ID   LYSC1_PIG               Reviewed;         128 AA.
AC   P12067;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Lysozyme C-1;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Stomach;
RX   PubMed=2504928; DOI=10.1007/bf02602933;
RA   Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.;
RT   "Episodic evolution in the stomach lysozymes of ruminants.";
RL   J. Mol. Evol. 28:528-535(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-128.
RC   TISSUE=Spleen;
RA   Echetebu Z.O., Nevils M., Roberts R.M., Trout W.E.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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: 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; L14853; AAA74656.1; -; mRNA.
DR   AlphaFoldDB; P12067; -.
DR   SMR; P12067; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PeptideAtlas; P12067; -.
DR   PRIDE; P12067; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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:0007586; P:digestion; 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; Digestion; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted.
FT   CHAIN           1..128
FT                   /note="Lysozyme C-1"
FT                   /id="PRO_0000208853"
FT   DOMAIN          1..128
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        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        63..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        75..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   128 AA;  14668 MW;  FD169D39228DF774 CRC64;
     KVYDRCEFAR ILKKSGMDGY RGVSLANWVC LAKWESDFNT KAINRNVGST DYGIFQINSR
     YWCNDGKTPK AVNACHISCK VLLDDDLSQD IECAKRVVRD PQGIKAWVAW RTHCQNKDVS
     QYIRGCKL