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Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (c-erbA-1) (c-erbA-alpha)

 THA_MOUSE               Reviewed;         492 AA.
P63058; A3KFN4; P10685; P15827; P16416; P37241; Q542U8; Q63107;
Q63195; Q63196; Q80Y90; Q99146;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 2.
22-NOV-2017, entry version 140.
RecName: Full=Thyroid hormone receptor alpha;
AltName: Full=Nuclear receptor subfamily 1 group A member 1;
AltName: Full=c-erbA-1;
AltName: Full=c-erbA-alpha;
Name=Thra; Synonyms=C-erba-alpha, Nr1a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1), AND NUCLEOTIDE SEQUENCE
[MRNA] OF 1-452 (ISOFORMS ALPHA-2 AND ALPHA-3).
STRAIN=C3H/HeJ; TISSUE=Muscle;
PubMed=3399404; DOI=10.1093/nar/16.13.6248;
Prost E., Koenig R.J., Moore D.D., Larsen P.R., Whalen R.G.;
"Multiple sequences encoding potential thyroid hormone receptors
isolated from mouse skeletal muscle cDNA libraries.";
Nucleic Acids Res. 16:6248-6248(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
STRAIN=C3H/HeJ; TISSUE=Testis;
PubMed=2349106; DOI=10.1093/nar/18.10.3055;
Masuda M., Yasuhara S., Yamashita M., Shibuya M., Odaka T.;
"Nucleotide sequence of the murine thyroid hormone receptor (alpha-1)
cDNA.";
Nucleic Acids Res. 18:3055-3055(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH C1D.
PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G.,
Lazar M.A.;
"Cloning and characterization of a corepressor and potential component
of the nuclear hormone receptor repression complex.";
Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
[8]
INTERACTION WITH NCOA6.
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor
coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[9]
ALTERNATIVE SPLICING (ISOFORMS ALPHA-1 AND ALPHA-DELTAE6), POTENTIAL
RNA EDITING OF ISOFORM ALPHA-DELTAE6, FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=16322094; DOI=10.1210/me.2005-0074;
Casas F., Busson M., Grandemange S., Seyer P., Carazo A.,
Pessemesse L., Wrutniak-Cabello C., Cabello G.;
"Characterization of a novel thyroid hormone receptor alpha variant
involved in the regulation of myoblast differentiation.";
Mol. Endocrinol. 20:749-763(2006).
[10]
INTERACTION WITH PER2.
PubMed=20159955; DOI=10.1101/gad.564110;
Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.;
"The mammalian clock component PERIOD2 coordinates circadian output by
interaction with nuclear receptors.";
Genes Dev. 24:345-357(2010).
-!- FUNCTION: Nuclear hormone receptor that can act as a repressor or
activator of transcription. High affinity receptor for thyroid
hormones, including triiodothyronine and thyroxine. Isoform Alpha-
deltaE6 does not bind DNA, inhibits the activity of isoform Alpha-
1, and stimulates myoblast differentiation.
{ECO:0000269|PubMed:16322094}.
-!- SUBUNIT: Binds DNA as a dimer; homodimer and heterodimer with
RXRB. Interacts with NCOA3 and NCOA6 coactivators, leading to a
strong increase of transcription of target genes. Probably
interacts with SFPQ. Interacts with AKAP13. Interacts with C1D.
Interacts with TP53INP2. Interacts with PER2.
{ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:20159955,
ECO:0000269|PubMed:9405624}.
-!- INTERACTION:
D4A055:Cacnb4 (xeno); NbExp=2; IntAct=EBI-6935292, EBI-8028403;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform Alpha-deltaE6: Cytoplasm.
Note=Sequesters isoform Alpha-1 into this compartment.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Alpha-2;
IsoId=P63058-1, P15827-1;
Sequence=Displayed;
Name=Alpha-1;
IsoId=P63058-2, P15827-2;
Sequence=VSP_003624;
Name=Alpha-3;
IsoId=P63058-3, P15827-3;
Sequence=VSP_003625;
Name=Alpha-deltaE6;
IsoId=P63058-4; Sequence=VSP_038640, VSP_003624;
Note=Due to mismatches with the underlying genomic sequence that
lie within a microexon, this isoform has been proposed to
undergo RNA editing involving both base insertion and deletion.;
-!- TISSUE SPECIFICITY: Ubiquitous (Isoform Alpha-deltaE6).
{ECO:0000269|PubMed:16322094}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
Isoform Alpha-deltaE6 lacks the hinge region that connects the
modulating domain and the DNA binding domain.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAM46188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X07750; CAA30575.1; -; mRNA.
EMBL; X07751; CAA30576.1; -; mRNA.
EMBL; X07752; CAA30577.1; -; mRNA.
EMBL; X51983; CAA36241.1; -; mRNA.
EMBL; AK078233; BAC37186.1; -; mRNA.
EMBL; AL590963; CAM46188.1; ALT_SEQ; Genomic_DNA.
EMBL; AL590963; CAM46189.1; -; Genomic_DNA.
EMBL; AL590963; CAM46190.1; -; Genomic_DNA.
EMBL; CH466556; EDL16164.1; -; Genomic_DNA.
EMBL; CH466556; EDL16165.1; -; Genomic_DNA.
EMBL; BC046795; AAH46795.1; -; mRNA.
CCDS; CCDS25362.1; -. [P63058-2]
CCDS; CCDS83893.1; -.
PIR; S14416; S14416.
PIR; S14417; S14417.
PIR; S14418; S14418.
PIR; S14690; QRMSA1.
RefSeq; NP_001300912.1; NM_001313983.1. [P63058-1]
RefSeq; NP_835161.1; NM_178060.4. [P63058-2]
UniGene; Mm.265917; -.
UniGene; Mm.442648; -.
ProteinModelPortal; P63058; -.
SMR; P63058; -.
BioGrid; 204183; 5.
DIP; DIP-43752N; -.
IntAct; P63058; 4.
MINT; MINT-3374329; -.
STRING; 10090.ENSMUSP00000099428; -.
iPTMnet; P63058; -.
PhosphoSitePlus; P63058; -.
MaxQB; P63058; -.
PaxDb; P63058; -.
PRIDE; P63058; -.
Ensembl; ENSMUST00000064187; ENSMUSP00000068281; ENSMUSG00000058756. [P63058-1]
Ensembl; ENSMUST00000103139; ENSMUSP00000099428; ENSMUSG00000058756. [P63058-2]
GeneID; 21833; -.
KEGG; mmu:21833; -.
UCSC; uc007lhe.1; mouse. [P63058-2]
UCSC; uc007lhf.1; mouse.
UCSC; uc007lhg.1; mouse. [P63058-3]
CTD; 7067; -.
MGI; MGI:98742; Thra.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOVERGEN; HBG005606; -.
InParanoid; P63058; -.
KO; K05547; -.
OMA; MEHMPKE; -.
OrthoDB; EOG091G0GC1; -.
PhylomeDB; P63058; -.
TreeFam; TF328382; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
PRO; PR:P63058; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000058756; -.
CleanEx; MM_THRA; -.
ExpressionAtlas; P63058; baseline and differential.
Genevisible; P63058; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
GO; GO:0032403; F:protein complex binding; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0002153; F:steroid receptor RNA activator RNA binding; IDA:MGI.
GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
GO; GO:0004887; F:thyroid hormone receptor activity; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0001502; P:cartilage condensation; IMP:MGI.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IDA:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO; GO:0008050; P:female courtship behavior; IMP:MGI.
GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; ISO:MGI.
GO; GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IC:ParkinsonsUK-UCL.
GO; GO:0045925; P:positive regulation of female receptivity; IMP:MGI.
GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
GO; GO:0050994; P:regulation of lipid catabolic process; IMP:MGI.
GO; GO:0033032; P:regulation of myeloid cell apoptotic process; IMP:MGI.
GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0009409; P:response to cold; IMP:MGI.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0060509; P:Type I pneumocyte differentiation; IGI:MGI.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001728; ThyrH_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
PRINTS; PR00546; THYROIDHORMR.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; DNA-binding;
Metal-binding; Nucleus; Receptor; Reference proteome; RNA editing;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 492 Thyroid hormone receptor alpha.
/FTId=PRO_0000053425.
DNA_BIND 53 127 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 53 73 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 91 115 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 52 Modulating.
REGION 190 370 Ligand-binding.
BINDING 228 228 Thyroid hormone. {ECO:0000250}.
BINDING 277 277 Thyroid hormone; via amide nitrogen.
{ECO:0000250}.
VAR_SEQ 121 197 AMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPT
PEEWDLIHVATEAHRSTNAQGSHWKQRRKFLPDDIG -> G
TSP (in isoform Alpha-deltaE6).
{ECO:0000305}.
/FTId=VSP_038640.
VAR_SEQ 371 492 EREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGP
QVRQLEQQLGEAGSLRGPVLQHQSPKSPQQRLLELLHRSGI
LHSRAVCGEDDSSEASSLSSSSDTEDTEVCEDQAGKAASP
-> VTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFEDQ
EV (in isoform Alpha-1 and isoform Alpha-
deltaE6). {ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2349106,
ECO:0000303|PubMed:3399404}.
/FTId=VSP_003624.
VAR_SEQ 371 409 Missing (in isoform Alpha-3).
{ECO:0000303|PubMed:3399404}.
/FTId=VSP_003625.
CONFLICT 106 106 Q -> H (in Ref. 2; CAA36241).
{ECO:0000305}.
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


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EIAAB42234 c-erbA-2,c-erbA-beta,Erba2,Mouse,Mus musculus,Nr1a2,Nuclear receptor subfamily 1 group A member 2,Thrb,Thyroid hormone receptor beta
EIAAB42233 c-erbA-2,c-erbA-beta,Erba2,Nr1a2,Nuclear receptor subfamily 1 group A member 2,Rat,Rattus norvegicus,Thrb,Thyroid hormone receptor beta
EIAAB42232 c-erbA-2,c-erbA-beta,ERBA2,Homo sapiens,Human,NR1A2,Nuclear receptor subfamily 1 group A member 2,THR1,THRB,Thyroid hormone receptor beta
EIAAB27773 EAR-1,Nr1d1,Nuclear receptor subfamily 1 group D member 1,Rat,Rattus norvegicus,Rev-erbA-alpha,V-erbA-related protein 1
EIAAB27776 Bos taurus,Bovine,EAR-1,NR1D1,Nuclear receptor subfamily 1 group D member 1,Rev-erbA-alpha,V-erbA-related protein 1
EIAAB27774 Ear1,EAR-1,Mouse,Mus musculus,Nr1d1,Nuclear receptor subfamily 1 group D member 1,Rev-erbA-alpha,V-erbA-related protein 1


 

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