LYSC1_RAT
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 03-AUG-2022, entry version 147.
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 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: 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}.
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DR EMBL; L12459; AAA41551.1; -; Genomic_DNA.
DR PIR; A40729; LZRT.
DR AlphaFoldDB; P00697; -.
DR SMR; P00697; -.
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; P00697; -.
DR PRIDE; P00697; -.
DR UCSC; RGD:3026; rat.
DR RGD; 3026; Lyz.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR InParanoid; P00697; -.
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:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; 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:0019835; P:cytolysis; IEA:UniProtKB-KW.
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:0031640; P:killing of cells of another organism; ISO:RGD.
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; 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
