   SMR; P80190; -.
DR   STRING; 9940.ENSOARP00000022041; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Ensembl; ENSOART00020004715; ENSOARP00020003874; ENSOARG00020003071.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   BRENDA; 3.2.1.17; 2668.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..130
FT                   /note="Lysozyme C, kidney isozyme"
FT                   /id="PRO_0000208856"
FT   DOMAIN          1..130
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   130 AA;  14611 MW;  C79D70D3B8F70A8E CRC64;
     KVFERCELAR TLKRFGMDGF RGISLANWMC LARWESSYNT QATNYNSGDR STDYGIFQIN
     SHWWCNDGKT PGAVNACHIP CSALLQDDIT QAVACAKRVV SDPQGIRAWV AWRSHCQNQD
     LTSYIQGCGV