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THA_SHEEP
ID   THA_SHEEP               Reviewed;         410 AA.
AC   Q28570;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Thyroid hormone receptor alpha;
DE   AltName: Full=Nuclear receptor subfamily 1 group A member 1;
GN   Name=THRA; Synonyms=NR1A1;
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=Placenta;
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 RXRB.
CC       Interacts with NCOA3 and NCOA6 coactivators, leading to a strong
CC       increase of transcription of target genes. Probably interacts with
CC       SFPQ. Interacts with C1D. Interacts with AKAP13. Interacts with
CC       TP53INP2. Interacts with PER2 (By similarity). Interacts with TACC1.
CC       The interaction with isoform alpha-1, but not alpha-2, is decreased in
CC       the presence of thyroid hormone T3 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P10827}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SUBCELLULAR LOCATION: [Isoform Alpha-2]: Cytoplasm
CC       {ECO:0000250|UniProtKB:P63058}. Nucleus {ECO:0000250|UniProtKB:P63058}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha-1;
CC         IsoId=Q28570-1; Sequence=Displayed;
CC       Name=Alpha-2;
CC         IsoId=Q28570-2; Sequence=Not described;
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- MISCELLANEOUS: [Isoform Alpha-2]: Does not bind thyroid hormone T3.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Z68308; CAA92650.1; -; mRNA.
DR   RefSeq; NP_001094389.1; NM_001100919.1. [Q28570-1]
DR   AlphaFoldDB; Q28570; -.
DR   SMR; Q28570; -.
DR   STRING; 9940.ENSOARP00000013803; -.
DR   Ensembl; ENSOART00020015224; ENSOARP00020012596; ENSOARG00020009790.
DR   GeneID; 443446; -.
DR   KEGG; oas:443446; -.
DR   CTD; 7067; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   OrthoDB; 1112927at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Receptor; Reference proteome; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..410
FT                   /note="Thyroid hormone receptor alpha"
FT                   /id="PRO_0000053428"
FT   DOMAIN          163..407
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        53..127
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         53..73
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         91..115
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..52
FT                   /note="Modulating"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         56
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="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P10828"
FT   BINDING         228
FT                   /ligand="3,3',5-triiodo-L-thyronine"
FT                   /ligand_id="ChEBI:CHEBI:533015"
FT                   /evidence="ECO:0000250|UniProtKB:P10827"
FT   BINDING         277
FT                   /ligand="3,3',5-triiodo-L-thyronine"
FT                   /ligand_id="ChEBI:CHEBI:533015"
FT                   /evidence="ECO:0000250|UniProtKB:P10827"
SQ   SEQUENCE   410 AA;  46802 MW;  D4944675867C766B CRC64;
     MEQKPSKVEC GSDPEESSTR SPDGKRKRKN GQCSLKTSMS 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 VTDLRMIGAC HASRFLHMKV ECPTELFPPL FLEVFEDQEV
 
 
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