THB_SHEEP
ID THB_SHEEP Reviewed; 411 AA.
AC Q28571;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thyroid hormone receptor beta;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2;
DE Flags: Fragment;
GN Name=THRB; Synonyms=NR1A2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8837333; DOI=10.1089/thy.1996.6.237;
RA Tucker M.A., Polk D.H.;
RT "Cloning of the alpha and beta ovine thyroid hormone receptor cDNAs.";
RL Thyroid 6:237-243(1996).
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 RXRA (By
CC similarity). Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1,
CC NCOA7 and MED1/TRAP220 in a ligand-inducible manner. Interacts with the
CC corepressor NCOR1 in absence of ligand (By similarity). Interacts with
CC C1D (By similarity). Interacts with NR2F6; the interaction impairs the
CC binding of the THRB homodimer and THRB:RXRB heterodimer to T3 response
CC elements (By similarity). Interacts with PRMT2 and THRSP (By
CC similarity). Interacts with TACC1; this interaction is decreased in the
CC presence of thyroid hormone T3 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10828}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; Z68307; CAA92649.1; -; mRNA.
DR AlphaFoldDB; Q28571; -.
DR SMR; Q28571; -.
DR STRING; 9940.ENSOARP00000004757; -.
DR eggNOG; KOG3575; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..>411
FT /note="Thyroid hormone receptor beta"
FT /id="PRO_0000053452"
FT DOMAIN 215..>411
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 105..179
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 105..125
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 143..167
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..104
FT /note="Modulating"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..>411
FT /note="Interaction with NR2F6"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 280
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 280
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 329
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 329
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT NON_TER 411
SQ SEQUENCE 411 AA; 46716 MW; 11ED3AD7D7475BE8 CRC64;
MTPNSMTENG LPAWDKPKPC PDGEPEWKLV GMSEACLHRK SHPERRGPLK HEQSPLIQAS
WTSSIFHLDH DDVSDQSAPS AQAFQTEEKK CKGYIPSYLD KDELCVVCGD KATGYHYRCI
TCEGCKGFFR RTIQKNLHPS YSCKYEGKCV IDKVTRNQCQ ECRFKKCIYV GMATDLVLDD
SKRLAKRKLI EENREKRRRE ELQRSMGHKP EPTDQEWELI KTVTEAHVAT NAQGSHWKQK
RKFLPEDIGQ APIVNAPEGG KVDLEAFSHF TKIITPAITR VVDFAKKLPM FCELPCEDQI
ILLKGCCMEI MSLRAAVRYD PESETLTLNG EMAVTRRQLK NGGLGVVSDA IFDLGMSLSS
FNLDDTEVAL LQAVLLMSSD RPGLACVERI EKYQDSFLLA FEHYINYRRN S
