ID LYSC_BOVIN Reviewed; 147 AA. AC P04421; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 28-JUN-2023, entry version 142. 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=LYZ1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2738070; DOI=10.1016/s0021-9258(18)60476-4; RA Irwin D.M., Wilson A.C.; RT "Multiple cDNA sequences and the evolution of bovine stomach lysozyme."; RL J. Biol. Chem. 264:11387-11393(1989). RN [2] RP PROTEIN SEQUENCE OF 19-147 (2B). RX PubMed=6470012; DOI=10.1016/s0021-9258(18)90908-7; RA Jolles P., Schoentgen F., Jolles J., Dobson D.E., Prager E.M., Wilson A.C.; RT "Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 RT and immunological comparisons with other lysozymes."; RL J. Biol. Chem. 259:11617-11625(1984). RN [3] RP SEQUENCE REVISION TO 116 (2B). 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). 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 -!- TISSUE SPECIFICITY: Stomach-specific. 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 -!- MISCELLANEOUS: The ruminant gastric lysozymes, which digest symbiotic CC bacteria coming with cud from the rumen, are much more resistant to CC inactivation by pepsin than are other lysozymes. CC -!- MISCELLANEOUS: Three non-allelic lysozymes C are present in the gastric CC mucosa of cattle. CC -!- MISCELLANEOUS: The sequence of isozyme 2B is shown. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. CC {ECO:0000255|PROSITE-ProRule:PRU00680}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M26246; AAA30627.1; -; mRNA. DR EMBL; M26245; AAA30626.1; -; mRNA. DR EMBL; M26242; AAA30632.1; -; mRNA. DR EMBL; M26241; AAA30628.1; -; mRNA. DR EMBL; M26243; AAA30629.1; -; mRNA. DR EMBL; M26244; AAA30630.1; -; mRNA. DR EMBL; M26240; AAA30631.1; -; mRNA. DR RefSeq; NP_001073808.1; NM_001080339.1. DR RefSeq; NP_776529.1; NM_174104.2. DR RefSeq; NP_851342.1; NM_180999.1. DR AlphaFoldDB; P04421; -. DR SMR; P04421; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR GeneID; 280849; -. DR GeneID; 281289; -. DR GeneID; 781349; -. DR KEGG; bta:280849; -. DR KEGG; bta:281289; -. DR KEGG; bta:781349; -. DR CTD; 17105; -. DR CTD; 77397; -. DR InParanoid; P04421; -. DR OrthoDB; 5344399at2759; -. DR Proteomes; UP000009136; Unplaced. 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:0007586; P:digestion; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:6470012" FT CHAIN 19..147 FT /note="Lysozyme C" FT /id="PRO_0000018453" FT DOMAIN 19..147 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..145 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680" FT DISULFID 48..133 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" FT VARIANT 3 FT /note="A -> T (in isozyme 2A)" FT VARIANT 5 FT /note="V -> I (in isozyme 1 and isozyme 3)" FT VARIANT 17 FT /note="Q -> K (in isozyme 2C)" FT VARIANT 45 FT /note="N -> S (in isozyme 2D)" FT VARIANT 66 FT /note="S -> G (in isozyme 1)" FT VARIANT 106 FT /note="D -> E (in isozyme 1)" FT VARIANT 116 FT /note="H -> Q (in isozyme 1)" FT VARIANT 143 FT /note="E -> Q (in isozyme 3)" SQ SEQUENCE 147 AA; 16373 MW; C678E7EECE1E66BF CRC64; MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCR ELMENDIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCTL //