THA_LITCT
ID THA_LITCT Reviewed; 418 AA.
AC Q02777;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thyroid hormone receptor alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1;
GN Name=thra; Synonyms=nr1a1;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tadpole tail;
RX PubMed=8243269; DOI=10.1210/endo.133.6.8243269;
RA Schneider M.J., Davey J.C., Galton V.A.;
RT "Rana catesbeiana tadpole red blood cells express an alpha, but not a beta,
RT c-erbA gene.";
RL Endocrinology 133:2488-2495(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-418.
RC TISSUE=Erythrocyte;
RX PubMed=1645454; DOI=10.1210/mend-5-2-201;
RA Schneider M.J., Galton V.A.;
RT "Regulation of c-erbA-alpha messenger RNA species in tadpole erythrocytes
RT by thyroid hormone.";
RL Mol. Endocrinol. 5:201-208(1991).
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highest level of expression in erythrocytes. Also
CC expressed in liver, tail, eye, muscle and skin.
CC -!- DEVELOPMENTAL STAGE: Expression is low at stage XII of tadpole
CC development, greatly increases by stage XIX, decreases thereafter and
CC is relatively low by stage XXIV, when metamorphosis is almost complete.
CC -!- INDUCTION: By thyroid hormone.
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; L06064; AAA16902.1; -; mRNA.
DR PIR; A37952; A37952.
DR AlphaFoldDB; Q02777; -.
DR SMR; Q02777; -.
DR PRIDE; Q02777; -.
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; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..418
FT /note="Thyroid hormone receptor alpha"
FT /id="PRO_0000053442"
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 /evidence="ECO:0000250"
FT REGION 1..41
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 BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 236
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT BINDING 285
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
SQ SEQUENCE 418 AA; 47748 MW; 2E79BCE92E3979F3 CRC64;
MDQNLSGLDC LSEPDEKRWP DGKRKRKNSQ CMGKSGMSGD SSVSLLSAGY IPSYLTKDEP
CVVCSDKATG YHYRCITCEG CKGFFRRTIQ KNLHPSYSCK YDGCCIIDKI TRNQCQLCRF
KKCIAVGMAM DLVLDDSKRV AKRKLIEENR ERRRKEEMIK TLQQRPEPSS EEWELIRIVT
EAHRSTNAQG SHWKQRRKFL PEDIGQNPMA SMPDSDKVDL EAFSEFTKII TPAITRVVDF
AKKLPMFSEL PCEDQIILLK GCCMEIMSLR AAVRYDPDSE TLTLSGEMAV KREQLKNGGL
GVVSDAIFDL GRSLSAFNLD DTEVALLQAV LLMSSDRTGL ICTDKIEKCQ ETYLLAFEHY
INHRKHNIPH FWPKLLMKVT DLRMIGACHA SRFLHMKVEC PTELFPPLFL EVFEDQEV
