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 01-MAY-2013, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Saccharomyces 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
RT in 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
RT cDNA 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
RT project: 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;
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
RT the complete primary structure; comparison with lysozymes of various
RT 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 FOLDING, AND MUTAGENESIS.
RX PubMed=8503881;
RA Kanaya E., Ishihara K., Tsunasawa S., Nokihara K., Kikuchi M.;
RT "Indication of possible post-translational formation of disulphide
RT bonds in the beta-sheet domain of human lysozyme.";
RL Biochem. J. 292:469-476(1993).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
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 [14]
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-
RT bonded and hydrogen-bond interactions.";
RL J. Mol. Biol. 152:737-762(1981).
RN [15]
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-99 AND ALA-113.
RX PubMed=2061330;
RA Inaka K., Taniyama Y., Kikuchi M., Morikawa K., Matsushima M.;
RT "The crystal structure of a mutant human lysozyme C77/95A with
RT increased secretion efficiency in yeast.";
RL J. Biol. Chem. 266:12599-12603(1991).
RN [17]
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 [18]
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
RT with hen lysozyme.";
RL Biochemistry 29:7201-7214(1990).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=1794972;
RA Ohkubo T., Taniyama Y., Kikuchi M.;
RT "1H and 15N NMR study of human lysozyme.";
RL J. Biochem. 110:1022-1029(1991).
RN [20]
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.,
RA Feest T.G., Zalin A.M., Hsuan J.J.;
RT "Human lysozyme gene mutations cause hereditary systemic
RT amyloidosis.";
RL Nature 362:553-557(1993).
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC in tissues and body fluids are associated with the monocyte-
CC macrophage system and enhance the activity of immunoagents.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC peptidoglycan and between N-acetyl-D-glucosamine residues in
CC chitodextrins.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary
CC generalized amyloidosis due to deposition of apolipoprotein A1,
CC fibrinogen and lysozyme amyloids. Viscera are particularly
CC affected. There is no involvement of the nervous system. Clinical
CC features include renal amyloidosis resulting in nephrotic
CC syndrome, arterial hypertension, hepatosplenomegaly, cholestasis,
CC petechial skin rash. Note=The disease is caused by mutations
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
CC acts rapidly on both peptide-substituted and unsubstituted
CC peptidoglycan, and slowly on chitin oligosaccharides.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32175.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/LYZ";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lysozyme entry;
CC URL="http://en.wikipedia.org/wiki/Lysozyme";
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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 IPI; IPI00019038; -.
DR PIR; S04938; LZHU.
DR RefSeq; NP_000230.1; NM_000239.2.
DR UniGene; Hs.524579; -.
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=20-148.
DR PDB; 1C45; X-ray; 1.80 A; A=20-148.
DR PDB; 1C46; X-ray; 2.20 A; A=18-148.
DR PDB; 1C7P; X-ray; 2.40 A; A=19-148.
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=21-148.
DR PDB; 1GAZ; X-ray; 1.80 A; A=21-148.
DR PDB; 1GB0; X-ray; 1.80 A; A=21-148.
DR PDB; 1GB2; X-ray; 1.80 A; A=21-148.
DR PDB; 1GB3; X-ray; 1.80 A; A=21-148.
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=21-148.
DR PDB; 1GF9; X-ray; 1.80 A; A=21-148.
DR PDB; 1GFA; X-ray; 1.80 A; A=21-148.
DR PDB; 1GFE; X-ray; 1.80 A; A=21-148.
DR PDB; 1GFG; X-ray; 1.80 A; A=21-148.
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=19-148.
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=21-148.
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=21-148.
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 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 ProteinModelPortal; P61626; -.
DR IntAct; P61626; 6.
DR MINT; MINT-5002660; -.
DR STRING; 9606.ENSP00000261267; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PhosphoSite; P61626; -.
DR DMDM; 48428995; -.
DR UCD-2DPAGE; P61626; -.
DR PaxDb; P61626; -.
DR PeptideAtlas; P61626; -.
DR PRIDE; P61626; -.
DR DNASU; 4069; -.
DR Ensembl; ENST00000261267; ENSP00000261267; ENSG00000090382.
DR GeneID; 4069; -.
DR KEGG; hsa:4069; -.
DR UCSC; uc001suw.2; human.
DR CTD; 4069; -.
DR GeneCards; GC12P069681; -.
DR HGNC; HGNC:6740; LYZ.
DR HPA; CAB000055; -.
DR MIM; 105200; phenotype.
DR MIM; 153450; gene.
DR neXtProt; NX_P61626; -.
DR Orphanet; 93561; Familial renal amyloidosis due to lysozyme variant.
DR PharmGKB; PA30503; -.
DR eggNOG; NOG85133; -.
DR HOGENOM; HOG000037357; -.
DR HOVERGEN; HBG052297; -.
DR InParanoid; P61626; -.
DR KO; K13915; -.
DR OMA; CNALLQD; -.
DR OrthoDB; EOG48KRCP; -.
DR PhylomeDB; P61626; -.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; LYZ; human.
DR EvolutionaryTrace; P61626; -.
DR GenomeRNAi; 4069; -.
DR NextBio; 15952; -.
DR ArrayExpress; P61626; -.
DR Bgee; P61626; -.
DR CleanEx; HS_LYZ; -.
DR Genevestigator; P61626; -.
DR GermOnline; ENSG00000090382; Homo sapiens.
DR GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; TAS:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; TAS: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.
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; LACTALBUMIN_LYSOZYME_1; 1.
DR PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; Amyloidosis; Antimicrobial;
KW Bacteriolytic enzyme; Complete proteome; Direct protein sequencing;
KW Disease mutation; Disulfide bond; Glycosidase; Hydrolase;
KW Polymorphism; Reference proteome; Secreted; Signal.
FT SIGNAL 1 18
FT CHAIN 19 148 Lysozyme C.
FT /FTId=PRO_0000018467.
FT ACT_SITE 53 53
FT ACT_SITE 71 71
FT DISULFID 24 146
FT DISULFID 48 134
FT DISULFID 83 99
FT DISULFID 95 113
FT VARIANT 74 74 I -> T (in AMYL8).
FT /FTId=VAR_004280.
FT VARIANT 85 85 D -> H (in AMYL8).
FT /FTId=VAR_004281.
FT VARIANT 88 88 T -> N (in dbSNP:rs1800973).
FT /FTId=VAR_012050.
FT CONFLICT 10 10 V -> A (in Ref. 5; AAC63078).
FT CONFLICT 41 41 I -> M (in Ref. 1; AAA36188).
FT CONFLICT 111 111 V -> A (in Ref. 5; AAC63078).
FT CONFLICT 124 124 I -> V (in Ref. 5; AAC63078).
FT CONFLICT 128 128 V -> A (in Ref. 5; AAC63078).
FT CONFLICT 136 136 N -> D (in Ref. 5; AAC63078).
FT HELIX 23 32
FT HELIX 38 40
FT HELIX 43 54
FT STRAND 55 57
FT STRAND 61 63
FT TURN 65 67
FT STRAND 70 72
FT TURN 73 76
FT TURN 79 81
FT STRAND 82 84
FT STRAND 88 90
FT HELIX 99 103
FT STRAND 104 106
FT HELIX 108 119
FT STRAND 120 122
FT HELIX 123 126
FT HELIX 128 133
FT TURN 134 136
FT HELIX 140 142
FT TURN 143 145
SQ SEQUENCE 148 AA; 16537 MW; 8ECFD276BEB2678A CRC64;
MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA
TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS ALLQDNIADA VACAKRVVRD
PQGIRAWVAW RNRCQNRDVR QYVQGCGV
//
