ID TTKA_DROME Reviewed; 813 AA. AC P42282; A4V3Q3; Q0KHY0; Q1LZ43; Q24313; Q9V9V2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 3. DT 04-NOV-2026, entry version 205. DE RecName: Full=Protein tramtrack, alpha isoform; DE AltName: Full=Repressor protein fushi tarazu; DE AltName: Full=Tramtrack p88; GN Name=ttk; Synonyms=FTZ-F2; ORFNames=CG1856; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=8504931; DOI=10.1101/gad.7.6.1085; RA Xiong W.C., Montell C.; RT "Tramtrack is a transcriptional repressor required for cell fate RT determination in the Drosophila eye."; RL Genes Dev. 7:1085-1096(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND DNA-BINDING. RC TISSUE=Embryo; RX PubMed=1372245; DOI=10.1002/j.1460-2075.1992.tb05142.x; RA Read D., Manley J.L.; RT "Alternatively spliced transcripts of the Drosophila tramtrack gene encode RT zinc finger proteins with distinct DNA binding specificities."; RL EMBO J. 11:1035-1044(1992). RN [3] 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 [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-487. RC STRAIN=Berkeley; 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 (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH CG33525. RX PubMed=15306652; DOI=10.1523/jneurosci.0238-04.2004; RA Dallman J.E., Allopenna J., Bassett A., Travers A., Mandel G.; RT "A conserved role but different partners for the transcriptional RT corepressor CoREST in fly and mammalian nervous system formation."; RL J. Neurosci. 24:7186-7193(2004). RN [7] RP FUNCTION, AND INTERACTION WITH PHYL. RX PubMed=17962185; DOI=10.1074/jbc.m707765200; RA Cooper S.E., Murawsky C.M., Lowe N., Travers A.A.; RT "Two modes of degradation of the tramtrack transcription factors by Siah RT homologues."; RL J. Biol. Chem. 283:1076-1083(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205; SER-206; RP THR-209 AND SER-682, AND 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: Binds to a number of sites in the transcriptional regulatory CC region of ftz. Isoform alpha is required to repress genes that promote CC the R7 cell fate. Probable repressor of the transcription of the CC segmentation genes ftz, eve, h, odd, run, and en. May bind to the CC region 5'-AGGG[CT]GG-3'. Degradation of ttk is directed by binding of CC sinah or sina, via the adapter molecule phyl which binds to the BTB CC domain of ttk. {ECO:0000269|PubMed:17962185, CC ECO:0000269|PubMed:8504931}. CC -!- SUBUNIT: Interacts with CoRest/CG33525, suggesting that it acts by CC recruiting a CoRest-containing corepressor complex. Interacts with CC phyl. {ECO:0000269|PubMed:15306652, ECO:0000269|PubMed:17962185}. CC -!- INTERACTION: CC P42282; Q95RJ9: ebi; NbExp=2; IntAct=EBI-77008, EBI-421390; CC P42282; Q27934: phyl; NbExp=10; IntAct=EBI-77008, EBI-77033; CC P42282; P21461: sina; NbExp=4; IntAct=EBI-77008, EBI-77019; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Alpha; Synonyms=p88, A, E; CC IsoId=P42282-1; Sequence=Displayed; CC Name=Beta; Synonyms=p69, C, D, F; CC IsoId=P17789-1; Sequence=External; CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC Expressed in preblastoderm embryos, followed by complete decay upon CC formation of the cellular blastoderm when ftz striped expression is at CC its peak. CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA77786.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X71626; CAA50633.1; -; mRNA. DR EMBL; Z11723; CAA77785.1; -; mRNA. DR EMBL; Z11723; CAA77786.1; ALT_INIT; mRNA. DR EMBL; AE014297; AAF57179.1; -; Genomic_DNA. DR EMBL; AE014297; AAF57180.1; -; Genomic_DNA. DR EMBL; AE014297; AAN14282.1; -; Genomic_DNA. DR EMBL; BT025183; ABF00108.1; -; mRNA. DR PIR; S36018; S36018. DR RefSeq; NP_001189329.1; NM_001202400.1. [P42282-1] DR RefSeq; NP_733443.1; NM_170564.3. [P42282-1] DR RefSeq; NP_733444.1; NM_170565.2. [P42282-1] DR RefSeq; NP_733445.1; NM_170566.3. [P42282-1] DR AlphaFoldDB; P42282; -. DR SMR; P42282; -. DR BioGRID; 71315; 104. DR FunCoup; P42282; 237. DR IntAct; P42282; 13. DR STRING; 7227.FBpp0085186; -. DR GlyGen; P42282; 2 sites. DR iPTMnet; P42282; -. DR PaxDb; 7227-FBpp0085186; -. DR PeptideAtlas; P42282; -. DR DNASU; 48317; -. DR EnsemblMetazoa; FBtr0085825; FBpp0085186; FBgn0003870. DR EnsemblMetazoa; FBtr0085827; FBpp0085188; FBgn0003870. DR EnsemblMetazoa; FBtr0085829; FBpp0085190; FBgn0003870. DR EnsemblMetazoa; FBtr0303227; FBpp0292319; FBgn0003870. DR GeneID; 48317; -. DR KEGG; dme:Dmel_CG1856; -. DR AGR; FB:FBgn0003870; -. DR CTD; 7272; -. DR FlyBase; FBgn0003870; ttk. DR VEuPathDB; VectorBase:FBgn0003870; -. DR eggNOG; ENOG502QQPP; Eukaryota. DR HOGENOM; CLU_013670_1_0_1; -. DR InParanoid; P42282; -. DR OrthoDB; 19132at2759; -. DR PhylomeDB; P42282; -. DR SignaLink; P42282; -. DR BioGRID-ORCS; 48317; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 48317; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0003870; Expressed in polar follicle cell (Drosophila) in ovary and 226 other cell types or tissues. DR ExpressionAtlas; P42282; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase. DR GO; GO:0017053; C:transcription repressor complex; IPI:FlyBase. DR GO; GO:0003677; F:DNA binding; IDA:FlyBase. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase. DR GO; GO:0031208; F:POZ domain binding; IDA:FlyBase. DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase. DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase. DR GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase. DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase. DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase. DR GO; GO:0048750; P:compound eye corneal lens morphogenesis; IMP:FlyBase. DR GO; GO:0031104; P:dendrite regeneration; IMP:FlyBase. DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase. DR GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase. DR GO; GO:0007307; P:eggshell chorion gene amplification; IMP:FlyBase. DR GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:FlyBase. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:FlyBase. DR GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase. DR GO; GO:0048626; P:myoblast fate specification; IMP:FlyBase. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:FlyBase. DR GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IMP:FlyBase. DR GO; GO:0045677; P:negative regulation of R7 cell differentiation; IMP:FlyBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase. DR GO; GO:0007422; P:peripheral nervous system development; TAS:FlyBase. DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase. DR GO; GO:0048053; P:R1/R6 development; IMP:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR GO; GO:0042682; P:regulation of compound eye cone cell fate specification; IMP:FlyBase. DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase. DR GO; GO:0045500; P:sevenless signaling pathway; IPI:FlyBase. DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase. DR CDD; cd18315; BTB_POZ_BAB-like; 1. DR FunFam; 3.30.710.10:FF:000091; Lola, isoform F; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR051095; Dros_DevTransReg. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR013087; Zf-C2H2_type. DR InterPro; IPR036236; Znf_C2H2_sf. DR PANTHER; PTHR23110; BTB DOMAIN TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR23110:SF82; PROTEIN TRAMTRACK, ALPHA ISOFORM; 1. DR Pfam; PF00651; BTB; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..813 FT /note="Protein tramtrack, alpha isoform" FT /id="PRO_0000047078" FT DOMAIN 33..98 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT ZN_FING 610..638 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 646..669 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 118..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 526..585 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..145 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..187 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 192..201 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..285 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..388 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 560..578 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 209 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 682 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT CONFLICT 186 FT /note="L -> V (in Ref. 2; CAA77785/CAA77786)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="P -> R (in Ref. 1; CAA50633)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="E -> Q (in Ref. 1; CAA50633)" FT /evidence="ECO:0000305" SQ SEQUENCE 813 AA; 88383 MW; CF3EE14069C79AA2 CRC64; MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSVT PTKATPELSQ RLFGSSSTTI SATAPGGSST GPSETISLLE ISDERESAPV HLPTILGLKI RAINTTTPAQ QGSPQTPTKS KPKIRQATGS NNSNSLLKQQ LRGGAKDPEV PPATRITGAV TPNAALNAEE QSKEMPKKNQ DEVNACIGLH SLANAAEQQA AQVASTGNLH HQLLLHMAAN NSMLNTTDYY QQQQQESPSS AGQFMDDDLE LLSLNDQQDK SDEPDHEMVT LADENAGLPG YQGNEAEATP AQEDSPAAET ATAPPPAPRS GKKGAKRPIQ RRRVRRKAQS TLDDQAEHLT EMSVRGLDLF RYASVVEGVY RCTECAKENM QKTFKNKYSF QRHAFLYHEG KHRKVFPCPV CSKEFSRPDK MKNHLKMTHE NFTPPKDIGA FSPLKYLISA AAAGDMHATI YQQQQDHYHR QLAEQLEQQN ASFDSRDSSL ILPDVKMEHA EDQDAEQEAE LSDGGYDASN PAAAAAAMLS LQQDVIIKDE IQISPSPSPT PPASCAVAEG KSLALASTAQ TAT //