BRDT_DANRE
ID BRDT_DANRE Reviewed; 918 AA.
AC F1QW93;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Bromodomain testis-specific protein;
GN Name=brdt; Synonyms=si:dkeyp-85h7.3;
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).
CC -!- FUNCTION: Testis-specific chromatin protein that specifically binds
CC histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac,
CC respectively) and plays a key role in spermatogenesis. Required in late
CC pachytene spermatocytes: plays a role in meiotic and post-meiotic cells
CC by binding to acetylated histones at the promoter of specific meiotic
CC and post-meiotic genes, facilitating their activation at the
CC appropriate time. In the post-meiotic phase of spermatogenesis, binds
CC to hyperacetylated histones and participates in their general removal
CC from DNA. Also recognizes and binds a subset of butyrylated histones:
CC able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is
CC not able to bind H4 butyrylated at 'Lys-5' (H4K5ac).
CC {ECO:0000250|UniProtKB:Q91Y44}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91Y44}.
CC Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q91Y44}.
CC -!- DOMAIN: Bromo domains mediate interaction with histones that have
CC acetylated lysine residues at specific positions. Bromo domain 1
CC mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8'
CC (H4K5ac and H4K8ac, respectively). The bromo domains also recognize and
CC bind a subset of butyrylated histones: able to bind histone H4
CC butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4
CC butyrylated at 'Lys-5' (H4K5ac). {ECO:0000250|UniProtKB:Q91Y44}.
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DR EMBL; BX927081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1QW93; -.
DR SMR; F1QW93; -.
DR PRIDE; F1QW93; -.
DR ZFIN; ZDB-GENE-030131-5928; brdt.
DR InParanoid; F1QW93; -.
DR PRO; PR:F1QW93; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140566; F:histone reader activity; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0051039; P:positive regulation of transcription involved in meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR CDD; cd05497; Bromo_Brdt_I_like; 1.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR031354; BRD4_CDT.
DR InterPro; IPR043508; Bromo_Brdt_I.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF17105; BRD4_CDT; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 3: Inferred from homology;
KW Activator; Bromodomain; Chromatin regulator; Coiled coil; Differentiation;
KW Meiosis; Nucleus; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation.
FT CHAIN 1..918
FT /note="Bromodomain testis-specific protein"
FT /id="PRO_0000420475"
FT DOMAIN 46..118
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 287..359
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 496..578
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 426..452
FT /evidence="ECO:0000255"
FT COILED 815..902
FT /evidence="ECO:0000255"
FT MOTIF 204..215
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q58F21"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 111
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT SITE 116
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
SQ SEQUENCE 918 AA; 103105 MW; 33E70155A3FAD2C8 CRC64;
MSDVKPPQHF TMNGNPPPPE FKNPKKPGRL TNHLQYIEKV VIRALWKHHF SWPFRQPVDA
VRLNLPDYYT IIKNPMDLTT IRKRLENNYY WKAMECVEDF NTMFTNCYVY NRPGDDIVLM
AQVLEKLFLE KVAEMPEEEY EISALTTKGP VKGARKSTIG LKKRPPSPMS EVVFQQTVTV
IPPDALHTIP SAPLSAQLTA KLKNGVKRKA DTTTPSASSI PSCESSSCVT EPKVLKLFSR
RGSGRPIKPP CKDLPESPPQ HQVGRRTKLS ERLKYCNAIL KEMFSKKHSA YAWPFYKPVD
AETLGLLDYH EIIHQPMDMS TIKKKMEARE YTDALQFAAD MRLMFSNCYK YNPPGHEVVS
MARKLQDVFE FRFSKIPDEP KNANPVSSHN RVKKERARSP SSSESSDSES SSPENSSDTE
EEDEEERAHR LASLEEQQLK AVREQLQLLT QTPLSKILKR SSSSKSSGCK VCTMMNSLKK
PKFNSVLRRK ESRACDSEEE MNTLPMSYEE KRQLSLDINK LPGDKLGKVV NIIKAREPLL
RDTDPEEIEI DFETLKPSTL RALECYVVGC LRKKKNKPPK KSKIKEKDKD LQHATGEQNS
HKKTKIETDG EIKDTTHPSR LSDSSSSSSS SDSSSSDSSS SDSCDSDSGL TEQKTKRKQS
KGPGHANKIK KKKYYPVVPL PEQALRQANA EVKDSSSASG VMCQSRPSSL VSETGSKDLF
ASQHAKHPVE DITAITGIPP LLSPLTSPSA AMPATGSQST SSSQFEASSP LCLYKDIVLK
HADSWTSLGK LATQTPCTIK SSKESFQQFR KVAMEKELTT ASRGLVSKHC LTQQPQKAKL
ECQPSKPEVE SAELPLMAAI LDTPKAPEPS SVLQNSVDRE REMARKREQE RRRREAMSGV
IDMTMQRDIM ATFEKNLE
