BM03_DROME
ID BM03_DROME Reviewed; 39 AA.
AC Q9V8G0;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Bomanin Short 3 {ECO:0000312|FlyBase:FBgn0040736};
DE AltName: Full=Bomanin-3 {ECO:0000303|PubMed:25915418};
DE AltName: Full=Immune-induced peptide 3 {ECO:0000312|FlyBase:FBgn0040736};
DE Short=DIM-3 {ECO:0000312|FlyBase:FBgn0040736};
DE Short=DIM3 {ECO:0000303|PubMed:9736738};
DE Flags: Precursor;
GN Name=BomS3 {ECO:0000312|FlyBase:FBgn0040736};
GN Synonyms=Bom3 {ECO:0000303|PubMed:25915418},
GN IM3 {ECO:0000312|FlyBase:FBgn0040736};
GN ORFNames=CG16844 {ECO:0000312|FlyBase:FBgn0040736};
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 {ECO:0000305};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 24-39, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R {ECO:0000305}; TISSUE=Hemolymph {ECO:0000305};
RA Bulet P., Charlet M., Ehret-Sabatier L.;
RL Submitted (JUL-2002) to UniProtKB.
RN [4] {ECO:0000305}
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 [5]
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 [6]
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:29920489). Has a role in resistance bacterial and fungal
CC infections (PubMed:25915418, PubMed:29920489). The strength of
CC antimicrobial activity appears to correlate with the overall level of
CC expression (PubMed:29920489). Has no activity against the fungus
CC C.glabrata in vitro (PubMed:29920489). {ECO:0000269|PubMed:25915418,
CC ECO:0000269|PubMed:29920489}.
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 (at protein level) (PubMed:9736738,
CC PubMed:29920489). Detected within 24 hours of infection
CC (PubMed:9736738). {ECO:0000269|PubMed:29920489,
CC ECO:0000269|PubMed:9736738}.
CC -!- MASS SPECTROMETRY: Mass=1701.71; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9736738, ECO:0000305};
CC -!- MISCELLANEOUS: Not induced after bacterial challenge in strains
CC carrying a loss-of-function mutation for Toll. Constitutively expressed
CC in Toll gain-of-function mutants. {ECO:0000269|PubMed:9736738}.
CC -!- SIMILARITY: Belongs to the bomanin family. {ECO:0000305}.
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DR EMBL; AE013599; AAF57707.1; -; Genomic_DNA.
DR RefSeq; NP_001286569.1; NM_001299640.1.
DR RefSeq; NP_652368.1; NM_144111.3.
DR AlphaFoldDB; Q9V8G0; -.
DR BioGRID; 72591; 2.
DR IntAct; Q9V8G0; 2.
DR STRING; 7227.FBpp0085846; -.
DR PaxDb; Q9V8G0; -.
DR DNASU; 50209; -.
DR EnsemblMetazoa; FBtr0086665; FBpp0085846; FBgn0040736.
DR EnsemblMetazoa; FBtr0340328; FBpp0309289; FBgn0040736.
DR GeneID; 50209; -.
DR KEGG; dme:Dmel_CG16844; -.
DR CTD; 50209; -.
DR FlyBase; FBgn0040736; BomS3.
DR VEuPathDB; VectorBase:FBgn0040736; -.
DR HOGENOM; CLU_204809_0_0_1; -.
DR InParanoid; Q9V8G0; -.
DR BioGRID-ORCS; 50209; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 50209; -.
DR PRO; PR:Q9V8G0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0040736; Expressed in capitellum (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q9V8G0; baseline and differential.
DR Genevisible; Q9V8G0; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral 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 Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..23
FT /evidence="ECO:0000255, ECO:0000305"
FT /id="PRO_0000021492"
FT PEPTIDE 24..39
FT /note="Bomanin Short 3"
FT /id="PRO_0000021493"
FT DISULFID 32..35
FT /evidence="ECO:0000305"
SQ SEQUENCE 39 AA; 4100 MW; F7A6F05C4096ADB0 CRC64;
MKFLSLAFVL GLLALANATP LNPGNVIING DCRVCNVRA
