ID LYSC1_RAT Reviewed; 148 AA. AC P00697; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 2. DT 04-NOV-2026, entry version 160. DE RecName: Full=Lysozyme C-1; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; DE Flags: Precursor; GN Name=Lyz1; Synonyms=Lyz; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sprague-Dawley; RX PubMed=8081549; DOI=10.1006/mpev.1993.1007; RA Yeh T.C., Wilson A.C., Irwin D.M.; RT "Evolution of rodent lysozymes: isolation and sequence of the rat lysozyme RT genes."; RL Mol. Phylogenet. Evol. 2:65-75(1993). RN [2] RP PROTEIN SEQUENCE OF 19-148. RC STRAIN=Wistar; RX PubMed=851497; DOI=10.1021/bi00626a030; RA White T.J., Mross G.A., Osserman E.F., Wilson A.C.; RT "Primary structure of rat lysozyme."; RL Biochemistry 16:1430-1436(1977). 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. In the intestine they CC may also have a digestive function. 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 -!- TISSUE SPECIFICITY: Expressed in lung, small intestine and spleen. CC -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and CC transglycosylation; it also shows a slight esterase activity. It acts CC rapidly on both peptide-substituted and unsubstituted peptidoglycan, CC and slowly on chitin oligosaccharides. CC -!- MISCELLANEOUS: Rat has two lysozymes, type 1 and type 2 of which only CC type 1 is expressed; type 2 being probably a pseudogene. 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; L12459; AAA41551.1; -; Genomic_DNA. DR PIR; A40729; LZRT. DR AlphaFoldDB; P00697; -. DR SMR; P00697; -. DR FunCoup; P00697; 7. DR STRING; 10116.ENSRNOP00000007747; -. DR BindingDB; P00697; -. DR ChEMBL; CHEMBL2297; -. DR DrugCentral; P00697; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR iPTMnet; P00697; -. DR PhosphoSitePlus; P00697; -. DR PaxDb; 10116-ENSRNOP00000007747; -. DR UCSC; RGD:3026; rat. DR AGR; RGD:3026; -. DR RGD; 3026; Lyz. DR eggNOG; ENOG502S1S1; Eukaryota. DR InParanoid; P00697; -. DR OMA; AKTYTEC; -. DR PhylomeDB; P00697; -. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-6803157; Antimicrobial peptides. DR PRO; PR:P00697; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:RGD. DR GO; GO:0005576; C:extracellular region; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD. DR GO; GO:0000137; C:Golgi cis cisterna; IDA:RGD. DR GO; GO:0005795; C:Golgi stack; IDA:RGD. DR GO; GO:0005902; C:microvillus; IDA:RGD. DR GO; GO:0048237; C:rough endoplasmic reticulum lumen; IDA:RGD. DR GO; GO:0030141; C:secretory granule; IDA:RGD. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:RGD. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IMP:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0003796; F:lysozyme activity; IDA:RGD. DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:RGD. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:RGD. DR GO; GO:0009615; P:response to virus; ISO:RGD. DR CDD; cd16897; LYZ_C; 1. DR FunFam; 1.10.530.10:FF:000001; Lysozyme 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; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Milk protein; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:851497" FT CHAIN 19..148 FT /note="Lysozyme C-1" FT /id="PRO_0000018484" 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" FT CONFLICT 20 FT /note="I -> T (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 148 AA; 16729 MW; 8E6E986539BD3EEE CRC64; MKALLVLGFL LLSASVQAKI YERCQFARTL KRNGMSGYYG VSLADWVCLA QHESNYNTQA RNYNPGDQST DYGIFQINSR YWCNDGKTPR AKNACGIPCS ALLQDDITQA IQCAKRVVRD PQGIRAWVAW QRHCKNRDLS GYIRNCGV //