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P18113 (THB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid hormone receptor beta
Alternative name(s):
Nuclear receptor subfamily 1 group A member 2
c-erbA-2
c-erbA-beta
Gene names
Name:Thrb
Synonyms:Erba2, Nr1a2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Binds DNA as a dimer; homodimer and heterodimer with RXRA By similarity. Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and MED1/TRAP220 in a ligand-inducible manner By similarity. Interacts with the corepressor NCOR1 in absence of ligand. Interacts with C1D By similarity. Interacts with NR2F6; the interaction impairs the binding of the THRB homodimer and THRB:RXRB heterodimer to T3 response elements By similarity. Interacts with PRMT2 and THRSP By similarity. Ref.4

Subcellular location

Nucleus.

Domain

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

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence AAA40916.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA42200.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processembryonic organ development

Inferred from expression pattern PubMed 17496154. Source: RGD

intracellular receptor signaling pathway

Inferred from direct assay Ref.1. Source: GOC

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 16574785. Source: RGD

positive regulation of chondrocyte differentiation

Inferred from direct assay PubMed 15647824. Source: RGD

positive regulation of ossification

Inferred from direct assay PubMed 15647824. Source: RGD

regulation of cholesterol metabolic process

Inferred from mutant phenotype PubMed 17878314. Source: RGD

regulation of lipid metabolic process

Inferred from direct assay PubMed 15941710. Source: RGD

regulation of triglyceride metabolic process

Inferred from mutant phenotype PubMed 17878314. Source: RGD

   Cellular_componentnucleus

Traceable author statement Ref.1. Source: RGD

   Molecular_functiondouble-stranded DNA binding

Inferred from direct assay PubMed 15766871. Source: RGD

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement Ref.1. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 15766871. Source: RGD

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

thyroid hormone binding

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone receptor activity

Inferred from direct assay Ref.1. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-1 (identifier: P18113-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Beta-2 (identifier: P18113-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MTPNSMTENR...QTFQTEEKKC → MNYCVPEVHE...QVRSPPHSHK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Thyroid hormone receptor beta
PRO_0000053450

Regions

DNA binding107 – 18175Nuclear receptor
Zinc finger107 – 12721NR C4-type
Zinc finger145 – 16925NR C4-type
Region1 – 106106Modulating
Region244 – 461218Interaction with NR2F6 By similarity
Region244 – 461218Ligand-binding

Sites

Binding site2821Thyroid hormone By similarity
Binding site3201Thyroid hormone By similarity
Binding site3311Thyroid hormone; via amide nitrogen By similarity
Binding site4351Thyroid hormone By similarity

Natural variations

Alternative sequence1 – 9393MTPNS…EEKKC → MNYCVPEVHEVCPAAGSNRY MQVTDYLAYLEDSPAYSGCD VQAVPGSSIYLEQAWTLNQP YTCSYPGNLFKSKDSDLDMA LSQYSQPAHLPEEKPFPQVR SPPHSHK in isoform Beta-2.
VSP_031079

Experimental info

Sequence conflict9 – 102NR → KC in AAA60743. Ref.2
Sequence conflict2631Q → K in AAA60743. Ref.2

Secondary structure

................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta-1 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 16705C200E02995B

FASTA46152,656
        10         20         30         40         50         60 
MTPNSMTENR LPAWDKQKPH PDRGQDWKLV GMSEACLHRK SHVERRGALK NEQTSSHLIQ 

        70         80         90        100        110        120 
ATWASSIFHL DPDDVNDQSV SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR 

       130        140        150        160        170        180 
CITCEGCKGF FRRTIQKSLH PSYSCKYEGK CIIDKVTRNQ CQECRFKKCI YVGMATDLVL 

       190        200        210        220        230        240 
DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK 

       250        260        270        280        290        300 
QKRKFLPEDI GQAPIVNAPE GGQVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED 

       310        320        330        340        350        360 
QIILLKGCCM EIMSLRAAVR YDPDSETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL 

       370        380        390        400        410        420 
SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK 

       430        440        450        460 
LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D 

« Hide

Isoform Beta-2 [UniParc] [UniParc].

Checksum: AA86694C55019718
Show »

FASTA47554,013

References

[1]"Isolation and characterization of rat cDNA clones for two distinct thyroid hormone receptors."
Murray M.B., Zilz N.D., McCreary N.L., Macdonald M.J., Towle H.C.
J. Biol. Chem. 263:12770-12777(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
Tissue: Liver.
[2]"Isolation of a cDNA clone encoding a biologically active thyroid hormone receptor."
Koenig R.J., Warne R.L., Brent G.A., Harney J.W., Larsen P.R., Moore D.D.
Proc. Natl. Acad. Sci. U.S.A. 85:5031-5035(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
Tissue: Pituitary.
[3]"Identification of a thyroid hormone receptor that is pituitary-specific."
Hodin R.A., Lazar M.A., Wintman B.I., Darling D.S., Koenig R.J., Larsen P.R., Moore D.D., Chin W.W.
Science 244:76-78(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-121 (ISOFORM BETA-2).
Tissue: Pituitary.
[4]"Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element."
Chen Y., Young M.A.
Mol. Endocrinol. 24:1650-1664(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 104-206, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03933 mRNA. Translation: AAA40916.1. Different initiation.
J03819 mRNA. Translation: AAA60743.1.
M25071 mRNA. Translation: AAA42200.1. Different initiation.
PIRA31820.
A41355.
UniGeneRn.34019.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M9EX-ray2.41A/B/E/F104-206[»]
ProteinModelPortalP18113.
SMRP18113. Positions 104-192, 211-460.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP18113.
ChEMBLCHEMBL3917.
GuidetoPHARMACOLOGY589.

PTM databases

PhosphoSiteP18113.

Proteomic databases

PaxDbP18113.
PRIDEP18113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3858. rat. [P18113-1]

Organism-specific databases

RGD3858. Thrb.

Phylogenomic databases

eggNOGNOG272726.
HOGENOMHOG000010313.
HOVERGENHBG005606.
InParanoidP37826.
PhylomeDBP18113.

Gene expression databases

GenevestigatorP18113.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18113.
PROP18113.

Entry information

Entry nameTHB_RAT
AccessionPrimary (citable) accession number: P18113
Secondary accession number(s): P37826
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references