ID   THA_MOUSE               Reviewed;         492 AA.
AC   P63058; A3KFN4; P10685; P15827; P16416; P37241; Q542U8; Q63107; Q63195;
AC   Q63196; Q80Y90; Q99146;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=Thyroid hormone receptor alpha;
DE   AltName: Full=Nuclear receptor subfamily 1 group A member 1;
DE   AltName: Full=c-erbA-1;
DE   AltName: Full=c-erbA-alpha;
GN   Name=Thra; Synonyms=C-erba-alpha, Nr1a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1), AND NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 1-452 (ISOFORMS ALPHA-2 AND ALPHA-3).
RC   STRAIN=C3H/HeJ; TISSUE=Muscle;
RX   PubMed=3399404; DOI=10.1093/nar/16.13.6248;
RA   Prost E., Koenig R.J., Moore D.D., Larsen P.R., Whalen R.G.;
RT   "Multiple sequences encoding potential thyroid hormone receptors isolated
RT   from mouse skeletal muscle cDNA libraries.";
RL   Nucleic Acids Res. 16:6248-6248(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
RC   STRAIN=C3H/HeJ; TISSUE=Testis;
RX   PubMed=2349106; DOI=10.1093/nar/18.10.3055;
RA   Masuda M., Yasuhara S., Yamashita M., Shibuya M., Odaka T.;
RT   "Nucleotide sequence of the murine thyroid hormone receptor (alpha-1)
RT   cDNA.";
RL   Nucleic Acids Res. 18:3055-3055(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH C1D.
RX   PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA   Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.;
RT   "Cloning and characterization of a corepressor and potential component of
RT   the nuclear hormone receptor repression complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
RN   [8]
RP   INTERACTION WITH NCOA6.
RX   PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
RA   Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
RT   "Cloning and characterization of RAP250, a nuclear receptor coactivator.";
RL   J. Biol. Chem. 275:5308-5317(2000).
RN   [9]
RP   ALTERNATIVE SPLICING (ISOFORMS ALPHA-1 AND ALPHA-DELTAE6), POTENTIAL RNA
RP   EDITING OF ISOFORM ALPHA-DELTAE6, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16322094; DOI=10.1210/me.2005-0074;
RA   Casas F., Busson M., Grandemange S., Seyer P., Carazo A., Pessemesse L.,
RA   Wrutniak-Cabello C., Cabello G.;
RT   "Characterization of a novel thyroid hormone receptor alpha variant
RT   involved in the regulation of myoblast differentiation.";
RL   Mol. Endocrinol. 20:749-763(2006).
RN   [10]
RP   INTERACTION WITH TACC1, AND SUBCELLULAR LOCATION (ISOFORM ALPHA-2).
RX   PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA   Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT   "The transforming acidic coiled coil (TACC1) protein modulates the
RT   transcriptional activity of the nuclear receptors TR and RAR.";
RL   BMC Mol. Biol. 11:3-3(2010).
RN   [11]
RP   INTERACTION WITH PER2.
RX   PubMed=20159955; DOI=10.1101/gad.564110;
RA   Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.;
RT   "The mammalian clock component PERIOD2 coordinates circadian output by
RT   interaction with nuclear receptors.";
RL   Genes Dev. 24:345-357(2010).
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. Isoform Alpha-
CC       deltaE6 does not bind DNA, inhibits the activity of isoform Alpha-1,
CC       and stimulates myoblast differentiation. {ECO:0000269|PubMed:16322094}.
CC   -!- SUBUNIT: Binds DNA as a dimer; homodimer and heterodimer with RXRB.
CC       Interacts with NCOA3 and NCOA6 coactivators, leading to a strong
CC       increase of transcription of target genes. Probably interacts with
CC       SFPQ. Interacts with AKAP13. Interacts with C1D. Interacts with
CC       TP53INP2. Interacts with PER2. Isoform alpha-2 and isoform alpha-1
CC       interact with TACC1, but the interaction with alpha-1 is much weaker.
CC       The interaction with isoform alpha-1, but not alpha-2, is decreased in
CC       the presence of thyroid hormone T3 (PubMed:20078863).
CC       {ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:20078863,
CC       ECO:0000269|PubMed:20159955, ECO:0000269|PubMed:9405624}.
CC   -!- INTERACTION:
CC       P63058; D4A055: Cacnb4; Xeno; NbExp=2; IntAct=EBI-6935292, EBI-8028403;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SUBCELLULAR LOCATION: [Isoform Alpha-deltaE6]: Cytoplasm.
CC       Note=Sequesters isoform Alpha-1 into this compartment.
CC   -!- SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm
CC       {ECO:0000269|PubMed:20078863}. Nucleus {ECO:0000269|PubMed:20078863}.
CC       Note=When overexpressed found in the cytoplasm where it colocalizes
CC       with TACC1. {ECO:0000269|PubMed:20078863}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Alpha-2;
CC         IsoId=P63058-1, P15827-1; Sequence=Displayed;
CC       Name=Alpha-1;
CC         IsoId=P63058-2, P15827-2; Sequence=VSP_003624;
CC       Name=Alpha-3;
CC         IsoId=P63058-3, P15827-3; Sequence=VSP_003625;
CC       Name=Alpha-deltaE6;
CC         IsoId=P63058-4; Sequence=VSP_038640, VSP_003624;
CC   -!- TISSUE SPECIFICITY: Ubiquitous (Isoform Alpha-deltaE6).
CC       {ECO:0000269|PubMed:16322094}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain. Isoform
CC       Alpha-deltaE6 lacks the hinge region that connects the modulating
CC       domain and the DNA binding domain.
CC   -!- MISCELLANEOUS: [Isoform Alpha-2]: Does not bind thyroid hormone T3.
CC       {ECO:0000305|PubMed:20078863}.
CC   -!- MISCELLANEOUS: [Isoform Alpha-deltaE6]: Due to mismatches with the
CC       underlying genomic sequence that lie within a microexon, this isoform
CC       has been proposed to undergo RNA editing involving both base insertion
CC       and deletion. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM46188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X07750; CAA30575.1; -; mRNA.
DR   EMBL; X07751; CAA30576.1; -; mRNA.
DR   EMBL; X07752; CAA30577.1; -; mRNA.
DR   EMBL; X51983; CAA36241.1; -; mRNA.
DR   EMBL; AK078233; BAC37186.1; -; mRNA.
DR   EMBL; AL590963; CAM46188.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL590963; CAM46189.1; -; Genomic_DNA.
DR   EMBL; AL590963; CAM46190.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL16164.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL16165.1; -; Genomic_DNA.
DR   EMBL; BC046795; AAH46795.1; -; mRNA.
DR   CCDS; CCDS25362.1; -. [P63058-2]
DR   CCDS; CCDS83893.1; -.
DR   PIR; S14416; S14416.
DR   PIR; S14417; S14417.
DR   PIR; S14418; S14418.
DR   PIR; S14690; QRMSA1.
DR   RefSeq; NP_001300912.1; NM_001313983.1. [P63058-1]
DR   RefSeq; NP_835161.1; NM_178060.4. [P63058-2]
DR   AlphaFoldDB; P63058; -.
DR   SMR; P63058; -.
DR   BioGRID; 204183; 10.
DR   ComplexPortal; CPX-713; RXRalpha-TRalpha nuclear hormone receptor complex. [P63058-2]
DR   DIP; DIP-43752N; -.
DR   IntAct; P63058; 5.
DR   MINT; P63058; -.
DR   STRING; 10090.ENSMUSP00000068281; -.
DR   iPTMnet; P63058; -.
DR   PhosphoSitePlus; P63058; -.
DR   MaxQB; P63058; -.
DR   PaxDb; 10090-ENSMUSP00000099428; -.
DR   ProteomicsDB; 262770; -.
DR   ProteomicsDB; 262771; -. [P63058-2]
DR   ProteomicsDB; 262772; -. [P63058-3]
DR   ProteomicsDB; 262773; -. [P63058-4]
DR   ABCD; P63058; 1 sequenced antibody.
DR   Antibodypedia; 1300; 762 antibodies from 44 providers.
DR   DNASU; 21833; -.
DR   Ensembl; ENSMUST00000064187.12; ENSMUSP00000068281.6; ENSMUSG00000058756.14. [P63058-1]
DR   Ensembl; ENSMUST00000103139.11; ENSMUSP00000099428.5; ENSMUSG00000058756.14. [P63058-2]
DR   GeneID; 21833; -.
DR   KEGG; mmu:21833; -.
DR   UCSC; uc007lhe.1; mouse. [P63058-2]
DR   UCSC; uc007lhf.1; mouse.
DR   UCSC; uc007lhg.1; mouse. [P63058-3]
DR   AGR; MGI:98742; -.
DR   CTD; 7067; -.
DR   MGI; MGI:98742; Thra.
DR   VEuPathDB; HostDB:ENSMUSG00000058756; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000157917; -.
DR   HOGENOM; CLU_007368_18_0_1; -.
DR   InParanoid; P63058; -.
DR   OMA; QCSVKSS; -.
DR   OrthoDB; 5390715at2759; -.
DR   PhylomeDB; P63058; -.
DR   TreeFam; TF328382; -.
DR   Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR   BioGRID-ORCS; 21833; 5 hits in 80 CRISPR screens.
DR   PRO; PR:P63058; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P63058; Protein.
DR   Bgee; ENSMUSG00000058756; Expressed in entorhinal cortex and 260 other cell types or tissues.
DR   ExpressionAtlas; P63058; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ComplexPortal.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0140296; F:general transcription initiation factor binding; ISO:MGI.
DR   GO; GO:0001161; F:intronic transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR   GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR   GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0008050; P:female courtship behavior; IMP:MGI.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:2000143; P:negative regulation of DNA-templated transcription initiation; ISO:MGI.
DR   GO; GO:0017055; P:negative regulation of RNA polymerase II transcription preinitiation complex assembly; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0001503; P:ossification; IMP:MGI.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045925; P:positive regulation of female receptivity; IMP:MGI.
DR   GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; IDA:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0050994; P:regulation of lipid catabolic process; IMP:MGI.
DR   GO; GO:0033032; P:regulation of myeloid cell apoptotic process; IMP:MGI.
DR   GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0009409; P:response to cold; IMP:MGI.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030878; P:thyroid gland development; IGI:MGI.
DR   GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0060509; P:type I pneumocyte differentiation; IGI:MGI.
DR   CDD; cd06961; NR_DBD_TR; 1.
DR   CDD; cd06935; NR_LBD_TR; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
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   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF42; THYROID HORMONE RECEPTOR ALPHA; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   Genevisible; P63058; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Receptor; Reference proteome; RNA editing; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..492
FT                   /note="Thyroid hormone receptor alpha"
FT                   /id="PRO_0000053425"
FT   DOMAIN          163..407
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        53..127
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         53..73
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         91..115
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..52
FT                   /note="Modulating"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         228
FT                   /ligand="3,3',5-triiodo-L-thyronine"
FT                   /ligand_id="ChEBI:CHEBI:533015"
FT                   /evidence="ECO:0000250|UniProtKB:P10827"
FT   BINDING         277
FT                   /ligand="3,3',5-triiodo-L-thyronine"
FT                   /ligand_id="ChEBI:CHEBI:533015"
FT                   /evidence="ECO:0000250|UniProtKB:P10827"
FT   VAR_SEQ         121..197
FT                   /note="AMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHVAT
FT                   EAHRSTNAQGSHWKQRRKFLPDDIG -> GTSP (in isoform
FT                   Alpha-deltaE6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038640"
FT   VAR_SEQ         371..492
FT                   /note="EREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGE
FT                   AGSLRGPVLQHQSPKSPQQRLLELLHRSGILHSRAVCGEDDSSEASSLSSSSDTEDTEV
FT                   CEDQAGKAASP -> VTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFEDQEV (in
FT                   isoform Alpha-1 and isoform Alpha-deltaE6)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:2349106, ECO:0000303|PubMed:3399404"
FT                   /id="VSP_003624"
FT   VAR_SEQ         371..409
FT                   /note="Missing (in isoform Alpha-3)"
FT                   /evidence="ECO:0000303|PubMed:3399404"
FT                   /id="VSP_003625"
FT   CONFLICT        106
FT                   /note="Q -> H (in Ref. 2; CAA36241)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  55023 MW;  870100FCB5C34A10 CRC64;
     MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCPLKSSMS GYIPSYLDKD EQCVVCGDKA
     TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID KITRNQCQLC RFKKCIAVGM
     AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM IRSLQQRPEP TPEEWDLIHV ATEAHRSTNA
     QGSHWKQRRK FLPDDIGQSP IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS
     ELPCEDQIIL LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF
     ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE HYVNHRKHNI
     PHFWPKLLMK EREVQSSILY KGAAAEGRPG GSLGVHPEGQ QLLGMHVVQG PQVRQLEQQL
     GEAGSLRGPV LQHQSPKSPQ QRLLELLHRS GILHSRAVCG EDDSSEASSL SSSSDTEDTE
     VCEDQAGKAA SP
//