BRDT_RAT
ID BRDT_RAT Reviewed; 952 AA.
AC D4A7T3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Bromodomain testis-specific protein;
GN Name=Brdt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH SMARCE1.
RX PubMed=22215678; DOI=10.1074/jbc.m111.288167;
RA Dhar S., Thota A., Rao M.R.;
RT "Insights into role of bromodomain, testis-specific (Brdt) in acetylated
RT histone H4-dependent chromatin remodeling in mammalian spermiogenesis.";
RL J. Biol. Chem. 287:6387-6405(2012).
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). Also acts as a
CC component of the splicing machinery in pachytene spermatocytes and
CC round spermatids and participates in 3'-UTR truncation of specific
CC mRNAs in post-meiotic spermatids. Required for chromocenter
CC organization, a structure comprised of peri-centromeric
CC heterochromatin. {ECO:0000250|UniProtKB:Q91Y44}.
CC -!- SUBUNIT: Interacts with the acetylated N-terminus of histone H1, H2, H3
CC and H4. Interacts with P-TEFb components CDK9 and CCNT1/cyclin-T1.
CC Interacts with mRNA splicing machinery proteins SRSF2, DDX5, HNRNPK and
CC TARDBP (By similarity). Interacts with SMARCE1 (PubMed:22215678).
CC {ECO:0000250|UniProtKB:Q58F21, ECO:0000250|UniProtKB:Q91Y44,
CC ECO:0000269|PubMed:22215678}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22215678}.
CC Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q91Y44}.
CC -!- DEVELOPMENTAL STAGE: Present in all stages of spermiogenesis, from
CC round to elongating spermatids (at protein level).
CC {ECO:0000269|PubMed:22215678}.
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 AlphaFoldDB; D4A7T3; -.
DR SMR; D4A7T3; -.
DR STRING; 10116.ENSRNOP00000058256; -.
DR PaxDb; D4A7T3; -.
DR PeptideAtlas; D4A7T3; -.
DR PRIDE; D4A7T3; -.
DR RGD; 1306678; Brdt.
DR eggNOG; KOG1474; Eukaryota.
DR InParanoid; D4A7T3; -.
DR TreeFam; TF317345; -.
DR PRO; PR:D4A7T3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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 1: Evidence at protein level;
KW Activator; Bromodomain; Chromatin regulator; Coiled coil; Differentiation;
KW Meiosis; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..952
FT /note="Bromodomain testis-specific protein"
FT /id="PRO_0000420474"
FT DOMAIN 43..115
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 286..358
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 495..577
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..442
FT /evidence="ECO:0000255"
FT COILED 837..936
FT /evidence="ECO:0000255"
FT MOTIF 208..219
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q58F21"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT SITE 113
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
SQ SEQUENCE 952 AA; 106719 MW; 0536239BE7E21B8B CRC64;
MSLPSRQMAI VNPPPPEYIN AKKTGRLTNQ LQFLQRVVLK ALWKHSFSWP FQQPVDAAKL
KLPDYYTIIE TPMDLSTIKK RLENRYYEKA SECVGDFNTM FSNCYLYNKP GDDIVVMAQA
LEKLFMQKLS QMPQEEQIVG GKERMKKDIQ QKTAVSSAKE QTPSKSAENV FKRQEIPAGF
PDVCLSPLNM AQEAPPTCDS QTVVQITKGV KRRADTTTPT TSSAKASSES PPPLREAKPA
NAPVKENTVK SVLPDSQQQH RVLKTVKVTE QLKHCSEILK EMLAKKHLPY AWPFYNPVDV
DALGLHNYYD IVKNPMDLGT IKGKMDKQEY KDACEFAADV RLMFMNCYKY NPPDHEVVTM
ARMLQDVFEM HFAKIPDEPV ESMRACHLTT NSAKALSRES SSEASSGDCS SEDSEDERVQ
RLAKLQEQLN AVHQQLQVLS QVPLRKLKKK NEKSKRAPKR KKVNRDENPK KKAKQMKQKE
KAKSNQPKKK KPLLKLEEED NAKPMNYDEK RQLSLDINKL PGDKLGRIVH IIQSREPSLR
NSNPDEIEID FETLKASTLR ELEKYVLACL RKRSLKPHAK KVVRSKEELH SEKKLELERR
LLDVNNQLNC RKRQTKRPAK VAVSPRPPLP PPPPPPPELA SGSRLSDSSS SSSSSGSGSS
SSSSSSSGSG SSSSDSSSSD SSDSEPEISP KFTGVKQNDL PSKENTKQIQ CSVPDITSAE
TALVQQSTGP CGAPGKPPQQ MPGCQVPHHL QATESTASVQ TQPLAGDCKR VLHGPPVVHA
SAESHTVLEL QCHAPVQKDI KIKNADSWKS LGKPVKASSV LKSSDELFNQ FRKAAIEKEV
KARTQEQIRK HLEHSAKDPK VSQESQREFG SGFTPESSSN KVQGRSHGEE QSEQQQLPSP
SETQDISKLW LLKDRNLARE KEQERRRREA MAGTIDMTLQ SDIMTMFENN FD
