THAA_XENLA
ID THAA_XENLA Reviewed; 418 AA.
AC P15204; B7ZR78; P18114;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Thyroid hormone receptor alpha-A;
DE Short=TRalphaA;
DE Short=XenTR-alpha1;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1-A;
GN Name=thra-a; Synonyms=nr1a1-a, thra1;
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], AND FUNCTION.
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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INHIBITION OF
RP TRIIODOTHYRONINE-BINDING.
RC TISSUE=Oocyte;
RX PubMed=2587261; DOI=10.1093/nar/17.22.9395;
RA Brooks A.R., Sweeney G., Old R.W.;
RT "Structure and functional expression of a cloned Xenopus thyroid hormone
RT receptor.";
RL Nucleic Acids Res. 17:9395-9405(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP OF VAL-133; ASN-149 AND ARG-392.
RX PubMed=8969201; DOI=10.1074/jbc.271.52.33394;
RA Puzianowska-Kuznicka M., Wong J., Kanamori A., Shi Y.-B.;
RT "Functional characterization of a mutant thyroid hormone receptor in
RT Xenopus laevis.";
RL J. Biol. Chem. 271:33394-33403(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: High affinity receptor for triiodothyronine (T3).
CC {ECO:0000269|PubMed:2402492, ECO:0000269|PubMed:2587261}.
CC -!- SUBUNIT: Binds to thyroid hormone receptor element (TRE) weakly as
CC homodimers and monomers, but binds TRE with much higher affinity as
CC heterodimers with retinoid X receptors. Can bind DNA as a heterodimer
CC with either rxra or rxrg. {ECO:0000269|PubMed:8969201}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expression peaks at the climax of metamorphosis.
CC {ECO:0000269|PubMed:8969201}.
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 compounds can compete with and disrupt
CC triiodothyronine (T3)-binding including 3,3',5-triiodothyroacetic acid.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; M35343; AAA49969.1; -; mRNA.
DR EMBL; X17385; CAA35252.1; -; mRNA.
DR EMBL; BC170071; AAI70071.1; -; mRNA.
DR EMBL; BC170077; AAI70077.1; -; mRNA.
DR PIR; S09605; TVXLTA.
DR RefSeq; NP_001081595.1; NM_001088126.1.
DR RefSeq; XP_018089633.1; XM_018234144.1.
DR AlphaFoldDB; P15204; -.
DR SMR; P15204; -.
DR BioGRID; 99278; 4.
DR GeneID; 397942; -.
DR KEGG; xla:397942; -.
DR CTD; 397942; -.
DR Xenbase; XB-GENE-5966552; thra.L.
DR OMA; IMCLRIA; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 397942; Expressed in blastula and 18 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA: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: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 DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..418
FT /note="Thyroid hormone receptor alpha-A"
FT /id="PRO_0000053443"
FT DOMAIN 171..415
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 61..135
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 61..81
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 99..123
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..60
FT /note="Modulating"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 133
FT /note="V->D: In TR-alpha V; severe reduction in DNA binding
FT and transcriptional activation."
FT /evidence="ECO:0000269|PubMed:8969201"
FT MUTAGEN 149
FT /note="N->D: In TR-alpha VII; abolishes DNA binding and
FT reduces transcriptional activation."
FT /evidence="ECO:0000269|PubMed:8969201"
FT MUTAGEN 392
FT /note="R->C: In TR-alpha II; 3-fold reduction in
FT triiodothyronine (T3)-binding activity."
FT /evidence="ECO:0000269|PubMed:8969201"
FT CONFLICT 54
FT /note="Y -> H (in Ref. 3; CAA35252)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="S -> G (in Ref. 1; AAA49969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47702 MW; 96092F8DBF61FBC4 CRC64;
MDQNLSGLDC LSEPDEKRWP DGKRKRKNSQ CMGKSGMSGD SLVSLPSAGY IPSYLDKDEP
CVVCSDKATG YHYRCITCEG CKGFFRRTIQ KNLHPSYSCK YDGCCIIDKI TRNQCQLCRF
KKCIAVGMAM DLVLDDSKRV AKRKLIEENR QRRRKEEMIK TLQQRPEPSS EEWELIRIVT
EAHRSTNAQG SHWKQRRKFL PEDIGQSPMA SMPDGDKVDL EAFSEFTKII TPAITRVVDF
AKKLPMFSEL TCEDQIILLK GCCMEIMSLR AAVRYDPDSE TLTLSGEMAV KREQLKNGGL
GVVSDAIFDL GRSLAAFNLD DTEVALLQAV LLMSSDRTGL ICTDKIEKCQ ETYLLAFEHY
INHRKHNIPH FWPKLLMKVT DLRMIGACHA SRFLHMKVEC PTELFPPLFL EVFEDQEV
