TTKA_DROME
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 03-AUG-2022, entry version 188.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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};
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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; 84.
DR IntAct; P42282; 11.
DR STRING; 7227.FBpp0085186; -.
DR iPTMnet; P42282; -.
DR PaxDb; P42282; -.
DR PRIDE; P42282; -.
DR DNASU; 48317; -.
DR EnsemblMetazoa; FBtr0085825; FBpp0085186; FBgn0003870. [P42282-1]
DR EnsemblMetazoa; FBtr0085827; FBpp0085188; FBgn0003870. [P42282-1]
DR EnsemblMetazoa; FBtr0085829; FBpp0085190; FBgn0003870. [P42282-1]
DR EnsemblMetazoa; FBtr0303227; FBpp0292319; FBgn0003870. [P42282-1]
DR GeneID; 48317; -.
DR KEGG; dme:Dmel_CG1856; -.
DR CTD; 7272; -.
DR FlyBase; FBgn0003870; ttk.
DR VEuPathDB; VectorBase:FBgn0003870; -.
DR eggNOG; ENOG502QQPP; Eukaryota.
DR GeneTree; ENSGT00940000175057; -.
DR HOGENOM; CLU_013670_1_0_1; -.
DR InParanoid; P42282; -.
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 presumptive embryonic/larval digestive system (Drosophila) and 66 other tissues.
DR ExpressionAtlas; P42282; baseline and differential.
DR Genevisible; P42282; DM.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035883; P:enteroendocrine cell differentiation; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0048626; P:myoblast fate specification; IMP: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; 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:0043388; P:positive regulation of DNA binding; IDA: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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 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 525..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..390
FT /note="Polar 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
