ID   LYSC2_CANLF             Reviewed;         130 AA.
AC   P81709;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Lysozyme C, spleen isozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Spleen;
RX   PubMed=8080284; DOI=10.1006/abbi.1994.1399;
RA   Grobler J.A., Rao K.R., Pervaiz S., Brew K.;
RT   "Sequences of two highly divergent canine type c lysozymes: implications
RT   for the evolutionary origins of the lysozyme/alpha-lactalbumin
RT   superfamily.";
RL   Arch. Biochem. Biophys. 313:360-366(1994).
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. {ECO:0000255|PROSITE-
CC       ProRule:PRU00680}.
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. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   PIR; S48642; S48642.
DR   AlphaFoldDB; P81709; -.
DR   SMR; P81709; -.
DR   STRING; 9615.ENSCAFP00000049287; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; 9612-ENSCAFP00000000619; -.
DR   Ensembl; ENSCAFT00000000675.5; ENSCAFP00000000619.4; ENSCAFG00000000426.5.
DR   Ensembl; ENSCAFT00030013696.1; ENSCAFP00030011952.1; ENSCAFG00030007455.1.
DR   Ensembl; ENSCAFT00040013862.1; ENSCAFP00040012005.1; ENSCAFG00040007445.1.
DR   Ensembl; ENSCAFT00845030510.1; ENSCAFP00845023932.1; ENSCAFG00845017223.1.
DR   VEuPathDB; HostDB:ENSCAFG00845017223; -.
DR   VGNC; VGNC:42901; LYZ.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000153832; -.
DR   InParanoid; P81709; -.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Reactome; R-CFA-6803157; Antimicrobial peptides.
DR   Proteomes; UP000002254; Chromosome 10.
DR   Proteomes; UP000694429; Chromosome 10.
DR   Proteomes; UP000694542; Chromosome 10.
DR   Proteomes; UP000805418; Chromosome 10.
DR   Bgee; ENSCAFG00000000426; Expressed in blood and 49 other cell types or tissues.
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: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; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..130
FT                   /note="Lysozyme C, spleen isozyme"
FT                   /id="PRO_0000208846"
FT   DOMAIN          1..130
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   130 AA;  14578 MW;  96C9BA30478D60F6 CRC64;
     KIFERCELAR TLKNLGLAGY KGVSLANWVC LAKWESNYNT RATNYNPGSK STDYGIFQIN
     SRYWCNDGKT PRAVNACHIS CSALLQDDIT QAVACAKRVV SDPNGIRAWV AWRAHCENRD
     VSQYVRNCGV
//