DMYC_DROME
ID DMYC_DROME Reviewed; 70 AA.
AC P41964; Q2UYN5; Q9VZQ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Drosomycin;
DE AltName: Full=Cysteine-rich peptide;
DE Flags: Precursor;
GN Name=Drs; Synonyms=CRP; ORFNames=CG10810;
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 [MRNA], PROTEIN SEQUENCE OF 27-70, AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=7806546; DOI=10.1016/s0021-9258(20)30111-3;
RA Fehlbaum P., Bulet P., Michaut L., Lagueux M., Broekaert W.F., Hetru C.,
RA Hoffmann J.A.;
RT "Insect immunity. Septic injury of Drosophila induces the synthesis of a
RT potent antifungal peptide with sequence homology to plant antifungal
RT peptides.";
RL J. Biol. Chem. 269:33159-33163(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G125, G128, G130, G140, G141, G179, G185, G187, KY258, N01, N02,
RC N03, N06, N07, N14, N15, N16, N17, N22, N29, and N30;
RX PubMed=16157672; DOI=10.1534/genetics.105.045435;
RA Jiggins F.M., Kim K.W.;
RT "The evolution of antifungal peptides in Drosophila.";
RL Genetics 171:1847-1859(2005).
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; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=8808632; DOI=10.1016/s0092-8674(00)80172-5;
RA Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.;
RT "The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the
RT potent antifungal response in Drosophila adults.";
RL Cell 86:973-983(1996).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R {ECO:0000303|PubMed:9736738};
RC TISSUE=Hemolymph {ECO:0000303|PubMed:9736738};
RX PubMed=9736738; DOI=10.1073/pnas.95.19.11342;
RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A.,
RA Hoffmann J.A., Bulet P.;
RT "Differential display of peptides induced during the immune response of
RT Drosophila: a matrix-assisted laser desorption ionization time-of-flight
RT mass spectrometry study.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998).
RN [8]
RP FUNCTION.
RX PubMed=12872120; DOI=10.1038/ni955;
RA Weber A.N., Tauszig-Delamasure S., Hoffmann J.A., Lelievre E., Gascan H.,
RA Ray K.P., Morse M.A., Imler J.L., Gay N.J.;
RT "Binding of the Drosophila cytokine Spatzle to Toll is direct and
RT establishes signaling.";
RL Nat. Immunol. 4:794-800(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION BY BACTERIA.
RX PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
RA Akhouayri I., Turc C., Royet J., Charroux B.;
RT "Toll-8/Tollo negatively regulates antimicrobial response in the Drosophila
RT respiratory epithelium.";
RL PLoS Pathog. 7:E1002319-E1002319(2011).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=9300487; DOI=10.1002/pro.5560060908;
RA Landon C., Sodano P., Hetru C., Hoffmann J.A., Ptak M.;
RT "Solution structure of drosomycin, the first inducible antifungal protein
RT from insects.";
RL Protein Sci. 6:1878-1884(1997).
RN [11]
RP FUNCTION, AND INDUCTION BY MELANIZATION.
RX PubMed=18854145; DOI=10.1016/j.devcel.2008.08.017;
RA Tang H., Kambris Z., Lemaitre B., Hashimoto C.;
RT "A serpin that regulates immune melanization in the respiratory system of
RT Drosophila.";
RL Dev. Cell 15:617-626(2008).
RN [12]
RP INDUCTION BY GRAM-POSITIVE BACTERIA AND FUNGI.
RX PubMed=19590012; DOI=10.1073/pnas.0901924106;
RA Buchon N., Poidevin M., Kwon H.M., Guillou A., Sottas V., Lee B.L.,
RA Lemaitre B.;
RT "A single modular serine protease integrates signals from pattern-
RT recognition receptors upstream of the Drosophila Toll pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12442-12447(2009).
CC -!- FUNCTION: Possesses antifungal activity and is active against a
CC relatively broad spectrum of filamentous fungi (PubMed:8808632,
CC PubMed:12872120). It inhibits spore germination at high concentrations
CC and at low concentrations delays growth of hyphae which subsequently
CC exhibit abnormal morphology (PubMed:7806546). Spz C-106 in the
CC hemolymph controls expression of the antifungal peptide by acting as a
CC ligand of Tl and inducing an intracellular signaling pathway
CC (PubMed:8808632). Part of a psh-dependent Toll pathway, which may
CC function in activating the systematic immune response in response to
CC localized melanization of the tracheal system (PubMed:18854145).
CC {ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:18854145,
CC ECO:0000269|PubMed:7806546, ECO:0000269|PubMed:8808632}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9736738}.
CC -!- TISSUE SPECIFICITY: Hemolymph (at protein level) (PubMed:9736738).
CC Synthesized in the fat body and is secreted into the blood
CC (PubMed:9736738). In larvae, expressed in the visceral branches and
CC posterior spiracles of the trachea (PubMed:22022271).
CC {ECO:0000269|PubMed:22022271, ECO:0000269|PubMed:9736738}.
CC -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738).
CC In hemolymph 6 hours after bacterial infection, levels of expression
CC increase for first 24 hours and persist for the following three weeks
CC (at protein level) (PubMed:9736738). Up-regulated by septic injury
CC caused by the Gram-positive bacterium M.luteus and the fungus
CC C.albicans, and by M.luteus or E.faecalis-derived peptidoglycans and by
CC B.subtilis or A.oryzae proteases (PubMed:19590012). Up-regulated by
CC Gram-negative bacteria in the respiratory epithelium (PubMed:22022271).
CC Up-regulated in the trachea and fat body in response to tracheal
CC melanization, either by spontaneous melanization or melanization
CC resulting from infection by bacteria (E.coli and M.luteus) or the
CC fungus B.bassiana (PubMed:18854145). {ECO:0000269|PubMed:18854145,
CC ECO:0000269|PubMed:19590012, ECO:0000269|PubMed:22022271,
CC ECO:0000269|PubMed:9736738}.
CC -!- MASS SPECTROMETRY: Mass=4889.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9736738};
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DR EMBL; X75595; CAA53267.1; -; mRNA.
DR EMBL; AJ885056; CAI76995.1; -; Genomic_DNA.
DR EMBL; AJ885057; CAI77002.1; -; Genomic_DNA.
DR EMBL; AJ885058; CAI77009.1; -; Genomic_DNA.
DR EMBL; AJ885059; CAI77016.1; -; Genomic_DNA.
DR EMBL; AJ885060; CAI77023.1; -; Genomic_DNA.
DR EMBL; AJ885061; CAI77030.1; -; Genomic_DNA.
DR EMBL; AJ885062; CAI77037.1; -; Genomic_DNA.
DR EMBL; AJ885063; CAI77044.1; -; Genomic_DNA.
DR EMBL; AJ885064; CAI77051.1; -; Genomic_DNA.
DR EMBL; AJ885065; CAI77058.1; -; Genomic_DNA.
DR EMBL; AJ885066; CAI77065.1; -; Genomic_DNA.
DR EMBL; AJ885067; CAI77072.1; -; Genomic_DNA.
DR EMBL; AJ885068; CAI77079.1; -; Genomic_DNA.
DR EMBL; AJ885069; CAI77086.1; -; Genomic_DNA.
DR EMBL; AJ885070; CAI77093.1; -; Genomic_DNA.
DR EMBL; AJ885071; CAI77100.1; -; Genomic_DNA.
DR EMBL; AJ885072; CAI77107.1; -; Genomic_DNA.
DR EMBL; AJ885073; CAI77114.1; -; Genomic_DNA.
DR EMBL; AJ885074; CAI77121.1; -; Genomic_DNA.
DR EMBL; AJ885075; CAI77128.1; -; Genomic_DNA.
DR EMBL; AJ885086; CAI77205.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47767.2; -; Genomic_DNA.
DR EMBL; AY119009; AAM50869.1; -; mRNA.
DR PIR; A55824; A55824.
DR RefSeq; NP_523901.1; NM_079177.4.
DR PDB; 1MYN; NMR; -; A=27-70.
DR PDBsum; 1MYN; -.
DR AlphaFoldDB; P41964; -.
DR SMR; P41964; -.
DR DIP; DIP-18879N; -.
DR IntAct; P41964; 3.
DR STRING; 7227.FBpp0072935; -.
DR TCDB; 8.B.1.1.9; the long (4c-c) scorpion toxin (l-st) superfamily.
DR PaxDb; P41964; -.
DR DNASU; 38419; -.
DR EnsemblMetazoa; FBtr0073073; FBpp0072935; FBgn0283461.
DR GeneID; 38419; -.
DR KEGG; dme:Dmel_CG10810; -.
DR CTD; 38419; -.
DR FlyBase; FBgn0283461; Drs.
DR VEuPathDB; VectorBase:FBgn0283461; -.
DR GeneTree; ENSGT00940000176294; -.
DR HOGENOM; CLU_2760455_0_0_1; -.
DR InParanoid; P41964; -.
DR OrthoDB; 1570019at2759; -.
DR PhylomeDB; P41964; -.
DR BioGRID-ORCS; 38419; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; P41964; -.
DR GenomeRNAi; 38419; -.
DR PRO; PR:P41964; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0283461; Expressed in spermathecum and 26 other tissues.
DR ExpressionAtlas; P41964; baseline and differential.
DR Genevisible; P41964; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0019731; P:antibacterial humoral response; TAS:FlyBase.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IDA:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:FlyBase.
DR GO; GO:0042832; P:defense response to protozoan; IDA:FlyBase.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
DR GO; GO:0009611; P:response to wounding; IEP:FlyBase.
DR CDD; cd00107; Knot1; 1.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..26
FT /evidence="ECO:0000269|PubMed:7806546"
FT /id="PRO_0000007038"
FT CHAIN 27..70
FT /note="Drosomycin"
FT /id="PRO_0000007039"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..70
FT DISULFID 37..59
FT DISULFID 45..65
FT DISULFID 49..67
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1MYN"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1MYN"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1MYN"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1MYN"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1MYN"
SQ SEQUENCE 70 AA; 7752 MW; 1A702E959ECEF181 CRC64;
MMQIKYLFAL FAVLMLVVLG ANEADADCLS GRYKGPCAVW DNETCRRVCK EEGRSSGHCS
PSLKCWCEGC
