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Lysozyme C, non-stomach isozyme (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C)

 LYSCN_BOVIN             Reviewed;         148 AA.
P80189; Q29447; Q2KIL2;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 4.
28-MAR-2018, entry version 133.
RecName: Full=Lysozyme C, non-stomach isozyme;
EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C;
Flags: Precursor;
Name=LYS; Synonyms=LZ;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Trachea;
PubMed=8262986;
Takeuchi K., Irwin D.M., Gallup M., Shinbrot E., Kai H., Stewart C.B.,
Basbaum C.;
"Multiple cDNA sequences of bovine tracheal lysozyme.";
J. Biol. Chem. 268:27440-27446(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Deutsche Schwarzbunte; TISSUE=Blood;
PubMed=8921904; DOI=10.1016/0378-1119(96)00352-6;
Henke M., Hobom G., Senft B., Seyfert H.-M.;
"Structural deviations in a bovine low expression lysozyme-encoding
gene active in tissues other than stomach.";
Gene 178:131-137(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7894180; DOI=10.1007/BF00292034;
Brunner R.M., Henke M., Guerin G., Goldammer T., Seyfert H.M.,
Schwerin M.;
"The macrophage expressed variant of the bovine lysozyme-encoding gene
maps to chromosome 5q23.";
Mamm. Genome 5:834-834(1994).
[4]
NUCLEOTIDE SEQUENCE.
TISSUE=Kidney;
PubMed=8477739; DOI=10.1111/j.1432-1033.1993.tb17805.x;
Ito Y., Yamada H., Nakamura M., Yoshikawa A., Ueda T., Imoto T.;
"The primary structures and properties of non-stomach lysozymes of
sheep and cow, and implication for functional divergence of
lysozyme.";
Eur. J. Biochem. 213:649-658(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-148.
TISSUE=Granulocyte, and Mammary gland;
PubMed=8206386; DOI=10.1016/0378-1119(94)90109-0;
Steinhoff U.M., Senft B., Seyfert H.-M.;
"Lysozyme-encoding bovine cDNAs from neutrophile granulocytes and
mammary gland are derived from a different gene than stomach
lysozymes.";
Gene 143:271-276(1994).
-!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
in tissues and body fluids are associated with the monocyte-
macrophage system and enhance the activity of immunoagents.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins.
-!- TISSUE SPECIFICITY: Expressed in blood cells.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
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EMBL; L23757; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U25810; AAC48683.1; -; Genomic_DNA.
EMBL; BC112597; AAI12598.1; -; mRNA.
EMBL; L19980; AAA99863.1; -; mRNA.
PIR; C49315; C49315.
RefSeq; NP_001071627.1; NM_001078159.1.
UniGene; Bt.64645; -.
ProteinModelPortal; P80189; -.
SMR; P80189; -.
STRING; 9913.ENSBTAP00000038081; -.
CAZy; GH22; Glycoside Hydrolase Family 22.
PaxDb; P80189; -.
PeptideAtlas; P80189; -.
PRIDE; P80189; -.
Ensembl; ENSBTAT00000038266; ENSBTAP00000038081; ENSBTAG00000026779.
GeneID; 777776; -.
KEGG; bta:777776; -.
CTD; 4069; -.
eggNOG; ENOG410IXGD; Eukaryota.
eggNOG; ENOG4111QHM; LUCA.
GeneTree; ENSGT00550000074398; -.
HOGENOM; HOG000037357; -.
HOVERGEN; HBG052297; -.
InParanoid; P80189; -.
KO; K13915; -.
OMA; KWESNYN; -.
OrthoDB; EOG091G0R9V; -.
TreeFam; TF324882; -.
BRENDA; 3.2.1.17; 908.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-6803157; Antimicrobial peptides.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000026779; -.
ExpressionAtlas; P80189; baseline and differential.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IBA:GO_Central.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000974; Glyco_hydro_22_lys.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR030056; Lysozyme_C.
PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
Pfam; PF00062; Lys; 1.
PRINTS; PR00137; LYSOZYME.
PRINTS; PR00135; LYZLACT.
SMART; SM00263; LYZ1; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
2: Evidence at transcript level;
Antimicrobial; Bacteriolytic enzyme; Complete proteome;
Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 148 Lysozyme C, non-stomach isozyme.
/FTId=PRO_0000018458.
ACT_SITE 53 53 {ECO:0000255|PROSITE-ProRule:PRU00680}.
ACT_SITE 71 71 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 24 146 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 48 134 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 83 99 {ECO:0000255|PROSITE-ProRule:PRU00680}.
DISULFID 95 113 {ECO:0000255|PROSITE-ProRule:PRU00680}.
CONFLICT 114 114 A -> T (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 117 117 V -> D (in Ref. 2 and 3). {ECO:0000305}.
SEQUENCE 148 AA; 16476 MW; 707A79AA7FDA4FAC CRC64;
MKALLILGLL LFSVAVQGKV FERCELARSL KRFGMDNFRG ISLANWMCLA RWESNYNTQA
TNYNAGDQST DYGIFQINSH WWCNDGKTPG AVNACHLPCG ALLQDDITQA VACAKRVVSD
PQGIRAWVAW RSHCQNQDLT SYIQGCGV


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