BTBD9_DROME
ID BTBD9_DROME Reviewed; 722 AA.
AC Q9W2S3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=BTB/POZ domain-containing protein 9 {ECO:0000303|PubMed:22658601};
GN Name=BTBD9 {ECO:0000312|FlyBase:FBgn0030228};
GN ORFNames=CG1826 {ECO:0000312|FlyBase:FBgn0030228};
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:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
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:0000312|EMBL:AAL39453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22658601; DOI=10.1016/j.cub.2012.04.027;
RA Freeman A., Pranski E., Miller R.D., Radmard S., Bernhard D., Jinnah H.A.,
RA Betarbet R., Rye D.B., Sanyal S.;
RT "Sleep fragmentation and motor restlessness in a Drosophila model of
RT Restless Legs Syndrome.";
RL Curr. Biol. 22:1142-1148(2012).
CC -!- FUNCTION: Essential for the homeostatic regulation of sleep and motor
CC activity, by depressing hyperactivity and wakefulness. May function, at
CC least in part, by ensuring dopamine biosynthesis.
CC {ECO:0000269|PubMed:22658601}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22658601}.
CC Note=Localized to distinct puncta in neuronal cytoplasm.
CC {ECO:0000269|PubMed:22658601}.
CC -!- TISSUE SPECIFICITY: Detected in the brain (at protein level).
CC {ECO:0000269|PubMed:22658601}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larval muscles.
CC {ECO:0000269|PubMed:22658601}.
CC -!- DISRUPTION PHENOTYPE: Adults display increased motor activity during
CC locomotion, fragmented sleep and a decreased lifespan. Walking speed is
CC not effected however flies spend more time moving with slightly fewer
CC pauses resulting in longer uninterrupted bouts of walking. The total
CC duration of sleep is not effected but average sleep bout length is
CC decreased, the number of sleep bouts is increased and the amount of
CC wake after sleep onset (WASO) is also increased. Dopamine levels are
CC decreased by 50%. No effect on flight or climbing (negative geotaxis).
CC RNAi-mediated knockdown in a large subset of dopaminergic neurons also
CC results in fragmented sleep. {ECO:0000269|PubMed:22658601}.
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DR EMBL; AE014298; AAF46616.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95274.1; -; Genomic_DNA.
DR EMBL; AY069308; AAL39453.1; -; mRNA.
DR RefSeq; NP_001259431.1; NM_001272502.1.
DR RefSeq; NP_572649.1; NM_132421.3.
DR AlphaFoldDB; Q9W2S3; -.
DR SMR; Q9W2S3; -.
DR STRING; 7227.FBpp0071426; -.
DR PaxDb; Q9W2S3; -.
DR PRIDE; Q9W2S3; -.
DR EnsemblMetazoa; FBtr0071497; FBpp0071426; FBgn0030228.
DR EnsemblMetazoa; FBtr0334456; FBpp0306532; FBgn0030228.
DR GeneID; 32000; -.
DR KEGG; dme:Dmel_CG1826; -.
DR UCSC; CG1826-RA; d. melanogaster.
DR CTD; 114781; -.
DR FlyBase; FBgn0030228; BTBD9.
DR VEuPathDB; VectorBase:FBgn0030228; -.
DR eggNOG; KOG4350; Eukaryota.
DR GeneTree; ENSGT00940000169300; -.
DR HOGENOM; CLU_004253_0_2_1; -.
DR InParanoid; Q9W2S3; -.
DR OMA; YFCRSWQ; -.
DR OrthoDB; 607923at2759; -.
DR PhylomeDB; Q9W2S3; -.
DR BioGRID-ORCS; 32000; 0 hits in 1 CRISPR screen.
DR ChiTaRS; BTBD9; fly.
DR GenomeRNAi; 32000; -.
DR PRO; PR:Q9W2S3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030228; Expressed in cleaving embryo and 23 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0048512; P:circadian behavior; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IMP:FlyBase.
DR CDD; cd14822; BACK_BTBD9; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR034091; BTBD9_BACK-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..722
FT /note="BTB/POZ domain-containing protein 9"
FT /id="PRO_0000438108"
FT DOMAIN 46..112
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 151..247
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REGION 577..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..593
FT /evidence="ECO:0000255"
FT COMPBIAS 577..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 82036 MW; F0A13EC35AF6DD73 CRC64;
MSSQGHHKMS GGGKKGAMEQ DYTDVVDLGD RFSADMARLC MNEQYADVEF IVEEERIPAH
RVILAARSEY FRALLYGGMA ETTQRQIPLE VPLEAFKVLL RYIYSGTLLL STLDEDSTID
VLGMANQYGF QDLEMAISNY LRQYLALDNV CMILDAARLY NLEELTEVCL MFMDRNAGDL
LLHNSFNTLS KESLEEVLRR DCFFAPEVQI FLAVWKWSRF NSNVDFKSVV SYVRLPLMNL
EHLLQVVRPS GILDPDKILD AIDERSTSKA LPYRAALWPE ENVAAETFLS RCIQGECRDA
LLDGDVTTYD MENGYTRHCI TDSKDAGIVV ELGTFCMINH IRMLLWDRDS RAYSYYVEVS
GDQQHWDRVV DYSDYHCRSW QYLYFEARPV RFIRLVGTQN TVNRVFHVVG LEAMHTAKVP
RLVNHFVAPK TNVATVEMSA IVTDGVSRTR NALINGDYVR YDWDSGYTCH QLGSGEIVVR
LGQPYYLGSM RLLLWDCDDR TYSFYIEIST NRKEWQMVVD RRNDRTRSWQ NFHFTPRPVV
YIRIVGTRNT ANEIFHCVHL ECPTQDKNYL KKIADMEKER EKREKEKKTA KTDDDNIAST
SGSSLASGHA ESPSTSSSSS QSVLRSIHWP PQTREVAVAP LTPPALSPPG TPALPAPLTP
ATSSPHNNHE QNQPSNISAD ASHHTSPSSR SNPSPSLSRS RSQSAELEPV PPLVELDTRE
TL
