LYSC3_BOVIN
ID LYSC3_BOVIN Reviewed; 147 AA.
AC Q06284;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Lysozyme C-3;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
GN Name=LYZ3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8308905; DOI=10.1007/bf00178866;
RA Irwin D.M., White R.T., Wilson A.C.;
RT "Characterization of the cow stomach lysozyme genes: repetitive DNA and
RT concerted evolution.";
RL J. Mol. Evol. 37:355-366(1993).
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 -!- TISSUE SPECIFICITY: Stomach-specific.
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 ruminant gastric lysozymes, which digest symbiotic
CC bacteria coming with cud from the rumen, are much more resistant to
CC inactivation by pepsin than are other lysozymes.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; M95099; AAC37312.1; -; Unassigned_DNA.
DR PIR; F34277; F34277.
DR RefSeq; NP_776529.1; NM_174104.2.
DR AlphaFoldDB; Q06284; -.
DR SMR; Q06284; -.
DR STRING; 9913.ENSBTAP00000027399; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; Q06284; -.
DR Ensembl; ENSBTAT00000027399; ENSBTAP00000027399; ENSBTAG00000046628.
DR GeneID; 281289; -.
DR KEGG; bta:281289; -.
DR CTD; 281289; -.
DR VEuPathDB; HostDB:ENSBTAG00000046628; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; Q06284; -.
DR OMA; AWKSHCQ; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000046628; Expressed in urinary bladder and 46 other tissues.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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:0007586; P:digestion; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Digestion; Disulfide bond;
KW Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..147
FT /note="Lysozyme C-3"
FT /id="PRO_0000018456"
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"
SQ SEQUENCE 147 AA; 16317 MW; 09CF5B9EC5B2B871 CRC64;
MKALIILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA
TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENDIAKA VACAKHIVSE
QGITAWVAWK SHCRDHDVSS YVQGCTL
