LYSP_DROME
ID LYSP_DROME Reviewed; 141 AA.
AC P29615; A0JQ50; Q4V3V7; Q9W0J4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Lysozyme P;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase P;
DE Flags: Precursor;
GN Name=LysP; ORFNames=CG9116;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=1588905; DOI=10.1007/bf00266235;
RA Kylsten P., Kimbrell D.A., Daffre S., Samakovlis C., Hultmark D.;
RT "The lysozyme locus in Drosophila melanogaster: different genes are
RT expressed in midgut and salivary glands.";
RL Mol. Gen. Genet. 232:335-343(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2006) 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 {ECO:0000269|PubMed:1588905, ECO:0000269|PubMed:8159165}.
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: Salivary gland. {ECO:0000269|PubMed:1588905,
CC ECO:0000269|PubMed:8159165}.
CC -!- DEVELOPMENTAL STAGE: Only expressed in adults.
CC {ECO:0000269|PubMed:1588905, ECO:0000269|PubMed:8159165}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK57077.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X58383; CAA41273.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47452.1; -; Genomic_DNA.
DR EMBL; BT023249; AAY55665.1; -; mRNA.
DR EMBL; BT029420; ABK57077.1; ALT_INIT; mRNA.
DR PIR; S20915; S20915.
DR RefSeq; NP_476828.1; NM_057480.5.
DR AlphaFoldDB; P29615; -.
DR SMR; P29615; -.
DR IntAct; P29615; 1.
DR STRING; 7227.FBpp0072529; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P29615; -.
DR DNASU; 38129; -.
DR EnsemblMetazoa; FBtr0072633; FBpp0072529; FBgn0004429.
DR GeneID; 38129; -.
DR KEGG; dme:Dmel_CG9116; -.
DR CTD; 38129; -.
DR FlyBase; FBgn0004429; LysP.
DR VEuPathDB; VectorBase:FBgn0004429; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000166760; -.
DR HOGENOM; CLU_111620_2_1_1; -.
DR InParanoid; P29615; -.
DR OMA; CHIKCED; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P29615; -.
DR Reactome; R-DME-5653890; Lactose synthesis.
DR SignaLink; P29615; -.
DR BioGRID-ORCS; 38129; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38129; -.
DR PRO; PR:P29615; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004429; Expressed in saliva-secreting gland and 12 other tissues.
DR ExpressionAtlas; P29615; baseline and differential.
DR Genevisible; P29615; DM.
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; ISS:FlyBase.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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:0000255"
FT CHAIN 19..141
FT /note="Lysozyme P"
FT /id="PRO_0000018514"
FT DOMAIN 20..141
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 25..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 46..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 81..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 93..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 141 AA; 15648 MW; 4D7C51B018FD5417 CRC64;
MKAFLVICAL TLTAVATQAR TMDRCSLARE MSKLGVPRDQ LAKWTCIAQH ESSFRTGVVG
PANSNGSNDY GIFQINNKYW CKPADGRFSY NECGLSCNAL LTDDITNSVK CARKIQRQQG
WTAWSTWKYC SGSLPSINSC F
