LYSE_DROME
ID LYSE_DROME Reviewed; 140 AA.
AC P37159; C9QP86; Q8MS67; Q9W0J5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Lysozyme E;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase E;
DE Flags: Precursor;
GN Name=LysE; ORFNames=CG1180;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=8159165; DOI=10.1007/bf00391008;
RA Daffre S., Kylsten P., Samakovlis C., Hultmark D.;
RT "The lysozyme locus in Drosophila melanogaster: an expanded gene family
RT adapted for expression in the digestive tract.";
RL Mol. Gen. Genet. 242:152-162(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Sandler J., Wan K.H., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Unlikely to play an active role in the humoral immune
CC defense. May have a function in the digestion of bacteria in the food.
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 -!- TISSUE SPECIFICITY: Found in the midgut.
CC -!- DEVELOPMENTAL STAGE: Maximal expression is found during the third
CC larval instar, it drops to become undetectable in the late pupal stage.
CC The expression in adults is similar to that of first and second larval
CC instars.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; Z22227; CAA80229.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47451.1; -; Genomic_DNA.
DR EMBL; AY119059; AAM50919.1; -; mRNA.
DR EMBL; BT099968; ACX53649.1; -; mRNA.
DR PIR; S41577; S41577.
DR RefSeq; NP_476827.2; NM_057479.3.
DR AlphaFoldDB; P37159; -.
DR SMR; P37159; -.
DR BioGRID; 63674; 1.
DR DIP; DIP-20170N; -.
DR STRING; 7227.FBpp0072526; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P37159; -.
DR DNASU; 38128; -.
DR EnsemblMetazoa; FBtr0072630; FBpp0072526; FBgn0004428.
DR GeneID; 38128; -.
DR KEGG; dme:Dmel_CG1180; -.
DR CTD; 38128; -.
DR FlyBase; FBgn0004428; LysE.
DR VEuPathDB; VectorBase:FBgn0004428; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000166760; -.
DR HOGENOM; CLU_111620_2_1_1; -.
DR InParanoid; P37159; -.
DR OMA; HWLCLAF; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P37159; -.
DR Reactome; R-DME-5653890; Lactose synthesis.
DR BioGRID-ORCS; 38128; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38128; -.
DR PRO; PR:P37159; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004428; Expressed in midgut and 11 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:FlyBase.
DR GO; GO:0003796; F:lysozyme activity; ISS:FlyBase.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
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; PTHR11407; 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 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..140
FT /note="Lysozyme E"
FT /id="PRO_0000018513"
FT DOMAIN 19..140
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 45..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 80..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 92..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CONFLICT 12
FT /note="M -> L (in Ref. 1; CAA80229)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="N -> D (in Ref. 1; CAA80229)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="G -> D (in Ref. 1; CAA80229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 15553 MW; CEB5465CF6B6F123 CRC64;
MKAFIVLVAL AMAAPALGRT LDRCSLAREM SNLGVPRDQL ARWACIAEHE SSYRTGVVGP
ENYNGSNDYG IFQINNYYWC APPSGRFSYN ECGLSCNALL TDDITHSVRC AQKVLSQQGW
SAWSTWHYCS GWLPSIDGCF
