ID   LYSC2_RAT               Reviewed;         148 AA.
AC   Q05820;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Putative lysozyme C-2;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=Lyz2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=94362956; 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
RT   lysozyme genes.";
RL   Mol. Phylogenet. Evol. 2:65-75(1993).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC       in tissues and body fluids are associated with the monocyte-
CC       macrophage system and enhance the activity of immunoagents. In the
CC       intestine they may also have a digestive function.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It
CC       acts rapidly on both peptide-substituted and unsubstituted
CC       peptidoglycan, and slowly on chitin oligosaccharides.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC   -!- CAUTION: Could be the product of a pseudogene. Lyz1 has been shown
CC       to be expressed, but not Lyz2.
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DR   EMBL; L12458; AAA41552.1; -; Genomic_DNA.
DR   IPI; IPI00193370; -.
DR   PIR; B40729; B40729.
DR   UniGene; Rn.162941; -.
DR   HSSP; P08905; 1IVM.
DR   SMR; Q05820; 19-148.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PRIDE; Q05820; -.
DR   HOVERGEN; Q05820; -.
DR   BRENDA; 3.2.1.17; 248.
DR   GO; GO:0000137; C:Golgi cis cisterna; 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:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:RGD.
DR   GO; GO:0003796; F:lysozyme activity; IDA:RGD.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   5: Uncertain;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Signal.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    148       Putative lysozyme C-2.
FT                                /FTId=PRO_0000018485.
FT   ACT_SITE     53     53       By similarity.
FT   ACT_SITE     71     71       By similarity.
FT   DISULFID     24    146       By similarity.
FT   DISULFID     48    134       By similarity.
FT   DISULFID     83     99       By similarity.
FT   DISULFID     95    113       By similarity.
SQ   SEQUENCE   148 AA;  16618 MW;  2855279E91CCC083 CRC64;
     MKALLVLGFL LLSASVQAKV FKHCELARIL RSSALAGYRG VSLENWMCMA QHESNFDTEA
     INYNSTDQST DYGIFQINSR YWCNDGKTPR AVNACGIPCS ALLQDDITQA IQCAKRVVRD
     PQGIRAWVAW QRHCQNRDLS GYIRNCGV
//