TR150_XENLA
ID TR150_XENLA Reviewed; 951 AA.
AC Q5BJ39;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Thyroid hormone receptor-associated protein 3;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component;
DE Short=Trap150;
GN Name=thrap3; Synonyms=trap150;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in pre-mRNA splicing. Involved in nuclear mRNA
CC decay. Initially thought to play a role in transcriptional coactivation
CC through its association with the TRAP complex; however, it is not
CC regarded as a stable Mediator complex subunit. May play a role in the
CC positive regulation of the circadian clock.
CC {ECO:0000250|UniProtKB:Q569Z6}.
CC -!- SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator
CC complex-like). {ECO:0000250|UniProtKB:Q9Y2W1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q569Z6}.
CC -!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
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DR EMBL; BC091635; AAH91635.1; -; mRNA.
DR RefSeq; NP_001184195.1; NM_001197266.1.
DR AlphaFoldDB; Q5BJ39; -.
DR MaxQB; Q5BJ39; -.
DR PRIDE; Q5BJ39; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR026667; THRAP3.
DR InterPro; IPR029199; THRAP3_BCLAF1.
DR PANTHER; PTHR15268; PTHR15268; 1.
DR PANTHER; PTHR15268:SF16; PTHR15268:SF16; 1.
DR Pfam; PF15440; THRAP3_BCLAF1; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; Biological rhythms; Developmental protein;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..951
FT /note="Thyroid hormone receptor-associated protein 3"
FT /id="PRO_0000235982"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549..556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 951 AA; 108204 MW; 66FB2B80076518B7 CRC64;
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS RKRRLSSRSR SRSYSPAHNR
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RLSSNHSRVE SSKRKSTKEK
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDIKGSESS KPWPDATTYG AGSASRASVS
DLSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG
QFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYSKRYLE EQKTENGKDK
EQKQTNADKE KLKEKGGFSD ADVKMKSDPF APKTDSEKPF RGSQSPKRYK LRDDFEKKMA
DFHKEELDEH DKDKSKGRKE PEFDDEPKFM SKVIAGASKN QEEEKSGKWE SLHTGKEKQR
KAEEMEDEPF TERSRKEERG GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE
SRDKLGSKGD FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK
EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER FTKYLKRGNE
QEAAKNKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG YKAEGKYKDD PVDLRLDIER
RKKHKERDLK RGKSRESVDS RDSSHSRERS TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS
SQSSHSYKAE EYPEEAEERE ESTSGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG
RGNYSGNNNN NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MGRGRGRGAF
PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA E