LYSC_BOVIN
ID LYSC_BOVIN Reviewed; 147 AA.
AC P04421;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
GN Name=LYZ1;
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 [MRNA].
RX PubMed=2738070; DOI=10.1016/s0021-9258(18)60476-4;
RA Irwin D.M., Wilson A.C.;
RT "Multiple cDNA sequences and the evolution of bovine stomach lysozyme.";
RL J. Biol. Chem. 264:11387-11393(1989).
RN [2]
RP PROTEIN SEQUENCE OF 19-147 (2B).
RX PubMed=6470012; DOI=10.1016/s0021-9258(18)90908-7;
RA Jolles P., Schoentgen F., Jolles J., Dobson D.E., Prager E.M., Wilson A.C.;
RT "Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2
RT and immunological comparisons with other lysozymes.";
RL J. Biol. Chem. 259:11617-11625(1984).
RN [3]
RP SEQUENCE REVISION TO 116 (2B).
RX PubMed=2504928; DOI=10.1007/bf02602933;
RA Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.;
RT "Episodic evolution in the stomach lysozymes of ruminants.";
RL J. Mol. Evol. 28:528-535(1989).
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 -!- MISCELLANEOUS: Three non-allelic lysozymes C are present in the gastric
CC mucosa of cattle.
CC -!- MISCELLANEOUS: The sequence of isozyme 2B is shown.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; M26246; AAA30627.1; -; mRNA.
DR EMBL; M26245; AAA30626.1; -; mRNA.
DR EMBL; M26242; AAA30632.1; -; mRNA.
DR EMBL; M26241; AAA30628.1; -; mRNA.
DR EMBL; M26243; AAA30629.1; -; mRNA.
DR EMBL; M26244; AAA30630.1; -; mRNA.
DR EMBL; M26240; AAA30631.1; -; mRNA.
DR RefSeq; NP_001073808.1; NM_001080339.1.
DR RefSeq; NP_776529.1; NM_174104.2.
DR RefSeq; NP_851342.1; NM_180999.1.
DR AlphaFoldDB; P04421; -.
DR SMR; P04421; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GeneID; 280849; -.
DR GeneID; 281289; -.
DR GeneID; 781349; -.
DR KEGG; bta:280849; -.
DR KEGG; bta:281289; -.
DR KEGG; bta:781349; -.
DR CTD; 17105; -.
DR CTD; 281289; -.
DR InParanoid; P04421; -.
DR OrthoDB; 1551203at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:6470012"
FT CHAIN 19..147
FT /note="Lysozyme C"
FT /id="PRO_0000018453"
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"
FT VARIANT 3
FT /note="A -> T (in isozyme 2A)"
FT VARIANT 5
FT /note="V -> I (in isozyme 1 and isozyme 3)"
FT VARIANT 17
FT /note="Q -> K (in isozyme 2C)"
FT VARIANT 45
FT /note="N -> S (in isozyme 2D)"
FT VARIANT 66
FT /note="S -> G (in isozyme 1)"
FT VARIANT 106
FT /note="D -> E (in isozyme 1)"
FT VARIANT 116
FT /note="H -> Q (in isozyme 1)"
FT VARIANT 143
FT /note="E -> Q (in isozyme 3)"
SQ SEQUENCE 147 AA; 16373 MW; C678E7EECE1E66BF CRC64;
MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA
TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCR ELMENDIAKA VACAKHIVSE
QGITAWVAWK SHCRDHDVSS YVEGCTL
