DSO1_DROME
ID DSO1_DROME Reviewed; 42 AA.
AC P82705; A0A0B4LG54; Q9W2Q9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Daisho1 {ECO:0000303|PubMed:32038657};
DE AltName: Full=Immune-induced peptide 4 {ECO:0000303|PubMed:12171930};
DE Short=DIM-4 {ECO:0000303|PubMed:12171930};
DE Flags: Precursor;
GN Name=Dso1 {ECO:0000303|PubMed:32038657, ECO:0000312|FlyBase:FBgn0040653};
GN Synonyms=IM4 {ECO:0000312|FlyBase:FBgn0040653};
GN ORFNames=CG15231 {ECO:0000312|FlyBase:FBgn0040653};
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 [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 [2]
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 [3]
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 [4] {ECO:0000312|EMBL:ANY27690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 27-41, AMIDATION AT THR-41, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION BY BACTERIA, 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 [6]
RP PROTEIN SEQUENCE OF 27-41, AND AMIDATION AT THR-41.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hemolymph {ECO:0000303|PubMed:16510152};
RX PubMed=16510152; DOI=10.1016/j.jinsphys.2005.12.007;
RA Verleyen P., Baggerman G., D'Hertog W., Vierstraete E., Husson S.J.,
RA Schoofs L.;
RT "Identification of new immune induced molecules in the haemolymph of
RT Drosophila melanogaster by 2D-nanoLC MS/MS.";
RL J. Insect Physiol. 52:379-388(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA,
RP MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=32038657; DOI=10.3389/fimmu.2020.00009;
RA Cohen L.B., Lindsay S.A., Xu Y., Lin S.J.H., Wasserman S.A.;
RT "The Daisho Peptides Mediate Drosophila Defense Against a Subset of
RT Filamentous Fungi.";
RL Front. Immunol. 11:9-9(2020).
CC -!- FUNCTION: Peptide which plays a role in the humoral immune response to
CC a subset of filamentous fungi, including F.oxysporum and
CC F.verticillioides. {ECO:0000269|PubMed:32038657}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16510152,
CC ECO:0000269|PubMed:32038657, ECO:0000269|PubMed:9736738}.
CC -!- TISSUE SPECIFICITY: Hemolymph (at protein level).
CC {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:32038657,
CC ECO:0000269|PubMed:9736738}.
CC -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738,
CC PubMed:32038657). Induced by Gram-positive bacteria M.luteus (at
CC protein level) (PubMed:32038657). However, another study found the
CC peptide was present in both immune challenged and unchallenged controls
CC (at protein level) (PubMed:16510152). {ECO:0000269|PubMed:16510152,
CC ECO:0000269|PubMed:32038657, ECO:0000269|PubMed:9736738}.
CC -!- MASS SPECTROMETRY: Mass=1720.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9736738};
CC -!- MASS SPECTROMETRY: Mass=1722; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:32038657};
CC -!- MASS SPECTROMETRY: Mass=1720.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16510152};
CC -!- DISRUPTION PHENOTYPE: Adult males infected with spores from F.oxysporum
CC or F.verticillioides display reduced survival.
CC {ECO:0000269|PubMed:32038657}.
CC -!- MISCELLANEOUS: 'Daisho' is the Japanese term for a matched pair of
CC samurai swords, one short and one long, and refers to the role of the
CC two Daisho peptides (Dso1 and Dso2) in defense against fungal
CC infection. {ECO:0000303|PubMed:32038657}.
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DR EMBL; AE013599; AAF46631.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56443.1; -; Genomic_DNA.
DR EMBL; AY070691; AAL48162.1; -; mRNA.
DR EMBL; KX531880; ANY27690.1; -; mRNA.
DR RefSeq; NP_001286648.1; NM_001299719.1.
DR RefSeq; NP_652295.1; NM_144038.3.
DR AlphaFoldDB; P82705; -.
DR BioGRID; 72555; 3.
DR DIP; DIP-21088N; -.
DR IntAct; P82705; 1.
DR STRING; 7227.FBpp0071487; -.
DR PaxDb; P82705; -.
DR DNASU; 50126; -.
DR EnsemblMetazoa; FBtr0071559; FBpp0071487; FBgn0040653.
DR EnsemblMetazoa; FBtr0345819; FBpp0311805; FBgn0040653.
DR GeneID; 50126; -.
DR KEGG; dme:Dmel_CG15231; -.
DR CTD; 492981; -.
DR FlyBase; FBgn0040653; Dso1.
DR VEuPathDB; VectorBase:FBgn0040653; -.
DR eggNOG; ENOG502R3CT; Eukaryota.
DR HOGENOM; CLU_3261061_0_0_1; -.
DR InParanoid; P82705; -.
DR PhylomeDB; P82705; -.
DR BioGRID-ORCS; 50126; 0 hits in 1 CRISPR screen.
DR ChiTaRS; IM4; fly.
DR GenomeRNAi; 50126; -.
DR PRO; PR:P82705; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0040653; Expressed in seminal fluid secreting gland and 21 other tissues.
DR ExpressionAtlas; P82705; baseline and differential.
DR Genevisible; P82705; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IEP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; HEP:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..26
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:9736738"
FT /id="PRO_0000021494"
FT PEPTIDE 27..41
FT /note="Daisho1"
FT /id="PRO_0000021495"
FT MOD_RES 41
FT /note="Threonine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:9736738"
SQ SEQUENCE 42 AA; 4523 MW; BDB1A618BD251003 CRC64;
MKFFQAAALL LAMFAALANA EPVPQPGTVL IQTDNTQYIR TG
