THA_CHICK
ID THA_CHICK Reviewed; 408 AA.
AC P04625;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Thyroid hormone receptor alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1;
GN Name=THRA; Synonyms=NR1A1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SPAFAS;
RX PubMed=2879242; DOI=10.1038/324635a0;
RA Sap J., Munoz A., Damm K., Ghysdael J., Leutz A., Beug H., Vennstroem B.;
RT "The c-erb-A protein is a high-affinity receptor for thyroid hormone.";
RL Nature 324:635-640(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
RX PubMed=3036525; DOI=10.1111/j.1432-1033.1987.tb13484.x;
RA Zahraoui A., Cuny G.;
RT "Nucleotide sequence of the chicken proto-oncogene c-erbA corresponding to
RT domain 1 of v-erbA.";
RL Eur. J. Biochem. 166:63-69(1987).
RN [3]
RP PHOSPHORYLATION AT SER-28.
RX PubMed=2903825; DOI=10.1002/j.1460-2075.1988.tb03088.x;
RA Goldberg Y., Glineur C., Gesquiere J.C., Ricouart A., Sap J., Vennstrom B.,
RA Ghysdael J.;
RT "Activation of protein kinase C or cAMP-dependent protein kinase increases
RT phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the
RT v-erbA-encoded protein.";
RL EMBO J. 7:2425-2433(1988).
RN [4]
RP PHOSPHORYLATION AT SER-12.
RX PubMed=2552374;
RA Glineur C., Bailly M., Ghysdael J.;
RT "The c-erbA alpha-encoded thyroid hormone receptor is phosphorylated in its
RT amino terminal domain by casein kinase II.";
RL Oncogene 4:1247-1254(1989).
RN [5]
RP INTERACTION WITH SFPQ.
RX PubMed=11259580; DOI=10.1128/mcb.21.7.2298-2311.2001;
RA Mathur M., Tucker P.W., Samuels H.H.;
RT "PSF is a novel corepressor that mediates its effect through Sin3A and the
RT DNA binding domain of nuclear hormone receptors.";
RL Mol. Cell. Biol. 21:2298-2311(2001).
CC -!- FUNCTION: Nuclear hormone receptor that can act as a repressor or
CC activator of transcription. High affinity receptor for thyroid
CC hormones, including triiodothyronine and thyroxine.
CC -!- SUBUNIT: Probably interacts with SFPQ. {ECO:0000269|PubMed:11259580}.
CC -!- INTERACTION:
CC P04625; P19793: RXRA; Xeno; NbExp=4; IntAct=EBI-286261, EBI-78598;
CC P04625; P23246-1: SFPQ; Xeno; NbExp=2; IntAct=EBI-286261, EBI-355463;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; X04854; CAA28545.1; -; Genomic_DNA.
DR EMBL; Y00987; CAA68792.1; -; mRNA.
DR PIR; A25236; TVCHVR.
DR RefSeq; NP_990644.1; NM_205313.1.
DR PDB; 3UVV; X-ray; 2.95 A; A=148-408.
DR PDBsum; 3UVV; -.
DR AlphaFoldDB; P04625; -.
DR SMR; P04625; -.
DR ComplexPortal; CPX-704; RXRalpha-TRalpha nuclear hormone receptor complex.
DR DIP; DIP-32625N; -.
DR IntAct; P04625; 5.
DR STRING; 9031.ENSGALP00000000351; -.
DR BindingDB; P04625; -.
DR iPTMnet; P04625; -.
DR PaxDb; P04625; -.
DR Ensembl; ENSGALT00000052263; ENSGALP00000052375; ENSGALG00000040017.
DR Ensembl; ENSGALT00000058539; ENSGALP00000050455; ENSGALG00000040017.
DR GeneID; 396251; -.
DR KEGG; gga:396251; -.
DR CTD; 7067; -.
DR VEuPathDB; HostDB:geneid_396251; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157917; -.
DR InParanoid; P04625; -.
DR OMA; IMCLRIA; -.
DR PhylomeDB; P04625; -.
DR PRO; PR:P04625; -.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000040017; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; P04625; baseline.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:AgBase.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50252; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00546; THYROIDHORMR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..408
FT /note="Thyroid hormone receptor alpha"
FT /id="PRO_0000053431"
FT DOMAIN 161..405
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 51..125
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 51..71
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 89..113
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..50
FT /note="Modulating"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 226
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT BINDING 275
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT MOD_RES 12
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:2552374"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2903825"
FT TURN 148..152
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:3UVV"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3UVV"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 210..233
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 244..262
FT /evidence="ECO:0007829|PDB:3UVV"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:3UVV"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3UVV"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:3UVV"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:3UVV"
FT TURN 288..292
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:3UVV"
FT TURN 304..308
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:3UVV"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 334..354
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 368..389
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:3UVV"
SQ SEQUENCE 408 AA; 46757 MW; AA7DB6B73322BAA4 CRC64;
MEQKPSTLDP LSEPEDTRWL DGKRKRKSSQ CLVKSSMSGY IPSYLDKDEQ CVVCGDKATG
YHYRCITCEG CKGFFRRTIQ KNLHPTYSCK YDGCCVIDKI TRNQCQLCRF KKCISVGMAM
DLVLDDSKRV AKRKLIEENR ERRRKEEMIK SLQHRPSPSA EEWELIHVVT EAHRSTNAQG
SHWKQKRKFL PEDIGQSPMA SMPDGDKVDL EAFSEFTKII TPAITRVVDF AKKLPMFSEL
PCEDQIILLK GCCMEIMSLR AAVRYDPESE TLTLSGEMAV KREQLKNGGL GVVSDAIFDL
GKSLSAFNLD DTEVALLQAV LLMSSDRTGL ICVDKIEKCQ ETYLLAFEHY INYRKHNIPH
FWPKLLMKVT DLRMIGACHA SRFLHMKVEC PTELFPPLFL EVFEDQEV
