THB_LITCT
ID THB_LITCT Reviewed; 373 AA.
AC Q02965;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Thyroid hormone receptor beta;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2;
GN Name=thrb; Synonyms=nr1a2;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye, and Liver;
RX PubMed=7923937; DOI=10.1002/dvg.1020150405;
RA Davey J.C., Schneider M.J., Galton V.A.;
RT "Cloning of a thyroid hormone-responsive Rana catesbeiana c-erbA-beta
RT gene.";
RL Dev. Genet. 15:339-346(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-373.
RC TISSUE=Liver;
RX PubMed=1291156; DOI=10.1002/dvg.1020130406;
RA Helbing C., Gergely G., Atkinson B.G.;
RT "Sequential up-regulation of thyroid hormone beta receptor, ornithine
RT transcarbamylase, and carbamyl phosphate synthetase mRNAs in the liver of
RT Rana catesbeiana tadpoles during spontaneous and thyroid hormone-induced
RT metamorphosis.";
RL Dev. Genet. 13:289-301(1992).
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By thyroid hormone.
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}.
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DR EMBL; L27344; AAA53658.1; -; mRNA.
DR EMBL; M95194; AAA49535.1; -; Genomic_DNA.
DR PIR; B48421; B48421.
DR PIR; I51165; I51165.
DR AlphaFoldDB; Q02965; -.
DR SMR; Q02965; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..373
FT /note="Thyroid hormone receptor beta"
FT /id="PRO_0000053457"
FT DOMAIN 129..373
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 19..93
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 19..39
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 57..81
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..18
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 73
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 194
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 194
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 243
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 243
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 347
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 347
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
SQ SEQUENCE 373 AA; 42285 MW; 96E086E2E8159EB4 CRC64;
MPSSMSGYIP SYLDKDELCV VCGDKATGYH YRCITCEGCK GFFRRTIQKN LHPSYSCKYE
GKCVIDKVTR NQCQECRFKK CIAVGMATDL VLDDSKRLAK RKLIEENREK RRKDELQKTL
VQKPEPTPEE WELIQVVTEA HVATNAQGSH WKQKRKFLPE DIGQAPIVNA PEGGKVDLEA
FSQFTKIITP AITRVVDFAK KLPMFCELPC EDQIILLKGC CMEIMSLRAA VRYDPESETL
TLNGEMAVTR GQLKNGGLGV VSDAIFDLGV SLSSFNLDDT EVALLQAVLL MSSDRPGLSS
VERIEKCQEG FLLAFEHYIN YRKHNVAHFW PKLLMKVTDL RMIGACHASR FLHMKVECPT
ELFPPLFLEV FED
