BOWEL_DROME
ID BOWEL_DROME Reviewed; 744 AA.
AC Q9VQU9; Q24219;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein bowel;
DE AltName: Full=Brother of odd with entrails limited;
GN Name=bowl {ECO:0000312|FlyBase:FBgn0004893}; ORFNames=CG10021;
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] {ECO:0000305, ECO:0000312|EMBL:AAB17949.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF THR-261; ASP-279; HIS-284; THR-343; THR-345 AND LEU-609.
RC STRAIN=Canton-S {ECO:0000269|PubMed:8670819};
RC TISSUE=Embryo {ECO:0000269|PubMed:8670819};
RX PubMed=8670819; DOI=10.1002/j.1460-2075.1996.tb00681.x;
RA Wang L., Coulter D.E.;
RT "Bowel, an odd-skipped homolog, functions in the terminal pathway during
RT Drosophila embryogenesis.";
RL EMBO J. 15:3182-3196(1996).
RN [2] {ECO:0000312|EMBL:AAF51065.1}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF51065.1}
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] {ECO:0000312|EMBL:AAQ23612.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23612.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAB17949.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 233-372, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S {ECO:0000269|PubMed:8878683};
RC TISSUE=Embryo {ECO:0000269|PubMed:8878683};
RX PubMed=8878683; DOI=10.1093/genetics/144.1.171;
RA Hart M.C., Wang L., Coulter D.E.;
RT "Comparison of the structure and expression of odd-skipped and two related
RT genes that encode a new family of zinc finger proteins in Drosophila.";
RL Genetics 144:171-182(1996).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11784087; DOI=10.1006/dbio.2001.0483;
RA Iwaki D.D., Johansen K.A., Singer J.B., Lengyel J.A.;
RT "Drumstick, bowl, and lines are required for patterning and cell
RT rearrangement in the Drosophila embryonic hindgut.";
RL Dev. Biol. 240:611-626(2001).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-284.
RX PubMed=14573519; DOI=10.1242/dev.00833;
RA de Celis Ibeas J.M., Bray S.J.;
RT "Bowl is required downstream of Notch for elaboration of distal limb
RT patterning.";
RL Development 130:5943-5952(2003).
RN [8] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14597202; DOI=10.1016/j.ydbio.2003.07.011;
RA Hao I., Green R.B., Dunaevsky O., Lengyel J.A., Rauskolb C.;
RT "The odd-skipped family of zinc finger genes promotes Drosophila leg
RT segmentation.";
RL Dev. Biol. 263:282-295(2003).
RN [9] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14568103; DOI=10.1016/j.mod.2003.08.001;
RA Johansen K.A., Green R.B., Iwaki D.D., Hernandez J.B., Lengyel J.A.;
RT "The Drm-Bowl-Lin relief-of-repression hierarchy controls fore- and hindgut
RT patterning and morphogenesis.";
RL Mech. Dev. 120:1139-1151(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Putative transcription factor. Required for leg joint
CC formation, acting downstream of Notch to pattern the leg tarsal
CC segments. Functions in the terminal pathway during embryogenesis,
CC acting downstream of tll in the posterior of the embryo. Acts in a
CC hierarchy downstream of drm and lin during foregut and hindgut
CC patterning and morphogenesis. Involved in cell rearrangement during
CC elongation of the embryonic hindgut. Regulates expression of hindgut
CC patterning genes to establish the small intestine region of the
CC embryonic hindgut. Required in the foregut for spatially localized gene
CC expression and morphogenesis of the proventriculus.
CC {ECO:0000269|PubMed:11784087, ECO:0000269|PubMed:14568103,
CC ECO:0000269|PubMed:14573519, ECO:0000269|PubMed:14597202,
CC ECO:0000269|PubMed:8670819}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at the termini of the blastoderm embryo
CC in three domains; strongly expressed at the posterior pole, relatively
CC weakly expressed at the anterior pole and expressed in a broad
CC transverse stripe just anterior to the presumptive cephalic furrow.
CC Subsequent to the blastoderm stage, the expression pattern reflects the
CC morphological rearrangements associated with gastrulation.
CC Additionally, at early gastrulation, terminal expression is
CC supplemented by weak expression in seven stripes. These primary stripes
CC are rapidly supplemented by seven secondary stripes. Relatively
CC uniformly expressed throughout the anlagen, primordia and epithelia of
CC the embryonic foregut and hindgut. By stage 13, hindgut expression is
CC greatly reduced but foregut expression remains high until stage 17.
CC Segmentally expressed in the developing leg; present at a subset of
CC segmental boundaries including all proximal joints (coxa/femur,
CC femur/tibia, tibia/t1) and the distal t5/pretarsal boundary.
CC {ECO:0000269|PubMed:11784087, ECO:0000269|PubMed:14568103,
CC ECO:0000269|PubMed:14573519, ECO:0000269|PubMed:14597202,
CC ECO:0000269|PubMed:8670819, ECO:0000269|PubMed:8878683}.
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DR EMBL; U58282; AAB17949.1; -; mRNA.
DR EMBL; AE014134; AAF51065.1; -; Genomic_DNA.
DR EMBL; BT010294; AAQ23612.1; -; mRNA.
DR PIR; S70619; S70619.
DR RefSeq; NP_001245861.1; NM_001258932.2.
DR RefSeq; NP_001245862.1; NM_001258933.2.
DR RefSeq; NP_001245863.1; NM_001258934.1.
DR RefSeq; NP_476883.1; NM_057535.4.
DR RefSeq; NP_722939.1; NM_164556.2.
DR RefSeq; NP_722940.1; NM_164557.3.
DR RefSeq; NP_722941.1; NM_164558.2.
DR AlphaFoldDB; Q9VQU9; -.
DR SMR; Q9VQU9; -.
DR BioGRID; 59806; 19.
DR ELM; Q9VQU9; -.
DR IntAct; Q9VQU9; 43.
DR STRING; 7227.FBpp0297869; -.
DR iPTMnet; Q9VQU9; -.
DR PaxDb; Q9VQU9; -.
DR DNASU; 33602; -.
DR EnsemblMetazoa; FBtr0077490; FBpp0077179; FBgn0004893.
DR EnsemblMetazoa; FBtr0077491; FBpp0077180; FBgn0004893.
DR EnsemblMetazoa; FBtr0077492; FBpp0077181; FBgn0004893.
DR EnsemblMetazoa; FBtr0077493; FBpp0077182; FBgn0004893.
DR EnsemblMetazoa; FBtr0307027; FBpp0297870; FBgn0004893.
DR EnsemblMetazoa; FBtr0307028; FBpp0297871; FBgn0004893.
DR EnsemblMetazoa; FBtr0307029; FBpp0297872; FBgn0004893.
DR GeneID; 33602; -.
DR KEGG; dme:Dmel_CG10021; -.
DR CTD; 33602; -.
DR FlyBase; FBgn0004893; bowl.
DR VEuPathDB; VectorBase:FBgn0004893; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000168461; -.
DR HOGENOM; CLU_015566_0_0_1; -.
DR InParanoid; Q9VQU9; -.
DR OMA; RQSPVHN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9VQU9; -.
DR SignaLink; Q9VQU9; -.
DR BioGRID-ORCS; 33602; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33602; -.
DR PRO; PR:Q9VQU9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004893; Expressed in wing disc and 78 other tissues.
DR ExpressionAtlas; Q9VQU9; baseline and differential.
DR Genevisible; Q9VQU9; DM.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:UniProtKB.
DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007362; P:terminal region determination; IMP:UniProtKB.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Nucleus; Pair-rule protein;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..744
FT /note="Protein bowel"
FT /id="PRO_0000046909"
FT ZN_FING 238..260
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..344
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 261
FT /note="T->M: In bowl3; embryonic lethal."
FT /evidence="ECO:0000269|PubMed:8670819"
FT MUTAGEN 279
FT /note="D->N: In bowl4; embryonic lethal with 50%
FT larval/pupal escapers."
FT /evidence="ECO:0000269|PubMed:8670819"
FT MUTAGEN 284
FT /note="H->Y: In bowl2; embryonic lethal. Legs containing
FT clones show fusion and truncation of tarsomeres and
FT disrupted expression of the leg patterning genes bab2, dac
FT and B-H1."
FT /evidence="ECO:0000269|PubMed:14573519,
FT ECO:0000269|PubMed:8670819"
FT MUTAGEN 343
FT /note="T->I: In bowl5; embryonic lethal; when associated
FT with K-345 and P-609."
FT /evidence="ECO:0000269|PubMed:8670819"
FT MUTAGEN 345
FT /note="T->K: In bowl5; embryonic lethal; when associated
FT with I-343 and P-609."
FT /evidence="ECO:0000269|PubMed:8670819"
FT MUTAGEN 609
FT /note="L->P: In bowl5; embryonic lethal; when associated
FT with I-343 and K-345."
FT /evidence="ECO:0000269|PubMed:8670819"
FT CONFLICT 196
FT /note="F -> S (in Ref. 1; AAB17949)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="P -> L (in Ref. 1; AAB17949)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="A -> P (in Ref. 1; AAB17949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 79831 MW; 403653CE7F57672D CRC64;
MPTESSSSEI SGGGGGAIPM LRPSRMDQFM NSMAAAAAAV GGGGLPGAAD RNGGSGGSDG
GSQNGNGDSR NSSASRISAY ETQLAYQQHL AGLHGPPPPP PPSHHREISA FVPVLPTGKV
RPGSNSNYEI IAMMADKRKE LALREAAAAA AMLGRGPGGP GGPGVPPPGV LYGPAGVPPP
PYLTGPGPSP TGAGSFPFPP GAAAAALFPP GLGPGMHAGL DRRLLRAPGR ASRPKKQFIC
KFCNRQFTKS YNLLIHERTH TDERPYSCDI CGKAFRRQDH LRDHRYIHSK EKPFKCTECG
KGFCQSRTLA VHKILHMEES PHKCPVCSRS FNQRSNLKTH LLTHTDHKPY ECSSCGKVFR
RNCDLRRHAL THAVGEVNSG DYVDVGEEDE ARNLSGDEED SLLEVDSPRQ SPVHNLGESG
GSGEKSESER MRLKRKAAID HEESEEEFDD FDEEEELQDL PRVHDLPREE DDDFDPEDEE
QAEVALVARF QASKAAATSQ SSSSVGTKPE RQGVTHCHHE GGETYTMRPH GEKHQEEPGN
SGIASLPVPP SFVRYSVPPG AAGPPPAPPG APPPTHQHPG HPHLLPPNGD PYLPILHVRR
DLHHKSLNLS KAGVPPPPHT PPTIITQPES GKPPNQPLHS PHEAMPSFLG SIPMRKRILP
APTLDLMDPH HHPGLGQRTF VDSPSIYALN MSRHPPRQLL GKPPSTETSG ATTEKGPPVA
APPIAPPPAP PRRTGFSIED IMRR