ID LYSC1_SHEEP Reviewed; 147 AA. AC P17607; Q9TUN2; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 03-MAY-2023, entry version 114. DE RecName: Full=Lysozyme C-1; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; DE Flags: Precursor; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10620405; DOI=10.1006/mpev.1999.0651; RA Wen Y., Irwin D.M.; RT "Mosaic evolution of ruminant stomach lysozyme genes."; RL Mol. Phylogenet. Evol. 13:474-482(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-147. RX PubMed=2318875; DOI=10.1016/s0021-9258(19)34066-9; RA Irwin D.M., Wilson A.C.; RT "Concerted evolution of ruminant stomach lysozymes. Characterization of RT lysozyme cDNA clones from sheep and deer."; RL J. Biol. Chem. 265:4944-4952(1990). 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 -!- TISSUE SPECIFICITY: Expressed in stomach. 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 sequence of isozyme 1A/1B/1C 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; AF170555; AAD51636.1; -; Genomic_DNA. DR EMBL; AF170552; AAD51636.1; JOINED; Genomic_DNA. DR EMBL; AF170553; AAD51636.1; JOINED; Genomic_DNA. DR EMBL; AF170554; AAD51636.1; JOINED; Genomic_DNA. DR EMBL; M32492; AAA31557.1; -; mRNA. DR EMBL; M32493; AAA31558.1; -; mRNA. DR EMBL; M32494; AAA31559.1; -; mRNA. DR EMBL; M32495; AAA31560.1; -; mRNA. DR EMBL; M32496; AAA31561.1; -; mRNA. DR EMBL; M32497; AAA31562.1; -; mRNA. DR EMBL; M32498; AAA31563.1; -; mRNA. DR PIR; D35558; D35558. DR PIR; E35558; E35558. DR PIR; F35558; F35558. DR RefSeq; NP_001295517.1; NM_001308588.1. DR AlphaFoldDB; P17607; -. DR SMR; P17607; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR Ensembl; ENSOART00020004615; ENSOARP00020003799; ENSOARG00020002988. DR GeneID; 443320; -. DR KEGG; oas:443320; -. DR OrthoDB; 5344399at2759; -. 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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. 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 2: Evidence at transcript level; KW Antimicrobial; Bacteriolytic enzyme; Digestion; Disulfide bond; KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000250" FT CHAIN 19..147 FT /note="Lysozyme C-1" FT /id="PRO_0000018488" 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 32 FT /note="E -> K (in isozyme 3A and isozyme 4A/4B)" FT VARIANT 37 FT /note="G -> D (in isozyme 4A/4B)" FT VARIANT 55 FT /note="S -> G (in isozyme 3A)" FT VARIANT 101 FT /note="E -> A (in isozyme 2A, isozyme 3A and isozyme FT 4A/4B)" FT VARIANT 106 FT /note="N -> D (in isozyme 2A, isozyme 3A and isozyme FT 4A/4B)" FT VARIANT 108 FT /note="A -> E (in isozyme 2A, isozyme 3A and isozyme FT 4A/4B)" FT VARIANT 146 FT /note="S -> T (in isozyme 2A, isozyme 3A and isozyme FT 4A/4B)" SQ SEQUENCE 147 AA; 16195 MW; 065D72BC42B0A6E0 CRC64; MKALIILGLL CLSVAVQGKV FERCELARTL KELGLDGYKG VSLANWLCLT KWESSYNTKA TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENNIAKA VACAKHIVSE QGITAWVAWK SHCRDHDVSS YVEGCSL //