BRDT_MACFA
ID BRDT_MACFA Reviewed; 947 AA.
AC Q4R8Y1; G7NTN6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 3.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Bromodomain testis-specific protein;
GN Name=BRDT; ORFNames=QtsA-11165;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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 SMARCE1 (By similarity). Interacts with mRNA
CC splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP. Interacts
CC with the acetylated N-terminus of histone H1, H2, H3 and H4. Interacts
CC with P-TEFb components CDK9 and CCNT1/cyclin-T1 (By similarity).
CC {ECO:0000250|UniProtKB:Q58F21, ECO:0000250|UniProtKB:Q91Y44}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91Y44}.
CC Note=Detected on chromatin. Excluded from the chromocenter.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE00440.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EHH50073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB168316; BAE00440.1; ALT_FRAME; mRNA.
DR EMBL; CM001276; EHH50073.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q4R8Y1; -.
DR SMR; Q4R8Y1; -.
DR STRING; 9541.XP_005542805.1; -.
DR eggNOG; KOG1474; Eukaryota.
DR Proteomes; UP000009130; Chromosome 1.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; 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; ISS:UniProtKB.
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:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..947
FT /note="Bromodomain testis-specific protein"
FT /id="PRO_0000239226"
FT DOMAIN 44..116
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 500..582
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 395..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..470
FT /evidence="ECO:0000255"
FT MOTIF 209..220
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q58F21"
FT COMPBIAS 395..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 109
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT SITE 114
FT /note="Histone H4K5ac binding"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y44"
FT CONFLICT 127
FT /note="V -> M (in Ref. 1; BAE00440)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="M -> R (in Ref. 1; BAE00440)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="D -> A (in Ref. 1; BAE00440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 107832 MW; 157821F2E105E01F CRC64;
MSLPSRQTAI IVNPPPPEYI NTKKNGRLTN QLQYLQKVVL KDLWKHSFSW PFQRPVDAVK
LKLPDYYTII KNPMDLNTIK KRLENKYYVK ASECIEDFNT MFSNCYLYNK PGDDIVLMAQ
ALEKLFVQKL SQMPQEEQVV GGKERIKKGT QQNIAVFSAK EKSSPNATEK VFKQQAIPSV
FPKTSVSPLN VAQGASVNSS SQSVAQVTKG VKRKADTTTP ATSVVKASSE FSPTFTEKSV
TLPPIKENMP KNVLPDSQQQ YNVVKSVKVT EQLRHCSEIL KEMLAKKHFS YAWPFYNPVD
VNALGLHNYY DIVKNPMDLG TIKEKMDNQE YKDAYKFAAD VRLMFMNCYK YNPPDHEVVT
MARMLQDVFE THFSKIPVEP VESMPLCYIK TDITETTGRE NTNEASSEGN SSGDSEDERV
QRLAKLQEQL KAVHQQLQVL SQVPFRKLNK KKEKSKKEKK KEKVNNSNEN PRKMCEQMRL
KEKSKRNQPK KRKQQYIGQK SEDEDNAKPM NYDEKRQLSL NINKLPGDKL GRVVHIIQSR
EPSLSNSNPD EIEIDFETLK ASTLRELEKY VSACLRKRPL KPPAKKIMMS KEELHSQKKQ
ELEKRLLDVN NQLNSRKRQT KSEKTQPSKA VGSVSRLSES SSSSSSSSES ESSSSDLSSS
DSSGSESEMF PKFTEVKPND SPSKENVKKM KNECILPEGR IGITQIECSV QDKTSANTTL
VHQTTPSHVM PPNHHQLAFN YQELEHLQTV KNISPLQILP PSGDSEQLSN GITVMHPSGD
NATTMLESEC QAPVQKDIKI KNADSWKSLG KSVKPSGVMK SSDELFNQFR KAAIEKEVKA
RTQELIRKHL EQNTKEPKVS QENQRDLGNG LTVESFSNKI QNKCSGEEQK EHQQSLEAQD
KSKLWLLKDR NLAREKEQER RRREAMAGTI DMTLQSDIMT MFENNFD
