ID   LYG_CHICK               Reviewed;         211 AA.
AC   P27042;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Lysozyme g;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   AltName: Full=Goose-type lysozyme;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1932124; DOI=10.1016/0167-4781(91)90118-6;
RA   Nakano T., Graf T.;
RT   "Goose-type lysozyme gene of the chicken: sequence, genomic organization
RT   and expression reveals major differences to chicken-type lysozyme gene.";
RL   Biochim. Biophys. Acta 1090:273-276(1991).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Granulocyte compartment of myelomonocytic cells.
CC   -!- MISCELLANEOUS: Shows preference for N-acetylmuramic acid residues that
CC       are substituted with a peptide moiety. It acts only as a
CC       glycanohydrolase.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family. {ECO:0000305}.
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DR   EMBL; X61001; CAA43319.1; -; Genomic_DNA.
DR   EMBL; X61002; CAA43320.1; -; mRNA.
DR   EMBL; X61197; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X61198; CAB37929.1; -; mRNA.
DR   PIR; S18463; S18463.
DR   RefSeq; NP_001001470.1; NM_001001470.1.
DR   RefSeq; XP_015133176.1; XM_015277690.1.
DR   AlphaFoldDB; P27042; -.
DR   SMR; P27042; -.
DR   STRING; 9031.ENSGALP00000027012; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PaxDb; P27042; -.
DR   GeneID; 395708; -.
DR   KEGG; gga:395708; -.
DR   CTD; 254773; -.
DR   VEuPathDB; HostDB:geneid_395708; -.
DR   eggNOG; ENOG502RZXI; Eukaryota.
DR   OrthoDB; 1255725at2759; -.
DR   PhylomeDB; P27042; -.
DR   PRO; PR:P27042; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   InterPro; IPR002152; Glyco_hydro_23.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   PIRSF; PIRSF001065; Lysozyme_g; 1.
DR   PRINTS; PR00749; LYSOZYMEG.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..211
FT                   /note="Lysozyme g"
FT                   /id="PRO_0000012022"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..55
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  23238 MW;  8ECBE38AC9F67A9E CRC64;
     MLGKNDPMCL VLVLLGLTAL LGICQGGTGC YGSVSRIDTT GASCRTAKPE GLSYCGVRAS
     RTIAERDLGS MNKYKVLIKR VGEALCIEPA VIAGIISRES HAGKILKNGW GDRGNGFGLM
     QVDKRYHKIE GTWNGEAHIR QGTRILIDMV KKIQRKFPRW TRDQQLKGGI SAYNAGVGNV
     RSYERMDIGT LHDDYSNDVV ARAQYFKQHG Y