BRUN_DROME
ID BRUN_DROME Reviewed; 1320 AA.
AC Q9VIL0; Q3KN61; Q961K0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein brunelleschi {ECO:0000303|PubMed:19934220};
DE AltName: Full=NIK- and IKBKB-binding protein;
GN Name=brun {ECO:0000312|FlyBase:FBgn0261787};
GN Synonyms=bru {ECO:0000303|PubMed:19934220};
GN ORFNames=CG2478 {ECO:0000312|FlyBase:FBgn0261787};
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=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-1320.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND THR-329, 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19934220; DOI=10.1242/jcs.054536;
RA Robinett C.C., Giansanti M.G., Gatti M., Fuller M.T.;
RT "TRAPPII is required for cleavage furrow ingression and localization of
RT Rab11 in dividing male meiotic cells of Drosophila.";
RL J. Cell Sci. 122:4526-4534(2009).
CC -!- FUNCTION: Cooperates with Rab11 and fwd/PI4K to mediate the flow of
CC membrane through the Golgi, which is required to support cleavage
CC furrow ingression, therefore promoting cytokinesis in male meiotic
CC cells. {ECO:0000269|PubMed:19934220}.
CC -!- SUBUNIT: May be part of the multisubunit TRAPP (transport protein
CC particle) complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19934220}. Golgi
CC apparatus {ECO:0000269|PubMed:19934220}. Note=Specific to
CC spermatocytes.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults of males and
CC females. {ECO:0000269|PubMed:19934220}.
CC -!- DISRUPTION PHENOTYPE: Failure of both actomyosin ring constriction and
CC furrow ingression in male meiotic cells. {ECO:0000269|PubMed:19934220}.
CC -!- SIMILARITY: Belongs to the NIBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK92972.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53907.2; -; Genomic_DNA.
DR EMBL; BT023878; ABA81812.1; -; mRNA.
DR EMBL; AY051548; AAK92972.1; ALT_FRAME; mRNA.
DR RefSeq; NP_610044.2; NM_136200.3.
DR AlphaFoldDB; Q9VIL0; -.
DR SMR; Q9VIL0; -.
DR BioGRID; 61289; 6.
DR STRING; 7227.FBpp0080933; -.
DR iPTMnet; Q9VIL0; -.
DR PaxDb; Q9VIL0; -.
DR PRIDE; Q9VIL0; -.
DR EnsemblMetazoa; FBtr0081403; FBpp0080933; FBgn0261787.
DR GeneID; 35325; -.
DR KEGG; dme:Dmel_CG2478; -.
DR UCSC; CG2478-RA; d. melanogaster.
DR CTD; 35325; -.
DR FlyBase; FBgn0261787; brun.
DR VEuPathDB; VectorBase:FBgn0261787; -.
DR eggNOG; KOG1953; Eukaryota.
DR HOGENOM; CLU_004738_0_0_1; -.
DR InParanoid; Q9VIL0; -.
DR OMA; HDHPVEH; -.
DR OrthoDB; 71855at2759; -.
DR PhylomeDB; Q9VIL0; -.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 35325; 0 hits in 1 CRISPR screen.
DR ChiTaRS; bru; fly.
DR GenomeRNAi; 35325; -.
DR PRO; PR:Q9VIL0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261787; Expressed in egg cell and 21 other tissues.
DR ExpressionAtlas; Q9VIL0; baseline and differential.
DR Genevisible; Q9VIL0; DM.
DR GO; GO:0036063; C:acroblast; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0030008; C:TRAPP complex; ISS:FlyBase.
DR GO; GO:1990071; C:TRAPPII protein complex; IDA:FlyBase.
DR GO; GO:0000916; P:actomyosin contractile ring contraction; IMP:FlyBase.
DR GO; GO:0048193; P:Golgi vesicle transport; IC:FlyBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:FlyBase.
DR GO; GO:0007111; P:meiosis II cytokinesis; IMP:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:FlyBase.
DR GO; GO:0048137; P:spermatocyte division; IMP:FlyBase.
DR InterPro; IPR013935; TRAPP_II_complex_Trs120.
DR PANTHER; PTHR21512; PTHR21512; 1.
DR Pfam; PF08626; TRAPPC9-Trs120; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1320
FT /note="Protein brunelleschi"
FT /id="PRO_0000372863"
FT REGION 313..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 83
FT /note="H -> Y (in Ref. 3; ABA81812)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="V -> I (in Ref. 3; ABA81812)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="V -> M (in Ref. 3; ABA81812)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> C (in Ref. 3; ABA81812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1320 AA; 145958 MW; 3E07FF2ECB3B5A50 CRC64;
MRAAVGLMLS HGAGGMEPAL SRPDYEQSAL HHSCLLVLLR GVGPSRARVL QRAFEKVRRV
NHIRVNDSSG HPRSIWIRFV HDHPVEHNDW GDFQTHRRLL GLVTIGKFDS QIELNELCRQ
HESLKVRYGS TLYESRAIFF GPDEQPLETI GEVLGPPAAG GRRLQDEFTT PSNFKAQAFF
YREQDSCADL ESRIGDFASA LFWVLESRRL ERSREKADKV SLLLAPFEKR DFVGLDMESR
NNRKRCVGRV MKNLADLSLQ AGLVDDALSL YHNANETLRS VGDSLWVGAT EEGLCAASAM
LLYPQMRETE TLHRNSSLQE AGTSPLKNTP EKWRASDATK KISASDATAN NVDSNQPQQR
VTSNSSSCSS VSSLVTTATN SSASDTPTTS SSSTSTISAA PIPGHQRNGD LPGNILKAEE
ISNYYRKAII NYSKYRHAAT IETEAALKAS RICIEQNRPL DVAMFLQNIL YINLSMSEAE
RVKRFEVITD LYQQIGYQRK AAFFQRLAAL KHVQQGSQAP DWNQSYRLML GSFTGYRLCL
DPLEVIENAA GWPALQIDLV QTLITAARRL GHSALATRHM TFLLQTQWDN MSPTEQSEMA
VQLQNLSAQC EGSPVPLVLE NGTVIPPANL TDLPYCIDLQ VKDLPAHLRP QRIKVAKADS
GPFLFTPIHF NSVDRRDKKK DKNKIAFQWV QNDLSEVTVR LRNPLPFELP VTDMRLLTNG
VVFESLPQTL VLQPHVPTYV ALHGTPIETG QLDLQGYSTH TLGVKSNCRL KHMRGRSFPP
NYVVDVIPAL PRISVKTSLP QTATFSNMNS ADIVVTSASL TLYNGESSSC TITITNESAT
LPLEHLEFSI NSNVEQELQQ KIFRIDEEAI KAHLPVPPQG TIEIIVDVFA EADFVCPQPP
ASLHSAAAPG DYGASSLTHY SSVSTSGHAS LPSRVGSPHH RRNEPQNSSF RSTISGGPPS
LAALTLHPGG GGGVGPSSLG SQYNQHIEAQ VRFKYSGGDA LTAGYCRQCA VSFNLELLPS
VQITSWDVLP AEVASQFYLV LDISNLTAQE MSLNYTDTKN ILIEAKESCR VPIPVDRCSL
EKVVAARAAE VAENLERELC FRTQLLSFND ALSKLCSIHI AERVKIKWLL TGTDIQGIAS
LRGIVLSQSM VDLTAVSPLE WAISFQDTLV QPHNEIVCTV GQRSLLSIQL ANQSLQPLRN
LVLSIKFYQD YLNGMENYNL ETRVAISGPN RIAIPLLEKQ EQKEHTCSVI FFTPGRFKAS
IECTSNPQKQ SEQPSSLLTR SCPAEAESVG QSVMFSSSYD EQQAHVWKFI PPIEVTVVEQ
