ID   LYS_HYACE               Reviewed;         139 AA.
AC   P05105;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase;
DE   Flags: Precursor;
OS   Hyalophora cecropia (Cecropia moth) (Samia cecropia).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Attacini; Hyalophora.
OX   NCBI_TaxID=7123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2007608; DOI=10.1016/s0021-9258(18)38165-1;
RA   Sun S.-C., Aasling B., Faye I.;
RT   "Organization and expression of the immunoresponsive lysozyme gene in the
RT   giant silk moth, Hyalophora cecropia.";
RL   J. Biol. Chem. 266:6644-6649(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 13-139, AND POLYMORPHISM.
RX   PubMed=16453632; DOI=10.1002/j.1460-2075.1985.tb03901.x;
RA   Engstroem A., Xanthopoulos K.G., Boman H.G., Bennich H.;
RT   "Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia.";
RL   EMBO J. 4:2119-2122(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 13-139.
RX   PubMed=3840100; DOI=10.1016/0145-305x(85)90018-7;
RA   Boman H.G., Faye I., von Hofsten P., Kockum K., Lee J.-Y.,
RA   Xanthopoulos K.G., Bennich H., Engstroem A., Merrifield R.B., Andreu D.;
RT   "On the primary structures of lysozyme, cecropins and attacins from
RT   Hyalophora cecropia.";
RL   Dev. Comp. Immunol. 9:551-558(1985).
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   -!- POLYMORPHISM: 3 allelic variants of cecropia moth lysozyme have been
CC       found. The sequence shown is that of lysozyme 1.
CC       {ECO:0000269|PubMed:16453632}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA29190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA26542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M60914; AAA29189.1; -; Genomic_DNA.
DR   EMBL; X02765; CAA26542.1; ALT_INIT; mRNA.
DR   EMBL; M34923; AAA29190.1; ALT_INIT; mRNA.
DR   PIR; A24649; LZWK.
DR   PIR; A38744; A38744.
DR   AlphaFoldDB; P05105; -.
DR   SMR; P05105; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16899; LYZ_C_invert; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF63; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..139
FT                   /note="Lysozyme"
FT                   /id="PRO_0000018506"
FT   DOMAIN          20..139
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        25..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        46..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        81..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        91..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   VARIANT         34
FT                   /note="L -> R (in lysozyme-2)"
FT   VARIANT         85
FT                   /note="T -> S (in lysozyme-2 and lysozyme-3)"
SQ   SEQUENCE   139 AA;  15877 MW;  E8AF5C2CE561F641 CRC64;
     MTKYVILLAV LAFALHCDAK RFTRCGLVQE LRRLGFDETL MSNWVCLVEN ESGRFTDKIG
     KVNKNGSRDY GLFQINDKYW CSKGTTPGKD CNVTCNQLLT DDISVAATCA KKIYKRHKFD
     AWYGWKNHCQ HGLPDISDC
//