THAB_XENLA
ID THAB_XENLA Reviewed; 418 AA.
AC P18115; Q91911;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thyroid hormone receptor alpha-B;
DE Short=TRalphaB;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1-B;
GN Name=thra-b; Synonyms=nr1a1-b, thra2;
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], SEQUENCE REVISION TO 133; 144; 165 AND 392,
RP FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole;
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).
CC -!- FUNCTION: High affinity receptor for triiodothyronine (T3).
CC {ECO:0000269|PubMed:2402492, ECO:0000269|PubMed:8969201}.
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 -!- 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}.
CC -!- CAUTION: The sequence derived in PubMed:2402492 was probably derived
CC from a mutant gene and shows poor transcriptional activation and DNA-
CC binding activity, but is still able to efficiently form heterodimers
CC with retinoic acid receptors. {ECO:0000305}.
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DR EMBL; M35344; AAA49970.1; -; mRNA.
DR EMBL; L76285; AAC38034.1; -; mRNA.
DR PIR; B36067; B36067.
DR AlphaFoldDB; P18115; -.
DR SMR; P18115; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; TAS:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X 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-B"
FT /id="PRO_0000053444"
FT DOMAIN 171..415
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 61..128
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..40
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 CONFLICT 133
FT /note="V -> D (in Ref. 1; AAA49970)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="N -> D (in Ref. 1; AAA49970)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="R -> C (in Ref. 1; AAA49970)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="R -> C (in Ref. 1; AAA49970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47683 MW; 092F308C423320AA CRC64;
MDQNLSGLDC LSEPDEKRWP DGKRKRKNSQ CMGKSGMSGD SLVSLPPAGY IPSYLDKDEP
CVVCSDKATG YHYRCITCEG CKGFFRRTIQ KNLHPSYSCK YDGCCIIDKI TRNQCQLCRF
KKCIAVGMAM DLVLDDSKRV AKRKLIEENR VRRRKEEMIK 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
