THB_DANRE
ID THB_DANRE Reviewed; 395 AA.
AC Q9PVE4; A3QJW1; B3DIF2; O42560; Q90Y31;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Thyroid hormone receptor beta;
DE Short=TR-beta;
DE Short=TRb;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2;
DE AltName: Full=Thyroid hormone receptor beta-1;
DE Short=TRbeta1;
GN Name=thrb; Synonyms=nr1a2, trb; ORFNames=si:ch211-264a6.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10687864; DOI=10.1016/s0303-7207(99)00193-8;
RA Liu Y.-W., Lo L.-J., Chan W.-K.;
RT "Temporal expression and T3 induction of thyroid hormone receptors alpha1
RT and beta1 during early embryonic and larval development in zebrafish, Danio
RT rerio.";
RL Mol. Cell. Endocrinol. 159:187-195(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-97.
RX PubMed=9192646; DOI=10.1073/pnas.94.13.6803;
RA Escriva H., Safi R., Haenni C., Langlois M.-C., Saumitou-Laprade P.,
RA Stehelin D., Capron A., Pierce R., Laudet V.;
RT "Ligand binding was acquired during evolution of nuclear receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6803-6808(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-347 (ISOFORM 1).
RX PubMed=11174854; DOI=10.1677/jme.0.0260051;
RA Marchand O., Safi R., Escriva H., Van Rompaey E., Prunet P., Laudet V.;
RT "Molecular cloning and characterization of thyroid hormone receptors in
RT teleost fish.";
RL J. Mol. Endocrinol. 26:51-65(2001).
RN [6]
RP REVIEW.
RX PubMed=11738632; DOI=10.1016/s1532-0456(01)00271-x;
RA Power D.M., Llewellyn L., Faustino M., Nowell M.A., Bjoernsson B.T.,
RA Einarsdottir I.E., Canario A.V.M., Sweeney G.E.;
RT "Thyroid hormones in growth and development of fish.";
RL Comp. Biochem. Physiol. 130C:447-459(2001).
RN [7]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=11963654; DOI=10.1046/j.1432-0436.2002.700104.x;
RA Liu Y.-W., Chan W.-K.;
RT "Thyroid hormones are important for embryonic to larval transitory phase in
RT zebrafish.";
RL Differentiation 70:36-45(2002).
RN [8]
RP INTERACTION WITH NCOA2.
RX PubMed=18248177; DOI=10.1089/zeb.2005.2.33;
RA Tan J.-H., Quek S.-I., Chan W.-K.;
RT "Cloning, genomic organization, and expression analysis of zebrafish
RT nuclear receptor coactivator, TIF2.";
RL Zebrafish 2:33-46(2005).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=17418841; DOI=10.1016/j.ygcen.2007.02.020;
RA Walpita C.N., Van der Geyten S., Rurangwa E., Darras V.M.;
RT "The effect of 3,5,3'-triiodothyronine supplementation on zebrafish (Danio
RT rerio) embryonic development and expression of iodothyronine deiodinases
RT and thyroid hormone receptors.";
RL Gen. Comp. Endocrinol. 152:206-214(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17997606; DOI=10.1371/journal.pgen.0030188;
RA Bertrand S., Thisse B., Tavares R., Sachs L., Chaumot A., Bardet P.-L.,
RA Escriva H., Duffraisse M., Marchand O., Safi R., Thisse C., Laudet V.;
RT "Unexpected novel relational links uncovered by extensive developmental
RT profiling of nuclear receptor expression.";
RL PLoS Genet. 3:E188-E188(2007).
CC -!- FUNCTION: Nuclear hormone receptor that can act as a repressor or
CC activator of transcription. High affinity receptor for the thyroid
CC gland hormone triiodothyronine (T3). Transactivating activity is
CC ligand-dependent, and is repressed in the absence of T3.
CC {ECO:0000269|PubMed:10687864}.
CC -!- SUBUNIT: Interacts (via the ligand-binding domain) with ncoa2.
CC {ECO:0000269|PubMed:18248177}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9PVE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9PVE4-2; Sequence=VSP_035801;
CC -!- TISSUE SPECIFICITY: Widely expressed in a range of adult tissues
CC including the brain, eye, fin, gill, intestine, liver, swim bladder and
CC ovary. In the eye, expressed in the outer nuclear layer of the retina.
CC {ECO:0000269|PubMed:10687864, ECO:0000269|PubMed:17997606}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at the 1 cell stage (0 hpf) but disappears by the 2 cell
CC stage. Expressed again from the 16 cell stage onwards. Embryonic
CC expression increases dramatically around the hatching period. High
CC expression then continues until 6 dpf, before declining.
CC {ECO:0000269|PubMed:10687864, ECO:0000269|PubMed:11963654,
CC ECO:0000269|PubMed:17418841}.
CC -!- INDUCTION: By triiodothyronine (T3) and L-thyroxine (T4).
CC {ECO:0000269|PubMed:10687864, ECO:0000269|PubMed:11963654}.
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 -!- CAUTION: In contrast to PubMed:10687864 and PubMed:11963654,
CC PubMed:17418841 found that triiodothyronine (T3) did not induce
CC expression in the embryo. {ECO:0000305}.
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DR EMBL; AF109732; AAF14239.1; -; mRNA.
DR EMBL; BX927163; CAN87984.1; -; Genomic_DNA.
DR EMBL; CR382334; CAN87984.1; JOINED; Genomic_DNA.
DR EMBL; CR382334; CAM56478.2; -; Genomic_DNA.
DR EMBL; BX927163; CAM56478.2; JOINED; Genomic_DNA.
DR EMBL; BC163106; AAI63106.1; -; mRNA.
DR EMBL; BC163114; AAI63114.1; -; mRNA.
DR EMBL; U93487; AAB68764.1; -; Genomic_DNA.
DR EMBL; AF302242; AAL06722.1; -; mRNA.
DR RefSeq; NP_571415.1; NM_131340.1. [Q9PVE4-2]
DR RefSeq; XP_017207667.1; XM_017352178.1.
DR AlphaFoldDB; Q9PVE4; -.
DR SMR; Q9PVE4; -.
DR STRING; 7955.ENSDARP00000126275; -.
DR PaxDb; Q9PVE4; -.
DR Ensembl; ENSDART00000151766; ENSDARP00000126275; ENSDARG00000021163. [Q9PVE4-1]
DR Ensembl; ENSDART00000166313; ENSDARP00000131464; ENSDARG00000021163. [Q9PVE4-2]
DR Ensembl; ENSDART00000170790; ENSDARP00000137456; ENSDARG00000021163. [Q9PVE4-2]
DR Ensembl; ENSDART00000176980; ENSDARP00000144469; ENSDARG00000021163. [Q9PVE4-2]
DR Ensembl; ENSDART00000186678; ENSDARP00000149633; ENSDARG00000021163. [Q9PVE4-1]
DR Ensembl; ENSDART00000188045; ENSDARP00000150484; ENSDARG00000021163. [Q9PVE4-1]
DR Ensembl; ENSDART00000188589; ENSDARP00000152213; ENSDARG00000021163. [Q9PVE4-2]
DR GeneID; 30607; -.
DR KEGG; dre:30607; -.
DR CTD; 7068; -.
DR ZFIN; ZDB-GENE-990415-268; thrb.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156809; -.
DR HOGENOM; CLU_007368_18_0_1; -.
DR InParanoid; Q9PVE4; -.
DR OMA; YCMQELY; -.
DR OrthoDB; 1112927at2759; -.
DR PhylomeDB; Q9PVE4; -.
DR Reactome; R-DRE-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DRE-4090294; SUMOylation of intracellular receptors.
DR PRO; PR:Q9PVE4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000021163; Expressed in photoreceptor layer of retina and 28 other tissues.
DR ExpressionAtlas; Q9PVE4; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:ZFIN.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
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:0048839; P:inner ear development; IMP:ZFIN.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ZFIN.
DR GO; GO:0046549; P:retinal cone cell development; IMP:ZFIN.
DR GO; GO:0042671; P:retinal cone cell fate determination; IMP:ZFIN.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; IMP:ZFIN.
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; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..395
FT /note="Thyroid hormone receptor beta"
FT /id="PRO_0000053455"
FT DOMAIN 142..395
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 29..106
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 32..52
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 70..89
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..31
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 52
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="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 216
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 265
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 369
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 VAR_SEQ 172..180
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10687864, ECO:0000303|Ref.3"
FT /id="VSP_035801"
FT CONFLICT 95..96
FT /note="IA -> NP (in Ref. 4; AAB68764)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="K -> Q (in Ref. 5; AAL06722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45155 MW; 1E18666BCCACFE8A CRC64;
MSEQADKCNS RWKDEAMQNG YIPSYLDKDE LCVVCGDKAT GYHYRCITCE GCKGFFRRTI
QKNLNPTYAC KYEGKCVIDK VTRNQCQECR FKKCIAVGMA TDLVLDDSKR LAKRKLIEEN
RERRRREELQ KTVWDRPEPT QEEWEMIRVV TEAHMATNAQ GNHWKQKRKF LSAVGVKEAK
PEDIGSAPIV NAPEGNKVDI EAFSQFTKII TPAITRVVDF AKKLPMFCEL PCEDQIILLK
GCCMEIMSLR AAVRYDPESD TLTLNGEMAV TRGQLKNGGL GVVSDAIFDL GVSLSSFNLD
DSEVALLQAV ILLSSDRPGL TSVERIERCQ EEFLLAFEHY INYRKHKVAH FWPKLLMKVT
DLRMIGACHA SRFLHMKVEC PTELFPPLFL EVFED
