ID   B2R4C5_HUMAN            Unreviewed;       148 AA.
AC   B2R4C5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Lysozyme C {ECO:0000256|ARBA:ARBA00016457};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
DE   AltName: Full=1,4-beta-N-acetylmuramidase C {ECO:0000256|ARBA:ARBA00032459};
GN   Name=LYZ {ECO:0000313|EMBL:ACO37637.1};
GN   Synonyms=LYZF1 {ECO:0000313|EMBL:CDM98740.1};
GN   ORFNames=hCG_24462 {ECO:0000313|EMBL:EAW97220.1};
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 {ECO:0000313|EMBL:BAG34722.1};
RN   [1] {ECO:0000313|EMBL:EAW97220.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW97220.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAG34722.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung {ECO:0000313|EMBL:BAG34722.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ACO37637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:ACO37637.1};
RA   Guan W.J., Ma Y.H., Yu L.L.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CDM98740.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26484105; DOI=10.1016/j.gdata.2014.08.003;
RA   Premzl M.;
RT   "Third party annotation gene data set of eutherian lysozyme genes.";
RL   Genom Data 2:258-260(2014).
RN   [6] {ECO:0000313|EMBL:AIL02126.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nath B., Kaushik R., Babu K.R., Singh K.P., Joshi M.K., Manik R.S.,
RA   Palta P., Singla S.K., Chauhan M.S., Singh M.K.;
RT   "Molecular cloning of human lysozyme and its expression in buffalo mammary
RT   epithelial cells.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:CDM98740.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26862561; DOI=10.1016/j.dib.2015.11.056;
RA   Premzl M.;
RT   "Curated eutherian third party data gene data sets.";
RL   Data Brief 6:208-213(2016).
RN   [8] {ECO:0000313|EMBL:CDM98740.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1016/j.genrep.2019.100414;
RA   Premzl M.;
RT   "Eutherian third-party data gene collections.";
RL   Gene Rep 16:100414-100414(2019).
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; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000256|RuleBase:RU004440}.
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DR   EMBL; FJ795023; ACO37637.1; -; mRNA.
DR   EMBL; KJ841928; AIL02126.1; -; mRNA.
DR   EMBL; AK311779; BAG34722.1; -; mRNA.
DR   EMBL; HG931739; CDM98740.1; -; Genomic_DNA.
DR   EMBL; CH471054; EAW97220.1; -; Genomic_DNA.
DR   RefSeq; NP_000230.1; NM_000239.2.
DR   SMR; B2R4C5; -.
DR   IntAct; B2R4C5; 1.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Antibodypedia; 3512; 1078 antibodies from 40 providers.
DR   DNASU; 4069; -.
DR   GeneID; 4069; -.
DR   KEGG; hsa:4069; -.
DR   CTD; 4069; -.
DR   PharmGKB; PA30503; -.
DR   VEuPathDB; HostDB:ENSG00000090382; -.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   OMA; NACNIKC; -.
DR   OrthoDB; 5344399at2759; -.
DR   BioGRID-ORCS; 4069; 19 hits in 1171 CRISPR screens.
DR   ChiTaRS; LYZ; human.
DR   GenomeRNAi; 4069; -.
DR   ExpressionAtlas; B2R4C5; baseline and differential.
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; cd16897; LYZ_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   2: Evidence at transcript level;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ACO37637.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACO37637.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..148
FT                   /note="Lysozyme C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014298326"
FT   DOMAIN          95..113
FT                   /note="Glycosyl hydrolases family 22 (GH22)"
FT                   /evidence="ECO:0000259|PROSITE:PS00128"
SQ   SEQUENCE   148 AA;  16537 MW;  8ECFD276BEB2678A CRC64;
     MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA
     TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS ALLQDNIADA VACAKRVVRD
     PQGIRAWVAW RNRCQNRDVR QYVQGCGV
//