ID THB_MOUSE Reviewed; 461 AA. AC P37242; P37244; Q0VDR8; Q3TY80; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 200. DE RecName: Full=Thyroid hormone receptor beta; DE AltName: Full=Nuclear receptor subfamily 1 group A member 2; DE AltName: Full=c-erbA-2; DE AltName: Full=c-erbA-beta; GN Name=Thrb; Synonyms=Erba2, Nr1a2; 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] (ISOFORMS BETA-1 AND BETA-2). RC TISSUE=Thyroid; RX PubMed=1944303; DOI=10.1210/mend-5-8-1049; RA Wood W.M., Ocran K.W., Gordon D.F., Ridgway E.C.; RT "Isolation and characterization of mouse complementary DNAs encoding alpha RT and beta thyroid hormone receptors from thyrotrope cells: the mouse RT pituitary-specific beta 2 isoform differs at the amino terminus from the RT corresponding species from rat pituitary tumor cells."; RL Mol. Endocrinol. 5:1049-1061(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DBA/2J; TISSUE=Liver; RX PubMed=7708051; DOI=10.1210/mend.8.12.7708051; RA Wood W.M., Dowding J.M., Haugen B.R., Bright T.M., Gordon D.F., RA Ridgway E.C.; RT "Structural and functional characterization of the genomic locus encoding RT the murine beta 2 thyroid hormone receptor."; RL Mol. Endocrinol. 8:1605-1617(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1). RC STRAIN=C57BL/6J; TISSUE=Visual cortex; 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 MRNA] (ISOFORM BETA-2). RC STRAIN=C57BL/6J; TISSUE=Eye; 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 [5] 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). 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: Binds DNA as a dimer; homodimer and heterodimer with RXRB. CC Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and CC MED1/TRAP220 in a ligand-inducible manner. Interacts with the CC corepressor NCOR1 in absence of ligand (By similarity). Interacts with CC C1D. Interacts with NR2F6; the interaction impairs the binding of the CC THRB homodimer and THRB:RXRB heterodimer to T3 response elements. CC Interacts with PRMT2 and THRSP (By similarity). Interacts with TACC1; CC this interaction is decreased in the presence of thyroid hormone T3 (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10828}. CC -!- INTERACTION: CC P37242; O08915: Aip; NbExp=2; IntAct=EBI-6935043, EBI-6935014; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta-1; CC IsoId=P37242-1; Sequence=Displayed; CC Name=Beta-2; CC IsoId=P37242-2, P37244-1; Sequence=VSP_031078; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S62756; AAB20226.1; -; mRNA. DR EMBL; S62758; AAB20227.1; -; mRNA. DR EMBL; U15548; AAA86957.1; -; Genomic_DNA. DR EMBL; U15542; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; U15543; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; U15544; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; U15545; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; U15546; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; U15547; AAA86957.1; JOINED; Genomic_DNA. DR EMBL; AK158826; BAE34683.1; -; mRNA. DR EMBL; BC089035; AAH89035.1; -; mRNA. DR EMBL; BC119552; AAI19553.1; -; mRNA. DR EMBL; BC119553; AAI19554.1; -; mRNA. DR CCDS; CCDS26835.1; -. [P37242-2] DR CCDS; CCDS49404.1; -. [P37242-1] DR PIR; A40377; A40377. DR PIR; A57035; A57035. DR RefSeq; NP_001106888.1; NM_001113417.1. [P37242-1] DR RefSeq; NP_033406.1; NM_009380.3. [P37242-2] DR RefSeq; XP_006518029.1; XM_006517966.2. DR RefSeq; XP_006518030.1; XM_006517967.3. [P37242-1] DR RefSeq; XP_006518031.1; XM_006517968.3. DR RefSeq; XP_006518033.1; XM_006517970.3. [P37242-1] DR RefSeq; XP_006518034.1; XM_006517971.3. [P37242-1] DR RefSeq; XP_006518035.1; XM_006517972.3. [P37242-1] DR RefSeq; XP_011243039.1; XM_011244737.1. [P37242-1] DR RefSeq; XP_011243040.1; XM_011244738.2. DR RefSeq; XP_011243041.1; XM_011244739.2. DR RefSeq; XP_011243042.1; XM_011244740.2. [P37242-1] DR RefSeq; XP_011243043.1; XM_011244741.2. [P37242-1] DR RefSeq; XP_011243044.1; XM_011244742.1. [P37242-1] DR RefSeq; XP_011243045.1; XM_011244743.2. [P37242-1] DR RefSeq; XP_017171435.1; XM_017315946.1. DR RefSeq; XP_017171436.1; XM_017315947.1. DR AlphaFoldDB; P37242; -. DR SMR; P37242; -. DR BioGRID; 204184; 117. DR ComplexPortal; CPX-710; RXRalpha-TRbeta nuclear hormone receptor complex. DR DIP; DIP-43750N; -. DR IntAct; P37242; 5. DR MINT; P37242; -. DR STRING; 10090.ENSMUSP00000022304; -. DR PhosphoSitePlus; P37242; -. DR MaxQB; P37242; -. DR PaxDb; 10090-ENSMUSP00000022304; -. DR ProteomicsDB; 262913; -. [P37242-1] DR ProteomicsDB; 262914; -. [P37242-2] DR ABCD; P37242; 3 sequenced antibodies. DR Antibodypedia; 4548; 586 antibodies from 42 providers. DR DNASU; 21834; -. DR Ensembl; ENSMUST00000022303.17; ENSMUSP00000022303.10; ENSMUSG00000021779.20. [P37242-1] DR Ensembl; ENSMUST00000022304.12; ENSMUSP00000022304.11; ENSMUSG00000021779.20. [P37242-2] DR Ensembl; ENSMUST00000091471.12; ENSMUSP00000089053.5; ENSMUSG00000021779.20. [P37242-1] DR GeneID; 21834; -. DR KEGG; mmu:21834; -. DR UCSC; uc007shk.2; mouse. [P37242-1] DR UCSC; uc007sho.2; mouse. [P37242-2] DR AGR; MGI:98743; -. DR CTD; 7068; -. DR MGI; MGI:98743; Thrb. DR VEuPathDB; HostDB:ENSMUSG00000021779; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000156809; -. DR HOGENOM; CLU_007368_18_2_1; -. DR InParanoid; P37242; -. DR OMA; AASSNCY; -. DR OrthoDB; 5390715at2759; -. DR PhylomeDB; P37242; -. DR TreeFam; TF328382; -. DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway. DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors. DR BioGRID-ORCS; 21834; 4 hits in 82 CRISPR screens. DR ChiTaRS; Thrb; mouse. DR PRO; PR:P37242; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; P37242; Protein. DR Bgee; ENSMUSG00000021779; Expressed in auditory system and 85 other cell types or tissues. DR ExpressionAtlas; P37242; baseline and differential. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0004879; F:nuclear receptor activity; IMP:MGI. 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; ISO:MGI. DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB. DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI. DR GO; GO:0008050; P:female courtship behavior; IMP:MGI. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0007621; P:negative regulation of female receptivity; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:MGI. DR GO; GO:0045778; P:positive regulation of ossification; ISO:MGI. DR GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:MGI. DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:MGI. DR GO; GO:0097474; P:retinal cone cell apoptotic process; IMP:MGI. DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IBA:GO_Central. 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:SF210; THYROID HORMONE RECEPTOR BETA; 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; P37242; MM. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..461 FT /note="Thyroid hormone receptor beta" FT /id="PRO_0000053448" FT DOMAIN 217..461 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 107..181 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 107..127 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 145..169 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..106 FT /note="Modulating" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 244..461 FT /note="Interaction with NR2F6" FT /evidence="ECO:0000250" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 124 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 282 FT /ligand="3,3',5-triiodo-L-thyronine" FT /ligand_id="ChEBI:CHEBI:533015" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 282 FT /ligand="L-thyroxine" FT /ligand_id="ChEBI:CHEBI:58448" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 331 FT /ligand="3,3',5-triiodo-L-thyronine" FT /ligand_id="ChEBI:CHEBI:533015" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 331 FT /ligand="L-thyroxine" FT /ligand_id="ChEBI:CHEBI:58448" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 435 FT /ligand="3,3',5-triiodo-L-thyronine" FT /ligand_id="ChEBI:CHEBI:533015" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P10828" FT BINDING 435 FT /ligand="L-thyroxine" FT /ligand_id="ChEBI:CHEBI:58448" FT /evidence="ECO:0000250|UniProtKB:P10828" FT VAR_SEQ 1..93 FT /note="MTPNSMTENGLPAWDKQKPRPDRGQDWKLVGMSEACLHRKSHVERRGALKNE FT QTSPHLIQATWTSSIFHLDPDDVNDQSISSAQTFQTEEKKC -> MNYCMPEVHEVCPA FT ASSNCYMQVTDYLAYLEDSPALSGRDVQAVPSSSIYMEQAWAVNQPYTCSYPGNLFKSK FT DSDLDMALSQSSQPAHLPEEKPFPQVQSPPHSQK (in isoform Beta-2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1944303" FT /id="VSP_031078" FT CONFLICT 445 FT /note="E -> G (in Ref. 3; BAE34683)" FT /evidence="ECO:0000305" SQ SEQUENCE 461 AA; 52630 MW; 99089194FC3E6B33 CRC64; MTPNSMTENG LPAWDKQKPR PDRGQDWKLV GMSEACLHRK SHVERRGALK NEQTSPHLIQ ATWTSSIFHL DPDDVNDQSI SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR CITCEGCKGF FRRTIQKSLH PSYSCKYEGK CIIDKVTRNQ CQECRFKKCI YVGMATDLVL DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK QKRKFLPEDI GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED QIILLKGCCM EIMSLRAAVR YDPDSETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D //