THA_MOUSE
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 03-AUG-2022, entry version 169.
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;
CC Sequence=Displayed;
CC Name=Alpha-1;
CC IsoId=P63058-2, P15827-2;
CC Sequence=VSP_003624;
CC Name=Alpha-3;
CC IsoId=P63058-3, P15827-3;
CC 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.ENSMUSP00000099428; -.
DR iPTMnet; P63058; -.
DR PhosphoSitePlus; P63058; -.
DR MaxQB; P63058; -.
DR PaxDb; P63058; -.
DR PRIDE; P63058; -.
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; 662 antibodies from 44 providers.
DR DNASU; 21833; -.
DR Ensembl; ENSMUST00000064187; ENSMUSP00000068281; ENSMUSG00000058756. [P63058-1]
DR Ensembl; ENSMUST00000103139; ENSMUSP00000099428; ENSMUSG00000058756. [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 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; IMCLRIA; -.
DR OrthoDB; 1112927at2759; -.
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 75 CRISPR screens.
DR PRO; PR:P63058; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63058; protein.
DR Bgee; ENSMUSG00000058756; Expressed in entorhinal cortex and 257 other tissues.
DR ExpressionAtlas; P63058; baseline and differential.
DR Genevisible; P63058; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; 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:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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: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 Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 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 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 Alpha-
FT 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
