LYSC_HUMAN
ID LYSC_HUMAN Reviewed; 148 AA.
AC P61626; P00695; Q13170; Q9UCF8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
GN Name=LYZ; Synonyms=LZM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2971592; DOI=10.1016/0378-1119(88)90359-9;
RA Castanon M.J., Spevak W., Adolf G.R., Chlebowicz-Sledziewska E.,
RA Sledziewski A.;
RT "Cloning of human lysozyme gene and expression in the yeast Saccharomyces
RT cerevisiae.";
RL Gene 66:223-234(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3413092; DOI=10.1073/pnas.85.17.6227;
RA Chung L.P., Keshav S., Gordon S.;
RT "Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in
RT situ hybridization for macrophages and Paneth cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6227-6231(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2829884; DOI=10.1016/0006-291x(88)90461-5;
RA Yoshimura K., Toibana A., Nakahama K.;
RT "Human lysozyme: sequencing of a cDNA, and expression and secretion by
RT Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 150:794-801(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2546758; DOI=10.1111/j.1432-1033.1989.tb14857.x;
RA Peters C.W.B., Kruse U., Pollwein R., Grzeschik K.H., Sippel A.E.;
RT "The human lysozyme gene. Sequence organization and chromosomal
RT localization.";
RL Eur. J. Biochem. 182:507-516(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang B., Zhao C., Lei X., Cai L.;
RT "The cloning, sequencing and analysis of Chinese human lysozyme gene cDNA
RT amplified with RT-PCR from human placental total RNA.";
RL Sheng Wu Hua Hsueh Tsa Chih 9:269-273(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 19-148.
RC TISSUE=Urine;
RX PubMed=5284421; DOI=10.1038/newbio232016a0;
RA Canfield R.E., Kammerman S., Sobel H.H., Morgan F.J.;
RT "Primary structure of lysozymes from man and goose.";
RL Nature New Biol. 232:16-17(1971).
RN [8]
RP PROTEIN SEQUENCE OF 19-148, AND SEQUENCE REVISION TO 118.
RC TISSUE=Urine;
RX PubMed=11946554; DOI=10.1016/0014-5793(72)80212-6;
RA Thomsen J., Lund E.H., Kristiansen K., Brunfeldt K., Malmquist J.;
RT "A Val-Val sequence found in a human monocytic leukemia lysozyme.";
RL FEBS Lett. 22:34-36(1972).
RN [9]
RP PROTEIN SEQUENCE OF 19-148.
RC TISSUE=Milk;
RX PubMed=5168859; DOI=10.1002/hlca.19710540830;
RA Jolles J., Jolles P.;
RT "Human milk lysozyme: unpublished data concerning the establishment of the
RT complete primary structure; comparison with lysozymes of various origins.";
RL Helv. Chim. Acta 54:2668-2675(1971).
RN [10]
RP PROTEIN SEQUENCE OF 19-148, AND SEQUENCE REVISION TO 118.
RC TISSUE=Milk;
RX PubMed=11946553; DOI=10.1016/0014-5793(72)80211-4;
RA Jolles J., Jolles P.;
RT "Comparison between human and bird lysozymes: note concerning the
RT previously observed deletion.";
RL FEBS Lett. 22:31-33(1972).
RN [11]
RP PROTEIN SEQUENCE OF 19-41 AND 96-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [12]
RP FOLDING, AND MUTAGENESIS.
RX PubMed=8503881; DOI=10.1042/bj2920469;
RA Kanaya E., Ishihara K., Tsunasawa S., Nokihara K., Kikuchi M.;
RT "Indication of possible post-translational formation of disulphide bonds in
RT the beta-sheet domain of human lysozyme.";
RL Biochem. J. 292:469-476(1993).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Banyard S.H., Blake C.C.F., Swan I.D.A.;
RT "The high resolution X-ray study of human. lysozyme: a preliminary
RT analysis.";
RL (In) Osserman E.F., Canfield R.E., Beychok S. (eds.);
RL Lysozyme, pp.71-79, Academic Press, New York (1974).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=7334520; DOI=10.1016/0022-2836(81)90125-x;
RA Artymiuk P.J., Blake C.C.F.;
RT "Refinement of human lysozyme at 1.5-A resolution analysis of non-bonded
RT and hydrogen-bond interactions.";
RL J. Mol. Biol. 152:737-762(1981).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=6876162; DOI=10.1016/s0022-2836(83)80105-3;
RA Blake C.C.F., Pulford W.C.A., Artymiuk P.J.;
RT "X-ray studies of water in crystals of lysozyme.";
RL J. Mol. Biol. 167:693-723(1983).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-99 AND ALA-113.
RX PubMed=2061330; DOI=10.1016/s0021-9258(18)98941-6;
RA Inaka K., Taniyama Y., Kikuchi M., Morikawa K., Matsushima M.;
RT "The crystal structure of a mutant human lysozyme C77/95A with increased
RT secretion efficiency in yeast.";
RL J. Biol. Chem. 266:12599-12603(1991).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 AND 1.1 ANGSTROMS).
RX PubMed=9757091; DOI=10.1107/s0907444997016922;
RA Steinrauf L.K.;
RT "Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic
RT lysozyme nitrate at 1.1 A.";
RL Acta Crystallogr. D 54:767-780(1998).
RN [20]
RP STRUCTURE BY NMR.
RX PubMed=2207098; DOI=10.1021/bi00483a007;
RA Redfield C., Dobson C.M.;
RT "1H NMR studies of human lysozyme: spectral assignment and comparison with
RT hen lysozyme.";
RL Biochemistry 29:7201-7214(1990).
RN [21]
RP STRUCTURE BY NMR.
RX PubMed=1794972; DOI=10.1093/oxfordjournals.jbchem.a123672;
RA Ohkubo T., Taniyama Y., Kikuchi M.;
RT "1H and 15N NMR study of human lysozyme.";
RL J. Biochem. 110:1022-1029(1991).
RN [22]
RP VARIANTS AMYL8 THR-74 AND HIS-85.
RX PubMed=8464497; DOI=10.1038/362553a0;
RA Pepy M.B., Hawkins P.N., Booth D.R., Vigushin D.M., Tennent G.A.,
RA Soutar A.K., Totty N., Nguyen O., Blake C.C.F., Terry C.J., Feest T.G.,
RA Zalin A.M., Hsuan J.J.;
RT "Human lysozyme gene mutations cause hereditary systemic amyloidosis.";
RL Nature 362:553-557(1993).
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 -!- INTERACTION:
CC P61626; P61626: LYZ; NbExp=3; IntAct=EBI-355360, EBI-355360;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary
CC generalized amyloidosis. Clinical features include extensive visceral
CC amyloid deposits, renal amyloidosis resulting in nephrotic syndrome,
CC arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin
CC rash. There is no involvement of the nervous system.
CC {ECO:0000269|PubMed:8464497}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lysozyme entry;
CC URL="https://en.wikipedia.org/wiki/Lysozyme";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M21119; AAA36188.1; -; mRNA.
DR EMBL; J03801; AAA59535.1; -; mRNA.
DR EMBL; M19045; AAA59536.1; -; mRNA.
DR EMBL; X14008; CAA32175.1; ALT_INIT; Genomic_DNA.
DR EMBL; U25677; AAC63078.1; -; mRNA.
DR EMBL; BC004147; AAH04147.1; -; mRNA.
DR CCDS; CCDS8989.1; -.
DR PIR; S04938; LZHU.
DR RefSeq; NP_000230.1; NM_000239.2.
DR PDB; 133L; X-ray; 1.77 A; A=19-148.
DR PDB; 134L; X-ray; 1.77 A; A=19-148.
DR PDB; 1B5U; X-ray; 1.80 A; A=19-148.
DR PDB; 1B5V; X-ray; 2.17 A; A=19-148.
DR PDB; 1B5W; X-ray; 2.17 A; A=19-148.
DR PDB; 1B5X; X-ray; 2.00 A; A=19-148.
DR PDB; 1B5Y; X-ray; 2.20 A; A=19-148.
DR PDB; 1B5Z; X-ray; 2.20 A; A/B=19-148.
DR PDB; 1B7L; X-ray; 1.80 A; A=19-148.
DR PDB; 1B7M; X-ray; 2.20 A; A=19-148.
DR PDB; 1B7N; X-ray; 1.80 A; A=19-148.
DR PDB; 1B7O; X-ray; 1.80 A; A=19-148.
DR PDB; 1B7P; X-ray; 2.00 A; A=19-148.
DR PDB; 1B7Q; X-ray; 2.00 A; A=19-148.
DR PDB; 1B7R; X-ray; 1.80 A; A=19-148.
DR PDB; 1B7S; X-ray; 2.00 A; A=19-148.
DR PDB; 1BB3; X-ray; 1.80 A; A/B=19-148.
DR PDB; 1BB4; X-ray; 2.23 A; A/B=19-148.
DR PDB; 1BB5; X-ray; 1.80 A; A/B=19-148.
DR PDB; 1C43; X-ray; 1.80 A; A=19-148.
DR PDB; 1C45; X-ray; 1.80 A; A=19-148.
DR PDB; 1C46; X-ray; 2.20 A; A=19-148.
DR PDB; 1C7P; X-ray; 2.40 A; A=16-148.
DR PDB; 1CJ6; X-ray; 1.80 A; A=19-148.
DR PDB; 1CJ7; X-ray; 1.80 A; A=19-148.
DR PDB; 1CJ8; X-ray; 1.80 A; A=19-148.
DR PDB; 1CJ9; X-ray; 1.80 A; A=19-148.
DR PDB; 1CKC; X-ray; 1.80 A; A=19-148.
DR PDB; 1CKD; X-ray; 1.80 A; A=19-148.
DR PDB; 1CKF; X-ray; 1.80 A; A=19-148.
DR PDB; 1CKG; X-ray; 2.20 A; A/B=19-148.
DR PDB; 1CKH; X-ray; 2.00 A; A=19-148.
DR PDB; 1D6P; X-ray; 2.23 A; A=19-148.
DR PDB; 1D6Q; X-ray; 1.96 A; A=19-148.
DR PDB; 1DI3; X-ray; 1.80 A; A=19-148.
DR PDB; 1DI4; X-ray; 2.00 A; A=19-148.
DR PDB; 1DI5; X-ray; 2.20 A; A=19-148.
DR PDB; 1EQ4; X-ray; 1.80 A; A=19-148.
DR PDB; 1EQ5; X-ray; 1.80 A; A=19-148.
DR PDB; 1EQE; X-ray; 1.80 A; A=19-148.
DR PDB; 1GAY; X-ray; 1.80 A; A=19-148.
DR PDB; 1GAZ; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB0; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB2; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB3; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB5; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB6; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB7; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB8; X-ray; 1.80 A; A=19-148.
DR PDB; 1GB9; X-ray; 1.80 A; A=19-148.
DR PDB; 1GBO; X-ray; 1.80 A; A=19-148.
DR PDB; 1GBW; X-ray; 1.80 A; A=19-148.
DR PDB; 1GBX; X-ray; 1.80 A; A=19-148.
DR PDB; 1GBY; X-ray; 1.80 A; A=19-148.
DR PDB; 1GBZ; X-ray; 1.80 A; A=19-148.
DR PDB; 1GDW; X-ray; 1.80 A; A=19-148.
DR PDB; 1GDX; X-ray; 1.80 A; A=19-148.
DR PDB; 1GE0; X-ray; 1.80 A; A=19-148.
DR PDB; 1GE1; X-ray; 1.70 A; A=19-148.
DR PDB; 1GE2; X-ray; 2.00 A; A=19-148.
DR PDB; 1GE3; X-ray; 1.80 A; A=19-148.
DR PDB; 1GE4; X-ray; 1.80 A; A=19-148.
DR PDB; 1GEV; X-ray; 2.10 A; A=19-148.
DR PDB; 1GEZ; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF0; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF3; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF4; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF5; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF6; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF7; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF8; X-ray; 1.80 A; A=19-148.
DR PDB; 1GF9; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFA; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFE; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFG; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFH; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFJ; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFK; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFR; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFT; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFU; X-ray; 1.80 A; A=19-148.
DR PDB; 1GFV; X-ray; 1.80 A; A=19-148.
DR PDB; 1HNL; X-ray; 1.80 A; A=19-148.
DR PDB; 1I1Z; X-ray; 1.80 A; A=19-148.
DR PDB; 1I20; X-ray; 1.90 A; A=19-148.
DR PDB; 1I22; X-ray; 1.80 A; A/B/C/D=19-148.
DR PDB; 1INU; X-ray; 1.80 A; A=19-148.
DR PDB; 1IOC; X-ray; 2.40 A; A=19-148.
DR PDB; 1IP1; X-ray; 1.80 A; A=19-148.
DR PDB; 1IP2; X-ray; 1.80 A; A=19-148.
DR PDB; 1IP3; X-ray; 1.80 A; A/B=19-148.
DR PDB; 1IP4; X-ray; 1.80 A; A=19-148.
DR PDB; 1IP5; X-ray; 1.80 A; A=19-148.
DR PDB; 1IP6; X-ray; 1.80 A; A=19-148.
DR PDB; 1IP7; X-ray; 1.90 A; A/B=19-146.
DR PDB; 1IWT; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWU; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWV; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWW; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWX; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWY; X-ray; 1.40 A; A=19-148.
DR PDB; 1IWZ; X-ray; 1.48 A; A=19-148.
DR PDB; 1IX0; X-ray; 1.80 A; A=19-148.
DR PDB; 1IY3; NMR; -; A=19-148.
DR PDB; 1IY4; NMR; -; A=19-148.
DR PDB; 1JKA; X-ray; 1.66 A; A=19-148.
DR PDB; 1JKB; X-ray; 1.66 A; A=19-148.
DR PDB; 1JKC; X-ray; 1.60 A; A=19-148.
DR PDB; 1JKD; X-ray; 1.80 A; A=19-148.
DR PDB; 1JSF; X-ray; 1.15 A; A=19-148.
DR PDB; 1JWR; X-ray; 1.40 A; A=19-148.
DR PDB; 1LAA; X-ray; 1.77 A; A=19-148.
DR PDB; 1LHH; X-ray; 1.80 A; A=19-148.
DR PDB; 1LHI; X-ray; 1.80 A; A=19-148.
DR PDB; 1LHJ; X-ray; 1.80 A; A=19-148.
DR PDB; 1LHK; X-ray; 1.80 A; A=19-148.
DR PDB; 1LHL; X-ray; 1.80 A; A=19-148.
DR PDB; 1LHM; X-ray; 1.80 A; A=19-148.
DR PDB; 1LMT; X-ray; 1.60 A; A=19-148.
DR PDB; 1LOZ; X-ray; 1.80 A; A=19-148.
DR PDB; 1LYY; X-ray; 1.80 A; A=19-148.
DR PDB; 1LZ1; X-ray; 1.50 A; A=19-148.
DR PDB; 1LZ4; X-ray; 1.80 A; A=19-148.
DR PDB; 1LZ5; X-ray; 1.80 A; A=19-144.
DR PDB; 1LZ6; X-ray; 1.80 A; A=19-140.
DR PDB; 1LZR; X-ray; 1.50 A; A=19-148.
DR PDB; 1LZS; X-ray; 1.60 A; A/B=19-148.
DR PDB; 1OP9; X-ray; 1.86 A; B=19-148.
DR PDB; 1OUA; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUB; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUC; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUD; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUE; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUF; X-ray; 1.80 A; A=19-147.
DR PDB; 1OUG; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUH; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUI; X-ray; 1.80 A; A=19-148.
DR PDB; 1OUJ; X-ray; 1.80 A; A=19-148.
DR PDB; 1QSW; X-ray; 1.85 A; A/B/C/D=19-148.
DR PDB; 1RE2; X-ray; 2.30 A; A=19-148.
DR PDB; 1REM; X-ray; 2.10 A; A=19-148.
DR PDB; 1REX; X-ray; 1.50 A; A=19-148.
DR PDB; 1REY; X-ray; 1.70 A; A=19-148.
DR PDB; 1REZ; X-ray; 1.70 A; A=19-148.
DR PDB; 1TAY; X-ray; 1.70 A; A=19-148.
DR PDB; 1TBY; X-ray; 1.77 A; A=19-148.
DR PDB; 1TCY; X-ray; 1.70 A; A=19-148.
DR PDB; 1TDY; X-ray; 1.70 A; A=19-148.
DR PDB; 1UBZ; X-ray; 2.00 A; A=19-148.
DR PDB; 1W08; X-ray; 2.50 A; A=19-148.
DR PDB; 1WQM; X-ray; 1.80 A; A=19-148.
DR PDB; 1WQN; X-ray; 1.80 A; A=19-148.
DR PDB; 1WQO; X-ray; 1.80 A; A=19-148.
DR PDB; 1WQP; X-ray; 1.80 A; A=19-148.
DR PDB; 1WQQ; X-ray; 1.80 A; A=19-148.
DR PDB; 1WQR; X-ray; 1.80 A; A=19-148.
DR PDB; 1YAM; X-ray; 1.80 A; A=19-148.
DR PDB; 1YAN; X-ray; 1.80 A; A=19-148.
DR PDB; 1YAO; X-ray; 1.80 A; A=19-148.
DR PDB; 1YAP; X-ray; 1.80 A; A=19-148.
DR PDB; 1YAQ; X-ray; 1.80 A; A=19-148.
DR PDB; 207L; X-ray; 1.80 A; A=19-148.
DR PDB; 208L; X-ray; 2.20 A; A=19-148.
DR PDB; 2BQA; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQB; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQC; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQD; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQE; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQF; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQG; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQH; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQI; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQJ; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQK; X-ray; 1.80 A; A=19-147.
DR PDB; 2BQL; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQM; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQN; X-ray; 1.80 A; A=19-148.
DR PDB; 2BQO; X-ray; 1.80 A; A=19-148.
DR PDB; 2HEA; X-ray; 1.80 A; A=19-148.
DR PDB; 2HEB; X-ray; 2.20 A; A=19-148.
DR PDB; 2HEC; X-ray; 1.80 A; A=19-148.
DR PDB; 2HED; X-ray; 1.80 A; A=19-148.
DR PDB; 2HEE; X-ray; 1.80 A; A=19-148.
DR PDB; 2HEF; X-ray; 1.80 A; A=19-148.
DR PDB; 2LHM; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEA; X-ray; 2.20 A; A/B=19-148.
DR PDB; 2MEB; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEC; X-ray; 2.20 A; A/B=19-148.
DR PDB; 2MED; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEE; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEF; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEG; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEH; X-ray; 1.80 A; A=19-148.
DR PDB; 2MEI; X-ray; 1.80 A; A=19-148.
DR PDB; 2NWD; X-ray; 1.04 A; X=19-148.
DR PDB; 2ZIJ; X-ray; 1.90 A; A=19-148.
DR PDB; 2ZIK; X-ray; 1.81 A; A=19-148.
DR PDB; 2ZIL; X-ray; 1.80 A; A=19-148.
DR PDB; 2ZWB; Neutron; 1.80 A; A=19-148.
DR PDB; 3EBA; X-ray; 1.85 A; B=19-148.
DR PDB; 3FE0; X-ray; 1.50 A; A=19-148.
DR PDB; 3LHM; X-ray; 1.80 A; A=19-148.
DR PDB; 3LN2; X-ray; 2.04 A; A/B=19-148.
DR PDB; 4I0C; X-ray; 1.95 A; A/B=19-148.
DR PDB; 4ML7; X-ray; 1.80 A; A/C=19-148.
DR PDB; 4R0P; X-ray; 1.52 A; A=74-79.
DR PDB; 5LSH; X-ray; 1.06 A; A=19-148.
DR PDB; 5LVK; X-ray; 2.49 A; A/B=19-148.
DR PDB; 6LFH; X-ray; 1.46 A; X=19-148.
DR PDB; 7AP7; X-ray; 1.15 A; A=19-148.
DR PDB; 7XF6; X-ray; 1.30 A; A=19-148.
DR PDB; 7XF7; X-ray; 1.55 A; A=19-148.
DR PDB; 7XF8; X-ray; 1.60 A; A=19-148.
DR PDBsum; 133L; -.
DR PDBsum; 134L; -.
DR PDBsum; 1B5U; -.
DR PDBsum; 1B5V; -.
DR PDBsum; 1B5W; -.
DR PDBsum; 1B5X; -.
DR PDBsum; 1B5Y; -.
DR PDBsum; 1B5Z; -.
DR PDBsum; 1B7L; -.
DR PDBsum; 1B7M; -.
DR PDBsum; 1B7N; -.
DR PDBsum; 1B7O; -.
DR PDBsum; 1B7P; -.
DR PDBsum; 1B7Q; -.
DR PDBsum; 1B7R; -.
DR PDBsum; 1B7S; -.
DR PDBsum; 1BB3; -.
DR PDBsum; 1BB4; -.
DR PDBsum; 1BB5; -.
DR PDBsum; 1C43; -.
DR PDBsum; 1C45; -.
DR PDBsum; 1C46; -.
DR PDBsum; 1C7P; -.
DR PDBsum; 1CJ6; -.
DR PDBsum; 1CJ7; -.
DR PDBsum; 1CJ8; -.
DR PDBsum; 1CJ9; -.
DR PDBsum; 1CKC; -.
DR PDBsum; 1CKD; -.
DR PDBsum; 1CKF; -.
DR PDBsum; 1CKG; -.
DR PDBsum; 1CKH; -.
DR PDBsum; 1D6P; -.
DR PDBsum; 1D6Q; -.
DR PDBsum; 1DI3; -.
DR PDBsum; 1DI4; -.
DR PDBsum; 1DI5; -.
DR PDBsum; 1EQ4; -.
DR PDBsum; 1EQ5; -.
DR PDBsum; 1EQE; -.
DR PDBsum; 1GAY; -.
DR PDBsum; 1GAZ; -.
DR PDBsum; 1GB0; -.
DR PDBsum; 1GB2; -.
DR PDBsum; 1GB3; -.
DR PDBsum; 1GB5; -.
DR PDBsum; 1GB6; -.
DR PDBsum; 1GB7; -.
DR PDBsum; 1GB8; -.
DR PDBsum; 1GB9; -.
DR PDBsum; 1GBO; -.
DR PDBsum; 1GBW; -.
DR PDBsum; 1GBX; -.
DR PDBsum; 1GBY; -.
DR PDBsum; 1GBZ; -.
DR PDBsum; 1GDW; -.
DR PDBsum; 1GDX; -.
DR PDBsum; 1GE0; -.
DR PDBsum; 1GE1; -.
DR PDBsum; 1GE2; -.
DR PDBsum; 1GE3; -.
DR PDBsum; 1GE4; -.
DR PDBsum; 1GEV; -.
DR PDBsum; 1GEZ; -.
DR PDBsum; 1GF0; -.
DR PDBsum; 1GF3; -.
DR PDBsum; 1GF4; -.
DR PDBsum; 1GF5; -.
DR PDBsum; 1GF6; -.
DR PDBsum; 1GF7; -.
DR PDBsum; 1GF8; -.
DR PDBsum; 1GF9; -.
DR PDBsum; 1GFA; -.
DR PDBsum; 1GFE; -.
DR PDBsum; 1GFG; -.
DR PDBsum; 1GFH; -.
DR PDBsum; 1GFJ; -.
DR PDBsum; 1GFK; -.
DR PDBsum; 1GFR; -.
DR PDBsum; 1GFT; -.
DR PDBsum; 1GFU; -.
DR PDBsum; 1GFV; -.
DR PDBsum; 1HNL; -.
DR PDBsum; 1I1Z; -.
DR PDBsum; 1I20; -.
DR PDBsum; 1I22; -.
DR PDBsum; 1INU; -.
DR PDBsum; 1IOC; -.
DR PDBsum; 1IP1; -.
DR PDBsum; 1IP2; -.
DR PDBsum; 1IP3; -.
DR PDBsum; 1IP4; -.
DR PDBsum; 1IP5; -.
DR PDBsum; 1IP6; -.
DR PDBsum; 1IP7; -.
DR PDBsum; 1IWT; -.
DR PDBsum; 1IWU; -.
DR PDBsum; 1IWV; -.
DR PDBsum; 1IWW; -.
DR PDBsum; 1IWX; -.
DR PDBsum; 1IWY; -.
DR PDBsum; 1IWZ; -.
DR PDBsum; 1IX0; -.
DR PDBsum; 1IY3; -.
DR PDBsum; 1IY4; -.
DR PDBsum; 1JKA; -.
DR PDBsum; 1JKB; -.
DR PDBsum; 1JKC; -.
DR PDBsum; 1JKD; -.
DR PDBsum; 1JSF; -.
DR PDBsum; 1JWR; -.
DR PDBsum; 1LAA; -.
DR PDBsum; 1LHH; -.
DR PDBsum; 1LHI; -.
DR PDBsum; 1LHJ; -.
DR PDBsum; 1LHK; -.
DR PDBsum; 1LHL; -.
DR PDBsum; 1LHM; -.
DR PDBsum; 1LMT; -.
DR PDBsum; 1LOZ; -.
DR PDBsum; 1LYY; -.
DR PDBsum; 1LZ1; -.
DR PDBsum; 1LZ4; -.
DR PDBsum; 1LZ5; -.
DR PDBsum; 1LZ6; -.
DR PDBsum; 1LZR; -.
DR PDBsum; 1LZS; -.
DR PDBsum; 1OP9; -.
DR PDBsum; 1OUA; -.
DR PDBsum; 1OUB; -.
DR PDBsum; 1OUC; -.
DR PDBsum; 1OUD; -.
DR PDBsum; 1OUE; -.
DR PDBsum; 1OUF; -.
DR PDBsum; 1OUG; -.
DR PDBsum; 1OUH; -.
DR PDBsum; 1OUI; -.
DR PDBsum; 1OUJ; -.
DR PDBsum; 1QSW; -.
DR PDBsum; 1RE2; -.
DR PDBsum; 1REM; -.
DR PDBsum; 1REX; -.
DR PDBsum; 1REY; -.
DR PDBsum; 1REZ; -.
DR PDBsum; 1TAY; -.
DR PDBsum; 1TBY; -.
DR PDBsum; 1TCY; -.
DR PDBsum; 1TDY; -.
DR PDBsum; 1UBZ; -.
DR PDBsum; 1W08; -.
DR PDBsum; 1WQM; -.
DR PDBsum; 1WQN; -.
DR PDBsum; 1WQO; -.
DR PDBsum; 1WQP; -.
DR PDBsum; 1WQQ; -.
DR PDBsum; 1WQR; -.
DR PDBsum; 1YAM; -.
DR PDBsum; 1YAN; -.
DR PDBsum; 1YAO; -.
DR PDBsum; 1YAP; -.
DR PDBsum; 1YAQ; -.
DR PDBsum; 207L; -.
DR PDBsum; 208L; -.
DR PDBsum; 2BQA; -.
DR PDBsum; 2BQB; -.
DR PDBsum; 2BQC; -.
DR PDBsum; 2BQD; -.
DR PDBsum; 2BQE; -.
DR PDBsum; 2BQF; -.
DR PDBsum; 2BQG; -.
DR PDBsum; 2BQH; -.
DR PDBsum; 2BQI; -.
DR PDBsum; 2BQJ; -.
DR PDBsum; 2BQK; -.
DR PDBsum; 2BQL; -.
DR PDBsum; 2BQM; -.
DR PDBsum; 2BQN; -.
DR PDBsum; 2BQO; -.
DR PDBsum; 2HEA; -.
DR PDBsum; 2HEB; -.
DR PDBsum; 2HEC; -.
DR PDBsum; 2HED; -.
DR PDBsum; 2HEE; -.
DR PDBsum; 2HEF; -.
DR PDBsum; 2LHM; -.
DR PDBsum; 2MEA; -.
DR PDBsum; 2MEB; -.
DR PDBsum; 2MEC; -.
DR PDBsum; 2MED; -.
DR PDBsum; 2MEE; -.
DR PDBsum; 2MEF; -.
DR PDBsum; 2MEG; -.
DR PDBsum; 2MEH; -.
DR PDBsum; 2MEI; -.
DR PDBsum; 2NWD; -.
DR PDBsum; 2ZIJ; -.
DR PDBsum; 2ZIK; -.
DR PDBsum; 2ZIL; -.
DR PDBsum; 2ZWB; -.
DR PDBsum; 3EBA; -.
DR PDBsum; 3FE0; -.
DR PDBsum; 3LHM; -.
DR PDBsum; 3LN2; -.
DR PDBsum; 4I0C; -.
DR PDBsum; 4ML7; -.
DR PDBsum; 4R0P; -.
DR PDBsum; 5LSH; -.
DR PDBsum; 5LVK; -.
DR PDBsum; 6LFH; -.
DR PDBsum; 7AP7; -.
DR PDBsum; 7XF6; -.
DR PDBsum; 7XF7; -.
DR PDBsum; 7XF8; -.
DR AlphaFoldDB; P61626; -.
DR BMRB; P61626; -.
DR SMR; P61626; -.
DR BioGRID; 110247; 101.
DR IntAct; P61626; 27.
DR MINT; P61626; -.
DR STRING; 9606.ENSP00000261267; -.
DR DrugBank; DB02159; (R)-Propylene glycol.
DR DrugBank; DB03487; (S)-Aspartimide.
DR DrugBank; DB02759; 4-methyl-umbelliferyl-N-acetyl-chitobiose.
DR DrugBank; DB03006; Arsanilic acid.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB03189; Cu-Cyclam.
DR DrugBank; DB03967; Dodecyl sulfate.
DR DrugBank; DB04268; Methylumbelliferyl chitotriose.
DR DrugBank; DB03013; N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosamine.
DR DrugBank; DB03120; p-Toluenesulfonic acid.
DR DrugBank; DB03175; Propyl alcohol.
DR DrugBank; DB11182; Rose bengal.
DR DrugBank; DB02772; Sucrose.
DR DrugBank; DB04194; Triacetylchitotriose.
DR DrugBank; DB06912; UNDECA-3,7-DIENE-1,3,7,11-TETRACARBALDEHYDE.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR iPTMnet; P61626; -.
DR PhosphoSitePlus; P61626; -.
DR BioMuta; LYZ; -.
DR DMDM; 48428995; -.
DR UCD-2DPAGE; P61626; -.
DR EPD; P61626; -.
DR jPOST; P61626; -.
DR MassIVE; P61626; -.
DR MaxQB; P61626; -.
DR PaxDb; P61626; -.
DR PeptideAtlas; P61626; -.
DR PRIDE; P61626; -.
DR ProteomicsDB; 57328; -.
DR TopDownProteomics; P61626; -.
DR ABCD; P61626; 12 sequenced antibodies.
DR Antibodypedia; 3512; 965 antibodies from 40 providers.
DR DNASU; 4069; -.
DR Ensembl; ENST00000261267.7; ENSP00000261267.2; ENSG00000090382.7.
DR GeneID; 4069; -.
DR KEGG; hsa:4069; -.
DR MANE-Select; ENST00000261267.7; ENSP00000261267.2; NM_000239.3; NP_000230.1.
DR UCSC; uc001suw.3; human.
DR CTD; 4069; -.
DR DisGeNET; 4069; -.
DR GeneCards; LYZ; -.
DR HGNC; HGNC:6740; LYZ.
DR HPA; ENSG00000090382; Tissue enhanced (bone marrow, salivary gland, stomach).
DR MalaCards; LYZ; -.
DR MIM; 105200; phenotype.
DR MIM; 153450; gene.
DR neXtProt; NX_P61626; -.
DR OpenTargets; ENSG00000090382; -.
DR Orphanet; 93561; ALys amyloidosis.
DR PharmGKB; PA30503; -.
DR VEuPathDB; HostDB:ENSG00000090382; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P61626; -.
DR OMA; WVAWKAH; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P61626; -.
DR TreeFam; TF324882; -.
DR BRENDA; 3.2.1.17; 2681.
DR PathwayCommons; P61626; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P61626; -.
DR SIGNOR; P61626; -.
DR BioGRID-ORCS; 4069; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; LYZ; human.
DR EvolutionaryTrace; P61626; -.
DR GeneWiki; Lysozyme; -.
DR GenomeRNAi; 4069; -.
DR Pharos; P61626; Tbio.
DR PRO; PR:P61626; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P61626; protein.
DR Bgee; ENSG00000090382; Expressed in monocyte and 183 other tissues.
DR ExpressionAtlas; P61626; baseline and differential.
DR Genevisible; P61626; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Amyloid; Amyloidosis; Antimicrobial; Bacteriolytic enzyme;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycosidase;
KW Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:11946553,
FT ECO:0000269|PubMed:11946554, ECO:0000269|PubMed:25946035,
FT ECO:0000269|PubMed:5168859, ECO:0000269|PubMed:5284421"
FT CHAIN 19..148
FT /note="Lysozyme C"
FT /id="PRO_0000018467"
FT DOMAIN 19..148
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT ACT_SITE 71
FT DISULFID 24..146
FT DISULFID 48..134
FT DISULFID 83..99
FT DISULFID 95..113
FT VARIANT 74
FT /note="I -> T (in AMYL8; dbSNP:rs121913547)"
FT /evidence="ECO:0000269|PubMed:8464497"
FT /id="VAR_004280"
FT VARIANT 85
FT /note="D -> H (in AMYL8; dbSNP:rs121913548)"
FT /evidence="ECO:0000269|PubMed:8464497"
FT /id="VAR_004281"
FT VARIANT 88
FT /note="T -> N (in dbSNP:rs1800973)"
FT /id="VAR_012050"
FT CONFLICT 10
FT /note="V -> A (in Ref. 5; AAC63078)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="I -> M (in Ref. 1; AAA36188)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="V -> A (in Ref. 5; AAC63078)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> V (in Ref. 5; AAC63078)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> A (in Ref. 5; AAC63078)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="N -> D (in Ref. 5; AAC63078)"
FT /evidence="ECO:0000305"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2NWD"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1BB3"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2NWD"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2NWD"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:2NWD"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7AP7"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2NWD"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2NWD"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1B7M"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2NWD"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:2NWD"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2NWD"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2NWD"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2NWD"
SQ SEQUENCE 148 AA; 16537 MW; 8ECFD276BEB2678A CRC64;
MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA
TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS ALLQDNIADA VACAKRVVRD
PQGIRAWVAW RNRCQNRDVR QYVQGCGV
