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LYSCN_BOVIN
ID   LYSCN_BOVIN             Reviewed;         148 AA.
AC   P80189; Q29447; Q2KIL2;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 4.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Lysozyme C, non-stomach isozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYS; Synonyms=LZ;
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].
RC   TISSUE=Trachea;
RX   PubMed=8262986; DOI=10.1016/s0021-9258(19)74267-7;
RA   Takeuchi K., Irwin D.M., Gallup M., Shinbrot E., Kai H., Stewart C.B.,
RA   Basbaum C.;
RT   "Multiple cDNA sequences of bovine tracheal lysozyme.";
RL   J. Biol. Chem. 268:27440-27446(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Deutsche Schwarzbunte; TISSUE=Blood;
RX   PubMed=8921904; DOI=10.1016/0378-1119(96)00352-6;
RA   Henke M., Hobom G., Senft B., Seyfert H.-M.;
RT   "Structural deviations in a bovine low expression lysozyme-encoding gene
RT   active in tissues other than stomach.";
RL   Gene 178:131-137(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7894180; DOI=10.1007/bf00292034;
RA   Brunner R.M., Henke M., Guerin G., Goldammer T., Seyfert H.M., Schwerin M.;
RT   "The macrophage expressed variant of the bovine lysozyme-encoding gene maps
RT   to chromosome 5q23.";
RL   Mamm. Genome 5:834-834(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney;
RX   PubMed=8477739; DOI=10.1111/j.1432-1033.1993.tb17805.x;
RA   Ito Y., Yamada H., Nakamura M., Yoshikawa A., Ueda T., Imoto T.;
RT   "The primary structures and properties of non-stomach lysozymes of sheep
RT   and cow, and implication for functional divergence of lysozyme.";
RL   Eur. J. Biochem. 213:649-658(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-148.
RC   TISSUE=Granulocyte, and Mammary gland;
RX   PubMed=8206386; DOI=10.1016/0378-1119(94)90109-0;
RA   Steinhoff U.M., Senft B., Seyfert H.-M.;
RT   "Lysozyme-encoding bovine cDNAs from neutrophile granulocytes and mammary
RT   gland are derived from a different gene than stomach lysozymes.";
RL   Gene 143:271-276(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.
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   -!- TISSUE SPECIFICITY: Expressed in blood cells.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; L23757; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U25810; AAC48683.1; -; Genomic_DNA.
DR   EMBL; BC112597; AAI12598.1; -; mRNA.
DR   EMBL; L19980; AAA99863.1; -; mRNA.
DR   PIR; C49315; C49315.
DR   RefSeq; NP_001071627.1; NM_001078159.1.
DR   AlphaFoldDB; P80189; -.
DR   SMR; P80189; -.
DR   STRING; 9913.ENSBTAP00000038081; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; P80189; -.
DR   PeptideAtlas; P80189; -.
DR   PRIDE; P80189; -.
DR   Ensembl; ENSBTAT00000038266; ENSBTAP00000038081; ENSBTAG00000026779.
DR   GeneID; 777776; -.
DR   KEGG; bta:777776; -.
DR   CTD; 4069; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026779; -.
DR   eggNOG; ENOG502S1S1; Eukaryota.
DR   GeneTree; ENSGT00940000153832; -.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; P80189; -.
DR   OMA; RINCSAF; -.
DR   OrthoDB; 1551203at2759; -.
DR   TreeFam; TF324882; -.
DR   BRENDA; 3.2.1.17; 908.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-6803157; Antimicrobial peptides.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000026779; Expressed in monocyte and 103 other tissues.
DR   ExpressionAtlas; P80189; baseline and differential.
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: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; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..148
FT                   /note="Lysozyme C, non-stomach isozyme"
FT                   /id="PRO_0000018458"
FT   DOMAIN          19..148
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..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        48..134
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   CONFLICT        114
FT                   /note="A -> T (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="V -> D (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   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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