TRRAP_DANRE
ID TRRAP_DANRE Reviewed; 3841 AA.
AC A0A0R4ITC5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Transformation/transcription domain-associated protein {ECO:0000312|ZFIN:ZDB-GENE-050809-47};
GN Name=trrap {ECO:0000312|ZFIN:ZDB-GENE-050809-47};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31231791; DOI=10.1111/cge.13590;
RA Xia W., Hu J., Ma J., Huang J., Wang X., Jiang N., Zhang J., Ma Z., Ma D.;
RT "Novel TRRAP mutation causes autosomal dominant non-syndromic hearing
RT loss.";
RL Clin. Genet. 96:300-308(2019).
CC -!- FUNCTION: Adapter protein, which is found in various multiprotein
CC chromatin complexes with histone acetyltransferase activity (HAT),
CC which gives a specific tag for epigenetic transcription activation. May
CC be required for the mitotic checkpoint and normal cell cycle
CC progression (By similarity). May play a role in the formation and
CC maintenance of the auditory system (PubMed:31231791).
CC {ECO:0000250|UniProtKB:Q9Y4A5, ECO:0000269|PubMed:31231791}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4A5}.
CC -!- DISRUPTION PHENOTYPE: Morpholino TRRAP knockdown results in defects in
CC the inner ear. Morphant larvae show reduced lateral line neuromasts,
CC decreased number of hair cells per neuromast, and fewer and thinner
CC stereocilia on the hair cells. In addition, the acoustic startle
CC response is decreased and sound-induced fast escape reflex is impaired.
CC {ECO:0000269|PubMed:31231791}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX005075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX571829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO082787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009304957.1; XM_009306682.2.
DR SMR; A0A0R4ITC5; -.
DR STRING; 7955.ENSDARP00000110252; -.
DR Ensembl; ENSDART00000160586; ENSDARP00000137625; ENSDARG00000100623.
DR GeneID; 557263; -.
DR KEGG; dre:557263; -.
DR CTD; 8295; -.
DR ZFIN; ZDB-GENE-050809-47; trrap.
DR GeneTree; ENSGT00390000017961; -.
DR OrthoDB; 7189at2759; -.
DR Reactome; R-DRE-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000100623; Expressed in presomitic mesoderm and 26 other tissues.
DR ExpressionAtlas; A0A0R4ITC5; baseline.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR GO; GO:0035675; P:neuromast hair cell development; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR033317; TRA1/TRRAP.
DR PANTHER; PTHR11139:SF1; PTHR11139:SF1; 2.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..3841
FT /note="Transformation/transcription domain-associated
FT protein"
FT /id="PRO_0000451069"
FT DOMAIN 2671..3239
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 3482..3805
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3809..3841
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 491..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2002..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3249..3271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3488..3494
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3669..3677
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3689..3714
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOTIF 2025..2040
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 493..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3251..3270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3841 AA; 435526 MW; 9769FD22B8197227 CRC64;
MSFVPTPSPT VVDQTTLMKK YLQFVAALTD NNTPDETKLK MMQEVSENFE NVTSSPQYST
FLEHIIPRFL TFLQDGEVQF LQEKPTQQLR KLVLEIIHRI PTNEHLRSHA KNILSVMFRF
LEIESEENVL ICLRIIIELH KQFRPPISQE IHHFLDFVKQ IYKELPKVVA RYFENPQVIA
ENTVPSPEMV GMITSVMVKT APERDDSETR THTIIPRGSL SLKVLAELPI IVVLMYQLYK
LNIHNVVSEF VPLIMNTIML QVSPQARQHK LFNKELYADF IAAQIKTLSF LAYIIRIYQD
LVGKYSQQMV KGMLQLLSNC PPETAHLRKE LLIAAKHILT TDLRSQFIPC MDKLFDESIL
IGSGYTARET LRPLAYSTLA DLVHHVRQNL PLTDLSLAVQ LFAKNIDDES LPSSIQTMSC
KLLLNLVDCI RSKSEQENGN GRDILMRMLE VFVLKFHTIA RYQLVSIFKK CKPQSEMGVV
DTGALPGVPA TPTVTTPALP PPAPPTPVTP APPPATSFDR AGEKEDKQTF QVSDCRSLVK
TLVCGVKTIT WGITSCKAPG EAQFIPNKQL QPKETQIYIK LVKYAMQALD IYQVQIAGNG
QTYIRVANCQ TVRMKEEKEV LEHFAGVFTM MNPLTFKEIF QTTVPYMVER ISKNYALQIV
ANSFLANLTT SALFATILVE YLLERLPEMG SNVELSNLYL KLFKLVFGSV SLFAAENEQM
LKPHLHKIVN SSMELAQSAK EPYNYFLLLR ALFRSIGGGS HDLLYQEFLP LLPNLLQGLN
MLQSGLHKQH MKDLFVELCL TVPVRLSSLL PYLPMLMDPL VSALNGSQTL VSQGLRTLEL
CVDNLQPDFL YDHIQPVRAE LMQALWRTLR NPAETISHVA YRVLGKFGGS NRKMLKESQK
LLYVVTEVQG PSIKAEFTDC KASIQLPMEK AIETALDCLK SANTEPYYRR QAWEVIKCFL
VAMTSLEDNK HSLYQLLAHP NFTEKWIPNV IISHRYKAQD TPARRTFEQA LTGAFMSAVI
KDLRPSALPF VASLIRHYTM VAVAQQCGPF LLPCYQSGSQ PSTGMFHSEE NGSKGMDPLV
LIDAIAICMA YEEKELCKIG EVALAVIFDV ASIILGSKER ACQLPLFSYI VERLCACCYE
QAWYAKLGGV VSIKFLMERL PLIWVLQNQL TFLKALLFVM MDLTGEVSNG AVAMAKTTLE
QLLIRCATPL KDEEKTEELL SAQDKSFHLV THDLVREVTS PNSTVRKQAM HSLQVLAQVT
GKSVTIIMEP HKEVLQDMVP PKKHLLRHQP ANAQIGLMEG NTFCTTLQPR LFTMDLNVME
HKVFYTELLN LCEAEDAALM KLPCYKSLPS LVPLRIAALN ALAACNYLPQ SREKIIAALF
KALNSTNSEL QEAGEACMGK FLEGATIEVD QIHTHMRPLL MMLGDYRSLT LNVVNRLTSV
TRLFPNSFND KFCDQMMQHL RKWMEVVVIT HKGGQRGDGS PAMEGVEEMR ICSAIINLFH
LIPAAPQTLV KPLLEVVMKT ERAMLIEAGS PFREPLIKFL TRHPSQTVEL FMMEATLNDP
QWSRMFMSFL KHKDAKPLRD VLASNPNRFV PLLVPAGSAA TVRPGSPSTS TARLDLQFQA
IKIISIIVKN DEGWLAGQHS LVSQLRRVWV SEAFQERHRK DNMAATNWKE PKLLAFCLLS
YCKRNYSEIE LLFQLLRAFT GRFLCNMTFL KEYMEEEIPK NYGITHKRAL FFRFVEFNDP
HFNDELKAKV LQHILNPAFL YSFEKGEGEQ LLGPPNPEGD NPESITSVFI TKVLDPEKQA
DLADSLRIYL LQFSTLLVEH APHHIHDNNK SRNSKLRRLM TFAWPCLLPK TCVDPACKYS
GHLLLAHIIA KFAIHKKIVL QVFHSLLKAH TMEARAIVRQ AMAILTPAVP ARMEDGHQML
THWTRKIIVE EGHTVPQLVH ILHLIVQHFR VYYPVRHHLV QHMISAMQRL GFTPSVTIEQ
RKLAVDLAEV VIKWELQRIK DQQPESEADP GSVGEGTSGA SAAMKRGMSV DSAQDVKRFR
TAAGAVGTVF GRSQSIPGTE ALLTKPVEKQ HTDTVVNFLI RIACQVNDST NVAGSPGELL
SRRCVNLMKT ALRPDMWPSS ELKLQWFDKL LMTVEQPNQA NFSNICTGLE ILCFLLSVLQ
PPAILSHFKP LQRGIAACMT CGNTKVLRAV HSLLSRLMST FPTEPSTSSV ASKYEELECL
YAAVGKVIYE GLTNYEKASS ANPTQLFGTL MILKSACSNN SSYIDRLISV FMRSLQKMVR
EHLSPQPNPG AAETSTVTSE LVMLSLDLVK MRLSVMNMEM RKNFIQVILT SLIEKSPDPK
ILRAVVKIVE EWVKNSGNPM ATNQVPNPRE KSILLVKMMT YIEKRFPDDL ELNAQFLDLV
NYVYRDDNLS GSDITSKLEP AFLSGLRCTQ PLIRAKFFEV FDASMKRRVY ERLLYICCSQ
NWESMGSHFW IKQCTELLLA VCERNTTIGT SCQGSMLPSI TNVINLADSH DRAAFAMATH
IKQEPREREN SETKEEDVEI DIELAPGDQT SLPKTKEQAE RDAGNQLHML TNRHDKFLDS
LREVKTGALL NALVQLCHIS TPLAEKTWVQ LFPRLWKILS DRQQHALSGE MGPFLCSGSH
QAQRDCQPSA LNCFVEAMSQ CVPPIPIRPC VLKYLGKTHN LWLRSTLMLE QQAFEKGLNL
HIKPKQSTEF YEQESITPPQ QEILDSLAEL YSLLQEEDMW AGLWQKRCKF PETSTAIAYE
QHGFFEQAQE TYEKAMEKAR KEHNVSPAIF PEYQLWEDHW IRCSKELNQW EPLTEYGQSK
GHNNPYLVLE CAWRVSNWAA MKEALVQVEL SCPKEMAWKV NMHRGYLAIC HPEEQQLNFI
ERLVEMASSL AIREWRRLPH IVSHVHTPLL QAAQQIIELQ EAAQINAGLQ PANLGRNTSL
HDMKTVVKTW RNRLPIVSDD LSHWSSIFMW RQHHYQAIVT AYENNTQHDP NTNNAMLGVH
ASASAIIQYG KIARKQGLVN VALDILSRIH TIPTVPIVDC FQKIRQQVKC YLQLAGVMGK
NECMQGLEVI ESTNLKYFTK EMTAEFYALK GMFLAQINKS EEANKAFSAA VQMHDVLVKA
WAMWGDYLEN IFVKDRQPHL GVSSITCYLH ACRHQNESKS RKYLAKVLWL LSFDDKNTLA
DAVDKYCIGV PPIQWLAWIP QLLTCLVGSE GKPLLNLISQ VGRVYPQAVY FPIRTLYLTL
KIEQRERYKS DSGQQQPSSA AAQTHSASDP GPIRATAPMW RCSRIMHMQR ELHPTLLSSL
EGIVDQMVWF RENWHEEVLR QLQQGLAKCY SVAFEKSGAV SDAKITPHTL NFVKKLVSTF
GVGLENVSNV STMFSSAASE SLARRAQATA QDPVFQKMKG QFTTDFDFSV PGSMKLHNLI
SKLKKWIKIL EAKTKQLPKF FLIEEKCRFL SNFSAQTAEV EIPGEFLMPK PTHYYIKIAR
FMPRVEIVQK HNTAARRLYI RGHNGKIYPY LVMNDACLTE SRREERVLQL LRLLNPCLEK
RKETTKRHLF FTVPRVVAVS PQMRLVEDNP SSLSLVEIYK QRCAKKGIEH DNPISRYYDR
LATVQARGTQ ASHQVLRDIL KEVQGNMVPR SMLKEWALHT FPNATDYWTF RKMFTIQLAL
IGLAEFMLHL NRLNPEMLQI AQDTGKLNVS YFRFDINDAT GDLDANRPVP FRLTPNISEF
LTTIGVSGPL TASMIAVARC FAQPNFKVDG ILKAVLRDEI IAWHKKTQED TSMPLSPAGQ
PENMDSQQLV SLVQKAVTAI MTRLHNLAQF EGGESKVNTL VAAANSLDNL CRMDPAWHPW
L