THA_NECMA
ID THA_NECMA Reviewed; 408 AA.
AC O57606;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Thyroid hormone receptor alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group A member 1;
GN Name=THRA; Synonyms=NR1A1;
OS Necturus maculosus (Mudpuppy) (Waterdog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Proteidae; Necturus.
OX NCBI_TaxID=42757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 95.
RA Safi R., Vlaeminck V., Duffraisse M., Plateroti M., Carreghi A.,
RA De Luze A., Duterque-Coquillaud M., Demeneix B., Laudet V.;
RT "Neoteny revisited: thyroid hormone receptors are functional in the
RT mudpuppy (Necturus maculosus), an obligatory neotene.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-280.
RX PubMed=9169551; DOI=10.1007/pl00006182;
RA Safi R., Begue A., Hanni C., Stehelin D., Tata J., Laudet V.;
RT "Thyroid hormone receptor genes of neotenic amphibians.";
RL J. Mol. Evol. 44:595-604(1997).
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: A high level expression seen in the gills,
CC intestine and muscles.
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; Y16623; CAA76327.2; -; mRNA.
DR AlphaFoldDB; O57606; -.
DR SMR; O57606; -.
DR PRIDE; O57606; -.
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..408
FT /note="Thyroid hormone receptor alpha"
FT /id="PRO_0000053441"
FT DOMAIN 161..405
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 48..125
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 51..71
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 89..113
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..50
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 95
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 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P10828"
FT BINDING 226
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
FT BINDING 275
FT /ligand="3,3',5-triiodo-L-thyronine"
FT /ligand_id="ChEBI:CHEBI:533015"
FT /evidence="ECO:0000250|UniProtKB:P10827"
SQ SEQUENCE 408 AA; 46922 MW; F5A1A2272595AE9E CRC64;
MDQNLSDLDC LSDPDEKRWL DGKRKRKNSQ CLLKNSMSGY IPSYLDKDEP CVVCSDKATG
YHYRCITCEG CKGFFRRTIQ KNLHPSYSCK YDACCIIDKI TRNQCQLCRF KKCIAVGMAM
DLVLDDSKRV AKRKLIEENR ERRRKEEMLK SMQNRPEPTS EEWELIRLVT DAHCSTNAQG
SHWKQKRKFL PDAIGQCPMT AVPENDRVDL EAFSEFTKII TPAITRVVDF AKKLPMFSEL
PCEDQIILLK GCCMEIMSLR AAVRYDPESE TLTLSGEMAV KREQLKNGGL GVVSDAIFDL
GKSLSAFNLD DTEVALLQAV LLMSSDRSGL TCMDKVEKCQ ETYLLAFEHY INHRKHHIPH
FWPKLLMKVT DLRMIGACHA SRFMHMKVEC PTELFPPLFL EVFEDQEV
