THA_CAIMO
ID THA_CAIMO Reviewed; 401 AA.
AC Q90382;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Thyroid hormone receptor alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1;
DE Flags: Fragment;
GN Name=THRA; Synonyms=NR1A1;
OS Cairina moschata (Muscovy duck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Cairina.
OX NCBI_TaxID=8855;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=R31 INRA; TISSUE=Liver;
RA Lachuer J., Ronfort C., Cohen-Adad F., Barges S., Faraut P., Quivet L.,
RA Legras C., Verdier G., Duchamp C., Barre H.;
RT "Molecular cloning and sequencing of a cDNA encoding the duckling alpha
RT thyroid hormone receptor.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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: Probably interacts with SFPQ. {ECO:0000250}.
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; Z50080; CAA90411.1; -; mRNA.
DR AlphaFoldDB; Q90382; -.
DR SMR; Q90382; -.
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; Phosphoprotein; Receptor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..>401
FT /note="Thyroid hormone receptor alpha"
FT /id="PRO_0000053430"
FT DOMAIN 160..>401
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 50..124
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 50..70
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 88..112
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION <1..49
FT /note="Modulating"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
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 67
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 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 104
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 225
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT BINDING 274
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT MOD_RES 11
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P04625"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04625"
FT NON_TER 1
FT NON_TER 401
SQ SEQUENCE 401 AA; 45878 MW; 059CEA6C75D68CAA CRC64;
EQKPSTLDPL SEPEDTRWLD GKRKRKSSQC LVKSSMSGYI PSYLDKDEQC VVCGDKATGY
HYRCITCEGC KGFFRRTIQK NLHPTYSCKY DGCCVIDKIT RNQCQLCRFK KCISVGMAMD
LVLDDSKRVA KRKLIEENRE RRRKEEMIKS LQHRPSPSAE EWELIHVVTE AHRSTNAQGS
HWKQKRKFLP EDIGQSPMAS MPDGDKVDLE AFSEFTKIIT PAITRVVDFA KKLPMFSELP
CEDQIILLKG CCMEIMSLRA AVRYDPESET LTLSGEMAVK REQLKNGGLG VVSDAIFDLG
KSLSAFNLDD TEVALLQAVL LMSSDRTGLI CVDKIEKCQE TYLLAFEHYI NYRKHNIPHF
WPKLLMKVTD LRMIGACHAS RFLHMKVECP TELFPPLFLE V
