BM01_DROME
ID BM01_DROME Reviewed; 45 AA.
AC P82706; Q9V8F6;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Bomanin Short 1 {ECO:0000312|FlyBase:FBgn0034329};
DE AltName: Full=Bomanin-1 {ECO:0000303|PubMed:25915418};
DE AltName: Full=Immune-induced peptide 1 {ECO:0000312|FlyBase:FBgn0034329};
DE Short=DIM-1 {ECO:0000303|PubMed:25915418, ECO:0000312|FlyBase:FBgn0034329};
DE Flags: Precursor;
GN Name=BomS1 {ECO:0000312|FlyBase:FBgn0034329};
GN Synonyms=Bom1 {ECO:0000303|PubMed:25915418},
GN IM1 {ECO:0000312|FlyBase:FBgn0034329};
GN ORFNames=CG18108 {ECO:0000312|FlyBase:FBgn0034329};
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 PROTEIN SEQUENCE OF 28-43, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY BACTERIA, AMIDATION AT GLY-43, DISULFIDE BOND,
RP 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 [4]
RP FUNCTION.
RX PubMed=25915418; DOI=10.1371/journal.ppat.1004876;
RA Clemmons A.W., Lindsay S.A., Wasserman S.A.;
RT "An effector Peptide family required for Drosophila toll-mediated
RT immunity.";
RL PLoS Pathog. 11:E1004876-E1004876(2015).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP BACTERIA.
RX PubMed=29920489; DOI=10.1159/000489831;
RA Lindsay S.A., Lin S.J.H., Wasserman S.A.;
RT "Short-Form Bomanins Mediate Humoral Immunity in Drosophila.";
RL J. Innate Immun. 10:306-314(2018).
CC -!- FUNCTION: Secreted immune-induced peptide induced by Toll signaling
CC (PubMed:9736738, PubMed:25915418, PubMed:29920489). Has a role in
CC resistance to bacterial and fungal infections (PubMed:9736738,
CC PubMed:25915418, PubMed:29920489). Has no activity against the fungus
CC C.glabrata in vitro (PubMed:29920489). {ECO:0000269|PubMed:25915418,
CC ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29920489,
CC ECO:0000269|PubMed:9736738}.
CC -!- TISSUE SPECIFICITY: Hemolymph (at protein level).
CC {ECO:0000269|PubMed:29920489, ECO:0000269|PubMed:9736738}.
CC -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:29920489,
CC ECO:0000269|PubMed:9736738}.
CC -!- MASS SPECTROMETRY: Mass=1687.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9736738};
CC -!- SIMILARITY: Belongs to the bomanin family. {ECO:0000305}.
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DR EMBL; AE013599; AAF57711.1; -; Genomic_DNA.
DR RefSeq; NP_611319.1; NM_137475.3.
DR AlphaFoldDB; P82706; -.
DR IntAct; P82706; 4.
DR STRING; 7227.FBpp0085843; -.
DR PaxDb; P82706; -.
DR DNASU; 37100; -.
DR EnsemblMetazoa; FBtr0086662; FBpp0085843; FBgn0034329.
DR GeneID; 37100; -.
DR KEGG; dme:Dmel_CG18108; -.
DR CTD; 37100; -.
DR FlyBase; FBgn0034329; BomS1.
DR VEuPathDB; VectorBase:FBgn0034329; -.
DR HOGENOM; CLU_204809_0_0_1; -.
DR OrthoDB; 1615923at2759; -.
DR PhylomeDB; P82706; -.
DR BioGRID-ORCS; 37100; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37100; -.
DR PRO; PR:P82706; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034329; Expressed in capitellum (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P82706; baseline and differential.
DR Genevisible; P82706; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; HEP:FlyBase.
DR InterPro; IPR013172; Bomanin.
DR Pfam; PF08194; DIM; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond; Immunity;
KW Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..27
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000269|PubMed:9736738"
FT /id="PRO_0000021488"
FT PEPTIDE 28..43
FT /note="Bomanin Short 1"
FT /id="PRO_0000021489"
FT MOD_RES 43
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:9736738"
FT DISULFID 36..39
FT /evidence="ECO:0000269|PubMed:9736738"
SQ SEQUENCE 45 AA; 4670 MW; 5DAB6236C020971D CRC64;
MKFFSVVTVF VLGLLAVANA VPLSPDPGNV IINGDCRVCN VHGGK
