LYSC1_SHEEP
ID LYSC1_SHEEP Reviewed; 147 AA.
AC P17607; Q9TUN2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Lysozyme C-1;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10620405; DOI=10.1006/mpev.1999.0651;
RA Wen Y., Irwin D.M.;
RT "Mosaic evolution of ruminant stomach lysozyme genes.";
RL Mol. Phylogenet. Evol. 13:474-482(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-147.
RX PubMed=2318875; DOI=10.1016/s0021-9258(19)34066-9;
RA Irwin D.M., Wilson A.C.;
RT "Concerted evolution of ruminant stomach lysozymes. Characterization of
RT lysozyme cDNA clones from sheep and deer.";
RL J. Biol. Chem. 265:4944-4952(1990).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in stomach.
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 sequence of isozyme 1A/1B/1C is shown.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AF170555; AAD51636.1; -; Genomic_DNA.
DR EMBL; AF170552; AAD51636.1; JOINED; Genomic_DNA.
DR EMBL; AF170553; AAD51636.1; JOINED; Genomic_DNA.
DR EMBL; AF170554; AAD51636.1; JOINED; Genomic_DNA.
DR EMBL; M32492; AAA31557.1; -; mRNA.
DR EMBL; M32493; AAA31558.1; -; mRNA.
DR EMBL; M32494; AAA31559.1; -; mRNA.
DR EMBL; M32495; AAA31560.1; -; mRNA.
DR EMBL; M32496; AAA31561.1; -; mRNA.
DR EMBL; M32497; AAA31562.1; -; mRNA.
DR EMBL; M32498; AAA31563.1; -; mRNA.
DR PIR; D35558; D35558.
DR PIR; E35558; E35558.
DR PIR; F35558; F35558.
DR RefSeq; NP_001295517.1; NM_001308588.1.
DR AlphaFoldDB; P17607; -.
DR SMR; P17607; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR Ensembl; ENSOART00020004615; ENSOARP00020003799; ENSOARG00020002988.
DR GeneID; 443320; -.
DR KEGG; oas:443320; -.
DR OrthoDB; 1551203at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..147
FT /note="Lysozyme C-1"
FT /id="PRO_0000018488"
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 32
FT /note="E -> K (in isozyme 3A and isozyme 4A/4B)"
FT VARIANT 37
FT /note="G -> D (in isozyme 4A/4B)"
FT VARIANT 55
FT /note="S -> G (in isozyme 3A)"
FT VARIANT 101
FT /note="E -> A (in isozyme 2A, isozyme 3A and isozyme 4A/
FT 4B)"
FT VARIANT 106
FT /note="N -> D (in isozyme 2A, isozyme 3A and isozyme 4A/
FT 4B)"
FT VARIANT 108
FT /note="A -> E (in isozyme 2A, isozyme 3A and isozyme 4A/
FT 4B)"
FT VARIANT 146
FT /note="S -> T (in isozyme 2A, isozyme 3A and isozyme 4A/
FT 4B)"
SQ SEQUENCE 147 AA; 16195 MW; 065D72BC42B0A6E0 CRC64;
MKALIILGLL CLSVAVQGKV FERCELARTL KELGLDGYKG VSLANWLCLT KWESSYNTKA
TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENNIAKA VACAKHIVSE
QGITAWVAWK SHCRDHDVSS YVEGCSL
