BRDT_XENTR
ID BRDT_XENTR Reviewed; 933 AA.
AC F7DRV9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Bromodomain testis-specific protein;
GN Name=brdt;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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; AAMC01026645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01026646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01026647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01026648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F7DRV9; -.
DR SMR; F7DRV9; -.
DR STRING; 8364.ENSXETP00000049781; -.
DR PaxDb; F7DRV9; -.
DR PRIDE; F7DRV9; -.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_001499_0_0_1; -.
DR InParanoid; F7DRV9; -.
DR OMA; FMQKIAQ; -.
DR TreeFam; TF317345; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; 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 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; 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; 1.
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..933
FT /note="Bromodomain testis-specific protein"
FT /id="PRO_0000420476"
FT DOMAIN 45..117
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 298..368
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 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 423..448
FT /evidence="ECO:0000255"
FT COILED 829..917
FT /evidence="ECO:0000255"
FT MOTIF 214..225
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q58F21"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 110
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT SITE 115
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
SQ SEQUENCE 933 AA; 105992 MW; 0CEAF6CE7F63D475 CRC64;
MSMSSRHLHS SIVNPPPPEY INRKKTGRLT NQLQYLEKVV LKALWRHHFS WPFQQPVDAA
KLNLPDYYQI IKNPMDLSTI RKRLEYNYYS KALDCIQDFN TMFTNCYIYN KPGDDIVVMS
QELEKVFMEK IAEMPHEEIE LSVVGNRGVK SRIKISAVAA EVCKKKMVSQ KMHRRTFPCP
VIAMMPKRTT LVPLSVIRSS TSSHSASSVS KVNKGIKRKA DTTTPAVSLI ATSCESSPTL
SEPKPNKILS GTEKTRSAET SAVDLPDSQH HIHFIKSNQI CEQLKHCNNI LNEMMSKKHA
EYAWPFYKTV IPTSLLDCSD AIKHPMDLAT IRDKMENGLY KDTQDFASDV RLMFMNSYKY
NPPDNEVVNM ARKMQDVFEG MFAKIPDDPL ATQSMVERYK TSTEESSSSS SSEQSSSSDS
EDERAQHLAL LQEQLRAVQE QLKALTETPI FSKIQPKSAV GVYDKYKQWV KCIEPMGKLL
KRKKNYDAKK KKLHVSDEEE DVKPMSYDEK RQLSLDINKL PGEKLGRIVH IIQSREPSLK
DSNPNEIEID FETLKQSTLR HLEKYVMVCL RKRPKKPSSI KSLKSKEQLN KEKKQELEKR
LRDVSGQLSS AKKPKIQGFL YPMQSIGGPS RLSESSTSSS ASDVSNSSDS SSSDSSDSES
ATFPKNILAK KQTSTNYEVP LLLYYGCFVN KPRTSIPQNG LCIGSQSLAY TTISTIVHPT
PMALMPLHPG STNYTSLQLL LKYGLHVPLI IENPLGNSVL FENYLEVLHP SQIEQTFAIK
EECLKPKYKN AKVKTSFCWE VFSKSLATTH VTIKSSSNSF QQFRKAAIAK EERERALKAQ
ELRRLEDSKA GMQEKLSPSL PMETKVHEMQ AQTIDEATKG EPTCNPVHEG ITEEERNLAR
MREQERRRRE AMAGTIDMYL QSDIMATFEE HLC
