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Protein

Thyroid hormone receptor alpha

Gene

THRA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei226 – 2261Thyroid hormoneBy similarity
Binding sitei275 – 2751Thyroid hormone; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi51 – 12575Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri51 – 7121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri89 – 11325NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid hormone receptor alpha
Alternative name(s):
Nuclear receptor subfamily 1 group A member 1
Gene namesi
Name:THRA
Synonyms:NR1A1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Thyroid hormone receptor alphaPRO_0000053431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine; by CK21 Publication
Modified residuei28 – 281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04625.

PTM databases

iPTMnetiP04625.

Interactioni

Subunit structurei

Probably interacts with SFPQ.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SFPQP23246-12EBI-286261,EBI-355463From a different organism.

Protein-protein interaction databases

DIPiDIP-32625N.
IntActiP04625. 4 interactions.
STRINGi9031.ENSGALP00000000351.

Chemistry

BindingDBiP04625.

Structurei

Secondary structure

1
408
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni148 – 1525Combined sources
Helixi161 – 17616Combined sources
Beta strandi177 – 1793Combined sources
Turni183 – 1864Combined sources
Helixi210 – 23324Combined sources
Helixi235 – 2384Combined sources
Helixi244 – 26219Combined sources
Turni267 – 2704Combined sources
Beta strandi271 – 2744Combined sources
Turni275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Helixi282 – 2876Combined sources
Turni288 – 2925Combined sources
Helixi293 – 30311Combined sources
Turni304 – 3085Combined sources
Helixi311 – 32212Combined sources
Beta strandi327 – 3293Combined sources
Helixi334 – 35421Combined sources
Helixi361 – 3666Combined sources
Helixi368 – 38922Combined sources
Helixi397 – 4037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVVX-ray2.95A148-408[»]
ProteinModelPortaliP04625.
SMRiP04625. Positions 48-136, 146-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5050ModulatingAdd
BLAST
Regioni168 – 408241Ligand-bindingAdd
BLAST

Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 7121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri89 – 11325NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
InParanoidiP04625.
KOiK05547.
PhylomeDBiP04625.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04625-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQKPSTLDP LSEPEDTRWL DGKRKRKSSQ CLVKSSMSGY IPSYLDKDEQ
60 70 80 90 100
CVVCGDKATG YHYRCITCEG CKGFFRRTIQ KNLHPTYSCK YDGCCVIDKI
110 120 130 140 150
TRNQCQLCRF KKCISVGMAM DLVLDDSKRV AKRKLIEENR ERRRKEEMIK
160 170 180 190 200
SLQHRPSPSA EEWELIHVVT EAHRSTNAQG SHWKQKRKFL PEDIGQSPMA
210 220 230 240 250
SMPDGDKVDL EAFSEFTKII TPAITRVVDF AKKLPMFSEL PCEDQIILLK
260 270 280 290 300
GCCMEIMSLR AAVRYDPESE TLTLSGEMAV KREQLKNGGL GVVSDAIFDL
310 320 330 340 350
GKSLSAFNLD DTEVALLQAV LLMSSDRTGL ICVDKIEKCQ ETYLLAFEHY
360 370 380 390 400
INYRKHNIPH FWPKLLMKVT DLRMIGACHA SRFLHMKVEC PTELFPPLFL

EVFEDQEV
Length:408
Mass (Da):46,757
Last modified:August 13, 1987 - v1
Checksum:iAA7DB6B73322BAA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04854 Genomic DNA. Translation: CAA28545.1.
Y00987 mRNA. Translation: CAA68792.1.
PIRiA25236. TVCHVR.
RefSeqiNP_990644.1. NM_205313.1.
UniGeneiGga.609.
Gga.725.

Genome annotation databases

GeneIDi396251.
KEGGigga:396251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04854 Genomic DNA. Translation: CAA28545.1.
Y00987 mRNA. Translation: CAA68792.1.
PIRiA25236. TVCHVR.
RefSeqiNP_990644.1. NM_205313.1.
UniGeneiGga.609.
Gga.725.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVVX-ray2.95A148-408[»]
ProteinModelPortaliP04625.
SMRiP04625. Positions 48-136, 146-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-32625N.
IntActiP04625. 4 interactions.
STRINGi9031.ENSGALP00000000351.

Chemistry

BindingDBiP04625.

PTM databases

iPTMnetiP04625.

Proteomic databases

PaxDbiP04625.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396251.
KEGGigga:396251.

Organism-specific databases

CTDi7067.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
InParanoidiP04625.
KOiK05547.
PhylomeDBiP04625.

Miscellaneous databases

PROiP04625.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The c-erb-A protein is a high-affinity receptor for thyroid hormone."
    Sap J., Munoz A., Damm K., Ghysdael J., Leutz A., Beug H., Vennstroem B.
    Nature 324:635-640(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SPAFAS.
  2. "Nucleotide sequence of the chicken proto-oncogene c-erbA corresponding to domain 1 of v-erbA."
    Zahraoui A., Cuny G.
    Eur. J. Biochem. 166:63-69(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
  3. "Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein."
    Goldberg Y., Glineur C., Gesquiere J.C., Ricouart A., Sap J., Vennstrom B., Ghysdael J.
    EMBO J. 7:2425-2433(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-28.
  4. "The c-erbA alpha-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase II."
    Glineur C., Bailly M., Ghysdael J.
    Oncogene 4:1247-1254(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-12.
  5. "PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors."
    Mathur M., Tucker P.W., Samuels H.H.
    Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFPQ.

Entry informationi

Entry nameiTHA_CHICK
AccessioniPrimary (citable) accession number: P04625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 6, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.