THBA_XENLA
ID THBA_XENLA Reviewed; 373 AA.
AC P18117; P18116;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Thyroid hormone receptor beta-A;
DE Short=TRbetaA;
DE Short=xTR;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 2-A;
GN Name=thrb-a; Synonyms=nr1a2-a, thrb1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-A1 AND BETA-A5), DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC TISSUE=Tadpole;
RX PubMed=2402492; DOI=10.1073/pnas.87.18.7090;
RA Yaoita Y., Shi Y.-B., Brown D.D.;
RT "Xenopus laevis alpha and beta thyroid hormone receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7090-7094(1990).
RN [2]
RP ERRATUM OF PUBMED:2402492.
RX PubMed=2236080; DOI=10.1073/pnas.87.21.8685a;
RA Yaoita Y., Shi Y.-B., Brown D.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 87:8684-8684(1990).
RN [3]
RP FUNCTION, AND LACK OF INHIBITION OF TRIIODOTHYRONINE-BINDING.
RX PubMed=12553426; DOI=10.1515/cclm.2002.216;
RA Yamauchi K., Eguchi R., Shimada N., Ishihara A.;
RT "The effects of endocrine-disrupting chemicals on thyroid hormone binding
RT to Xenopus laevis transthyretin and thyroid hormone receptor.";
RL Clin. Chem. Lab. Med. 40:1250-1256(2002).
RN [4]
RP FUNCTION, AND INHIBITION OF TRIIODOTHYRONINE-BINDING.
RX PubMed=15590892; DOI=10.1093/toxsci/kfi049;
RA Kudo Y., Yamauchi K.;
RT "In vitro and in vivo analysis of the thyroid disrupting activities of
RT phenolic and phenol compounds in Xenopus laevis.";
RL Toxicol. Sci. 84:29-37(2005).
RN [5]
RP FUNCTION, AND INHIBITION OF TRIIODOTHYRONINE-BINDING.
RX PubMed=16627555; DOI=10.1093/toxsci/kfj204;
RA Kudo Y., Yamauchi K., Fukazawa H., Terao Y.;
RT "In vitro and in vivo analysis of the thyroid system-disrupting activities
RT of brominated phenolic and phenol compounds in Xenopus laevis.";
RL Toxicol. Sci. 92:87-95(2006).
CC -!- FUNCTION: High affinity receptor for triiodothyronine (T3).
CC {ECO:0000269|PubMed:12553426, ECO:0000269|PubMed:15590892,
CC ECO:0000269|PubMed:16627555}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Beta-A5; Synonyms=BetaA-II;
CC IsoId=P18117-1; Sequence=Displayed;
CC Name=Beta-A1; Synonyms=BetaA-I;
CC IsoId=P18117-2; Sequence=VSP_003627;
CC -!- DEVELOPMENTAL STAGE: Expression peaks at the climax of metamorphosis.
CC {ECO:0000269|PubMed:2402492}.
CC -!- INDUCTION: By thyroid hormone. {ECO:0000269|PubMed:2402492}.
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: A number of phenolic and phenol compounds can weakly
CC compete with and disrupt triiodothyronine (T3)-binding including 3,3'5-
CC trichlorobisphenol A, triiodophenol, 3,3'-dibromobisphenol A and 3,3'5-
CC tribromobisphenol A. The synthetic estrogen diethylstilbestrol (DES) is
CC not an effective competitor for T3-binding.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; M35360; AAA49656.1; -; mRNA.
DR EMBL; M35359; AAA49654.1; -; mRNA.
DR PIR; C36067; C36067.
DR RefSeq; NP_001090182.1; NM_001096713.1. [P18117-1]
DR RefSeq; NP_001090533.1; NM_001097064.1. [P18117-2]
DR AlphaFoldDB; P18117; -.
DR SMR; P18117; -.
DR BioGRID; 608169; 1.
DR PRIDE; P18117; -.
DR GeneID; 779054; -.
DR GeneID; 780755; -.
DR KEGG; xla:779054; -.
DR CTD; 7068; -.
DR CTD; 779054; -.
DR Xenbase; XB-GENE-6070716; thrb.L.
DR OMA; YCMQELY; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 779054; Expressed in internal ear and 8 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; TAS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..373
FT /note="Thyroid hormone receptor beta-A"
FT /id="PRO_0000053458"
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 VAR_SEQ 1..6
FT /note="MPSSMS -> ME (in isoform Beta-A1)"
FT /evidence="ECO:0000303|PubMed:2402492"
FT /id="VSP_003627"
SQ SEQUENCE 373 AA; 42300 MW; 5125B75A1FFEE07A CRC64;
MPSSMSGYIP SYLDKDELCV VCGDKATGYH YRCITCEGCK GFFRRTIQKN LHPSYSCKYE
GKCVIDKVTR NQCQECRFKK CIAVGMATDL VLDDNKRLAK RKLIEENREK RRKDEIQKSL
VQKPEPTQEE WELIQVVTEA HVATNAQGSH WKQKRKFLPE DIGQAPIVNA PEGGKVDLEA
FSQFTKIITP AITRVVDFAK KLPMFCELPC EDQIILLKGC CMEIMSLRAA VRYDPESETL
TLNGEMAVTR GQLKNGGLGV VSDAIFDLGV SLSSFSLDDT EVALLQAVLL MSSDRPGLAS
VERIEKCQEG FLLAFEHYIN YRKHNIAHFW PKLLMKVTDL RMIGACHASR FLHMKVECPT
ELFPPLFLEV FED
