BM02_DROME
ID BM02_DROME Reviewed; 45 AA.
AC O77150; Q8MLI5; Q9V8F9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bomanin Short 2 {ECO:0000312|FlyBase:FBgn0025583};
DE AltName: Full=Bomanin-2 {ECO:0000303|PubMed:25915418};
DE AltName: Full=Immune-induced peptide 2 {ECO:0000312|FlyBase:FBgn0025583};
DE Short=DIM-2 {ECO:0000303|PubMed:9736738, ECO:0000312|FlyBase:FBgn0025583};
DE Flags: Precursor;
GN Name=BomS2 {ECO:0000312|FlyBase:FBgn0025583};
GN Synonyms=Bom2 {ECO:0000312|FlyBase:FBgn0025583},
GN IM2 {ECO:0000312|FlyBase:FBgn0025583};
GN ORFNames=CG18106 {ECO:0000312|FlyBase:FBgn0025583};
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 29-44, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AMIDATION
RP AT GLY-43, DISULFIDE BOND, 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 [2]
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 28-43, AND AMIDATION AT GLY-43.
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 [6]
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 [7]
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). {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; AF074003; AAC62494.1; -; mRNA.
DR EMBL; AE013599; AAF57708.1; -; Genomic_DNA.
DR EMBL; AY071680; AAL49302.1; -; mRNA.
DR RefSeq; NP_725776.1; NM_166277.3.
DR AlphaFoldDB; O77150; -.
DR DIP; DIP-17127N; -.
DR IntAct; O77150; 3.
DR STRING; 7227.FBpp0085845; -.
DR PaxDb; O77150; -.
DR DNASU; 49802; -.
DR EnsemblMetazoa; FBtr0086664; FBpp0085845; FBgn0025583.
DR GeneID; 49802; -.
DR KEGG; dme:Dmel_CG18106; -.
DR CTD; 49802; -.
DR FlyBase; FBgn0025583; BomS2.
DR VEuPathDB; VectorBase:FBgn0025583; -.
DR GeneTree; ENSGT00940000176352; -.
DR HOGENOM; CLU_204809_0_0_1; -.
DR InParanoid; O77150; -.
DR OrthoDB; 1615923at2759; -.
DR PhylomeDB; O77150; -.
DR BioGRID-ORCS; 49802; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 49802; -.
DR PRO; PR:O77150; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0025583; Expressed in capitellum (Drosophila) and 21 other tissues.
DR Genevisible; O77150; 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:12171930"
FT /id="PRO_0000021490"
FT PEPTIDE 28..43
FT /note="Bomanin Short 2"
FT /id="PRO_0000021491"
FT MOD_RES 43
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:9736738"
FT DISULFID 36..39
FT /evidence="ECO:0000269|PubMed:9736738"
FT CONFLICT 12..19
FT /note="FGLLALAN -> LRSAGSGQT (in Ref. 1; AAC62494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 45 AA; 4740 MW; 81986CD63B8135B7 CRC64;
MKFFSVVTVF VFGLLALANA VPLSPDPGNV VINGDCKYCN VHGGK
