THB_CHICK
ID THB_CHICK Reviewed; 369 AA.
AC P68306; P18112;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Thyroid hormone receptor beta;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2;
GN Name=THRB; Synonyms=C-ERBA-BETA, NR1A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SPAFAS; TISSUE=Kidney;
RX PubMed=1970296; DOI=10.1002/j.1460-2075.1990.tb08270.x;
RA Forest D., Sjoeberg M., Vennstroem B.;
RT "Contrasting developmental and tissue-specific expression of alpha and beta
RT thyroid hormone receptor genes.";
RL EMBO J. 9:1519-1528(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1707280; DOI=10.1089/dna.1991.10.211;
RA Showers M.O., Darling D.S., Kieffer G.D., Chin W.W.;
RT "Isolation and characterization of a cDNA encoding a chicken beta thyroid
RT hormone receptor.";
RL DNA Cell Biol. 10:211-221(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9244185; DOI=10.1016/0167-4889(95)00162-x;
RA Lachuer J.L., Legras C.L., Ronfort C.R., Barges S.B., Cohen-Adad F.C.,
RA Quivet L.Q., Duchamp C.D., Verdier G.V., Barre H.B.;
RT "Molecular cloning and sequencing of a cDNA encoding a beta-thyroid hormone
RT receptor in muscovy duckling.";
RL Biochim. Biophys. Acta 1310:127-130(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 -!- INTERACTION:
CC P68306; Q8IXJ9: ASXL1; Xeno; NbExp=2; IntAct=EBI-5743841, EBI-1646500;
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; X17504; CAA35544.1; -; mRNA.
DR EMBL; M65207; AAA49107.1; -; mRNA.
DR EMBL; Z50188; CAA90566.1; -; mRNA.
DR PIR; S09625; TVCHTB.
DR RefSeq; NP_990778.2; NM_205447.2.
DR RefSeq; XP_015136810.1; XM_015281324.1.
DR RefSeq; XP_015136811.1; XM_015281325.1.
DR RefSeq; XP_015136812.1; XM_015281326.1.
DR AlphaFoldDB; P68306; -.
DR SMR; P68306; -.
DR IntAct; P68306; 3.
DR STRING; 9031.ENSGALP00000018401; -.
DR PaxDb; P68306; -.
DR Ensembl; ENSGALT00000031162; ENSGALP00000030526; ENSGALG00000011294.
DR GeneID; 396431; -.
DR KEGG; gga:396431; -.
DR CTD; 7068; -.
DR VEuPathDB; HostDB:geneid_396431; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156809; -.
DR HOGENOM; CLU_007368_18_0_1; -.
DR InParanoid; P68306; -.
DR PhylomeDB; P68306; -.
DR Reactome; R-GGA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors.
DR PRO; PR:P68306; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000011294; Expressed in cerebellum and 9 other tissues.
DR ExpressionAtlas; P68306; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:AgBase.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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: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:0002154; P:thyroid hormone mediated signaling pathway; IBA:GO_Central.
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 DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..369
FT /note="Thyroid hormone receptor beta"
FT /id="PRO_0000053454"
FT DOMAIN 125..369
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 15..89
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 15..35
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 53..77
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..14
FT /note="Modulating"
FT /evidence="ECO:0000255"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
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 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 190
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 190
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 239
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 239
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 343
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 343
FT /ligand="L-thyroxine"
FT /ligand_id="ChEBI:CHEBI:58448"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT CONFLICT 116
FT /note="I -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="G -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="G -> V (in Ref. 2; AAA49107)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="C -> L (in Ref. 2; AAA49107)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> V (in Ref. 2; AAA49107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 42097 MW; 36FC16B41383138F CRC64;
MSGYIPSYLD KDELCVVCGD KATGYHYRCI TCEGCKGFFR RTIQKNLHPT YSCKYEGKCV
IDKVTRNQCQ ECRFKKCIFV GMATDLVLDD SKRLAKRKLI EENREKRRRE ELQKTIGHKP
EPTDEEWELI KIVTEAHVAT NAQGSHWKQK RKFLPEDIGQ APIVNAPEGG KVDLEAFSQF
TKIITPAITR VVDFAKKLPM FCELPCEDQI ILLKGCCMEI MSLRAAVRYD PESETLTLNG
EMAVTRGQLK NGGLGVVSDA IFDLGMSLSS FNLDDTEVAL LQAVLLMSSD RPGLVCVERI
EKCQEGFLLA FEHYINYRKH HVAHFWPKLL MKVTDLRMIG ACHASRFLHM KVECPTELFP
PLFLEVFED
