DROS_DROME
ID DROS_DROME Reviewed; 64 AA.
AC P36193; Q53ZZ5; Q867T5; Q86BV9; Q9V749;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Drosocin;
DE Flags: Precursor;
GN Name=Dro; ORFNames=CG10816;
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], PROTEIN SEQUENCE OF 22-40, VARIANT
RP ALA-52, AND GLYCOSYLATION AT THR-32.
RC STRAIN=Oregon-R;
RX PubMed=8325867; DOI=10.1016/s0021-9258(18)82417-6;
RA Bulet P., Dimarcq J.-L., Hetru C., Lagueux M., Charlet M., Hegy G.,
RA van Dorsselaer A., Hoffmann J.A.;
RT "A novel inducible antibacterial peptide of Drosophila carries an O-
RT glycosylated substitution.";
RL J. Biol. Chem. 268:14893-14897(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-52.
RC STRAIN=Oregon-R;
RX PubMed=8944755; DOI=10.1111/j.1432-1033.1996.00699.x;
RA Charlet M., Lagueux M., Reichhart J.-M., Hoffmann D., Braun A., Meister M.;
RT "Cloning of the gene encoding the antibacterial peptide drosocin involved
RT in Drosophila immunity. Expression studies during the immune response.";
RL Eur. J. Biochem. 241:699-706(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-52 AND VAL-64.
RC STRAIN=10B, 10C, 10D, 10F, 10G, 10H, 2CPA1, 2CPA103, 2CPA105, 2CPA118,
RC 2CPA12, 2CPA122, 2CPA129, 2CPA14, 2CPA43, 2CPA46, 2CPA51, 2CPA7, 8B, 8C,
RC 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, 9F, 9G, and 9H;
RX PubMed=12716986; DOI=10.1093/molbev/msg109;
RA Lazzaro B.P., Clark A.G.;
RT "Molecular population genetics of inducible antibacterial peptide genes in
RT Drosophila melanogaster.";
RL Mol. Biol. Evol. 20:914-923(2003).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [7]
RP SEQUENCE REVISION.
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA,
RP GLYCOSYLATION AT SER-28, AND MASS 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 [9]
RP STRUCTURE BY NMR, AND GLYCOSYLATION AT THR-32.
RX PubMed=9888811; DOI=10.1021/bi981956d;
RA McManus A.M., Otvos L. Jr., Hoffmann R., Craik D.J.;
RT "Conformational studies by NMR of the antimicrobial peptide, drosocin, and
RT its non-glycosylated derivative: effects of glycosylation on solution
RT conformation.";
RL Biochemistry 38:705-714(1999).
CC -!- FUNCTION: Antibacterial peptide with strong anti-Gram-negative bacteria
CC activity.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9736738}.
CC -!- TISSUE SPECIFICITY: Hemolymph (at protein level).
CC {ECO:0000269|PubMed:9736738}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and in adults.
CC -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738).
CC In hemolymph 6 hours after immune challenge, levels of expression
CC increase for first 24 hours and persist for the following two weeks (at
CC protein level) (PubMed:9736738). {ECO:0000269|PubMed:9736738}.
CC -!- PTM: O-glycosylated (PubMed:8325867, PubMed:9888811, PubMed:9736738).
CC O-glycosylation is essential for full biological activity
CC (PubMed:8325867). {ECO:0000269|PubMed:8325867,
CC ECO:0000269|PubMed:9736738, ECO:0000269|PubMed:9888811}.
CC -!- MASS SPECTROMETRY: Mass=2401.9; Method=MALDI; Note=With monosaccharide
CC on Thr-32.; Evidence={ECO:0000269|PubMed:9736738};
CC -!- MASS SPECTROMETRY: Mass=2564.4; Method=MALDI; Note=With disaccharide on
CC Ser-28 and Thr-32.; Evidence={ECO:0000269|PubMed:9736738};
CC -!- SIMILARITY: Belongs to the drosocin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29584.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z21942; CAA79936.1; -; Genomic_DNA.
DR EMBL; X98416; CAA67062.1; -; Genomic_DNA.
DR EMBL; AY224606; AAO72465.1; -; Genomic_DNA.
DR EMBL; AY224607; AAO72466.1; -; Genomic_DNA.
DR EMBL; AY224608; AAO72467.1; -; Genomic_DNA.
DR EMBL; AY224609; AAO72468.1; -; Genomic_DNA.
DR EMBL; AY224610; AAO72469.1; -; Genomic_DNA.
DR EMBL; AY224611; AAO72470.1; -; Genomic_DNA.
DR EMBL; AY224612; AAO72471.1; -; Genomic_DNA.
DR EMBL; AY224613; AAO72472.1; -; Genomic_DNA.
DR EMBL; AY224614; AAO72473.1; -; Genomic_DNA.
DR EMBL; AY224615; AAO72474.1; -; Genomic_DNA.
DR EMBL; AY224616; AAO72475.1; -; Genomic_DNA.
DR EMBL; AY224617; AAO72476.1; -; Genomic_DNA.
DR EMBL; AY224643; AAO72502.1; -; Genomic_DNA.
DR EMBL; AY224644; AAO72503.1; -; Genomic_DNA.
DR EMBL; AY224645; AAO72504.1; -; Genomic_DNA.
DR EMBL; AY224646; AAO72505.1; -; Genomic_DNA.
DR EMBL; AY224647; AAO72506.1; -; Genomic_DNA.
DR EMBL; AY224648; AAO72507.1; -; Genomic_DNA.
DR EMBL; AY224649; AAO72508.1; -; Genomic_DNA.
DR EMBL; AY224650; AAO72509.1; -; Genomic_DNA.
DR EMBL; AY224651; AAO72510.1; -; Genomic_DNA.
DR EMBL; AY224652; AAO72511.1; -; Genomic_DNA.
DR EMBL; AY224653; AAO72512.1; -; Genomic_DNA.
DR EMBL; AY224654; AAO72513.1; -; Genomic_DNA.
DR EMBL; AY224655; AAO72514.1; -; Genomic_DNA.
DR EMBL; AY224656; AAO72515.1; -; Genomic_DNA.
DR EMBL; AY224657; AAO72516.1; -; Genomic_DNA.
DR EMBL; AY224658; AAO72517.1; -; Genomic_DNA.
DR EMBL; AY224659; AAO72518.1; -; Genomic_DNA.
DR EMBL; AY224660; AAO72519.1; -; Genomic_DNA.
DR EMBL; AY224661; AAO72520.1; -; Genomic_DNA.
DR EMBL; AY224662; AAO72521.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58216.1; -; Genomic_DNA.
DR EMBL; AY113579; AAM29584.2; ALT_INIT; mRNA.
DR PIR; S35984; A47103.
DR RefSeq; NP_001246324.1; NM_001259395.2.
DR RefSeq; NP_523744.1; NM_079020.5.
DR PDB; 4EZR; X-ray; 1.90 A; B=33-40.
DR PDB; 6Z2P; X-ray; 2.16 A; C=22-40.
DR PDB; 6Z2Q; X-ray; 2.35 A; D=22-40.
DR PDBsum; 4EZR; -.
DR PDBsum; 6Z2P; -.
DR PDBsum; 6Z2Q; -.
DR AlphaFoldDB; P36193; -.
DR SMR; P36193; -.
DR STRING; 7227.FBpp0301076; -.
DR GlyGen; P36193; 2 sites.
DR iPTMnet; P36193; -.
DR PaxDb; P36193; -.
DR PRIDE; P36193; -.
DR DNASU; 36635; -.
DR EnsemblMetazoa; FBtr0087436; FBpp0086566; FBgn0010388.
DR EnsemblMetazoa; FBtr0309055; FBpp0301076; FBgn0010388.
DR GeneID; 36635; -.
DR KEGG; dme:Dmel_CG10816; -.
DR CTD; 36635; -.
DR FlyBase; FBgn0010388; Dro.
DR VEuPathDB; VectorBase:FBgn0010388; -.
DR HOGENOM; CLU_2869984_0_0_1; -.
DR InParanoid; P36193; -.
DR OMA; CVFAMAV; -.
DR OrthoDB; 1608809at2759; -.
DR PhylomeDB; P36193; -.
DR BioGRID-ORCS; 36635; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36635; -.
DR PRO; PR:P36193; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010388; Expressed in seminal fluid secreting gland and 15 other tissues.
DR ExpressionAtlas; P36193; baseline and differential.
DR Genevisible; P36193; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IEP:FlyBase.
DR GO; GO:0006952; P:defense response; IDA:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; TAS:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:FlyBase.
DR GO; GO:0002213; P:defense response to insect; IEP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Immunity; Innate immunity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..21
FT /evidence="ECO:0000269|PubMed:8325867"
FT /id="PRO_0000004958"
FT PEPTIDE 22..40
FT /note="Drosocin"
FT /id="PRO_0000004959"
FT PROPEP 43..64
FT /evidence="ECO:0000255"
FT /id="PRO_0000004960"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:9736738"
FT CARBOHYD 32
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8325867,
FT ECO:0000269|PubMed:9736738, ECO:0000269|PubMed:9888811"
FT VARIANT 52
FT /note="T -> A (in strain: 2CPA1, 2CPA12, 2CPA51, 2CPA105,
FT 2CPA118, 2CPA122, 8B, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E,
FT 9F, 9G, 9H, 10B, 10F, 10G, 10H and Oregon-R)"
FT /evidence="ECO:0000269|PubMed:12716986,
FT ECO:0000269|PubMed:8325867, ECO:0000269|PubMed:8944755"
FT VARIANT 64
FT /note="A -> V (in strain: 2CPA51)"
FT /evidence="ECO:0000269|PubMed:12716986"
FT CONFLICT 17
FT /note="G -> A (in Ref. 1; CAA79936, 2; CAA67062 and 3;
FT AAO72465/AAO72466/AAO72467/AAO72468/AAO72469/AAO72470/
FT AAO72471/AAO72472/AAO72473/AAO72474/AAO72475/AAO72476/
FT AAO72502/AAO72503/AAO72504/AAO72505/AAO72506/AAO72507/
FT AAO72508/AAO72509/AAO72510/AAO72511/AAO72512/AAO72513/
FT AAO72514/AAO72515/AAO72516/AAO72517/AAO72518/AAO72519/
FT AAO72520/AAO72521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 64 AA; 7085 MW; D715F5BA52FDAD17 CRC64;
MKFTIVFLLL ACVFAMGVAT PGKPRPYSPR PTSHPRPIRV RREALAIEDH LTQAAIRPPP
ILPA
