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 27-NOV-2024, entry version 199. 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 AMYLD5 THR-74 AND HIS-85, AND INVOLVEMENT IN AMYLD5. 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, hereditary systemic 5 (AMYLD5) [MIM:620658]: A CC form of hereditary systemic amyloidosis, a disorder characterized by CC amyloid deposition in multiple tissues resulting in a wide clinical CC spectrum. AMYLD5 primarily affects the viscera, and the predominant CC clinical features are renal dysfunction of varying severity, and intra- CC abdominal bleeding. Inheritance is autosomal dominant. 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; 132. DR IntAct; P61626; 55. 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 GlyGen; P61626; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61626; -. DR PhosphoSitePlus; P61626; -. DR SwissPalm; P61626; -. DR BioMuta; LYZ; -. DR DMDM; 48428995; -. DR jPOST; P61626; -. DR MassIVE; P61626; -. DR PaxDb; 9606-ENSP00000261267; -. DR PeptideAtlas; P61626; -. DR PRIDE; P61626; -. DR ProteomicsDB; 57328; -. DR TopDownProteomics; P61626; -. DR ABCD; P61626; 12 sequenced antibodies. DR Antibodypedia; 3512; 968 antibodies from 42 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 AGR; HGNC:6740; -. 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; 153450; gene. DR MIM; 620658; phenotype. 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; NACNIKC; -. DR OrthoDB; 5344399at2759; -. 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; 19 hits in 1171 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 185 other cell types or tissues. DR ExpressionAtlas; P61626; baseline and differential. 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: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 CDD; cd16897; LYZ_C; 1. DR FunFam; 1.10.530.10:FF:000001; Lysozyme C; 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:SF28; 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 1: Evidence at protein level; KW 3D-structure; Amyloid; Amyloidosis; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycosidase; KW Hydrolase; Proteomics identification; 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 AMYLD5; dbSNP:rs121913547)" FT /evidence="ECO:0000269|PubMed:8464497" FT /id="VAR_004280" FT VARIANT 85 FT /note="D -> H (in AMYLD5; 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 //