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P21463 (TSHR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thyrotropin receptor
Alternative name(s):
Thyroid-stimulating hormone receptor
Short name=TSH-R
Gene names
Name:Tshr
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for thyrothropin. Plays a central role in controlling thyroid cell metabolism. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Also acts as a receptor for thyrostimulin (GPA2+GPB5).

Subunit structure

Interacts (via the PDZ-binding motif) with SCRIB; regulates TSHR trafficking and function By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.

Contains 7 LRR (leucine-rich) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 764743Thyrotropin receptor
PRO_0000012788

Regions

Topological domain22 – 413392Extracellular Potential
Transmembrane414 – 44128Helical; Name=1; Potential
Topological domain442 – 4509Cytoplasmic Potential
Transmembrane451 – 47323Helical; Name=2; Potential
Topological domain474 – 49421Extracellular Potential
Transmembrane495 – 51723Helical; Name=3; Potential
Topological domain518 – 53720Cytoplasmic Potential
Transmembrane538 – 56023Helical; Name=4; Potential
Topological domain561 – 58020Extracellular Potential
Transmembrane581 – 60222Helical; Name=5; Potential
Topological domain603 – 62523Cytoplasmic Potential
Transmembrane626 – 64924Helical; Name=6; Potential
Topological domain650 – 66011Extracellular Potential
Transmembrane661 – 68222Helical; Name=7; Potential
Topological domain683 – 76482Cytoplasmic Potential
Repeat100 – 12425LRR 1
Repeat125 – 15026LRR 2
Repeat151 – 17424LRR 3
Repeat176 – 19924LRR 4
Repeat201 – 22323LRR 5
Repeat225 – 24824LRR 6
Repeat264 – 28825LRR 7
Motif762 – 7643PDZ-binding

Amino acid modifications

Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 41 By similarity
Disulfide bond494 ↔ 569 By similarity

Experimental info

Mutagenesis6231A → E or K: Loss of TSH-increased inositol phosphate, but not cAMP formation. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P21463 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 79FC45CC9D26167B

FASTA76486,475
        10         20         30         40         50         60 
MRPGSLLQLT LLLALPRSLW GRGCTSPPCE CHQEDDFRVT CKELHQIPSL PPSTQTLKLI 

        70         80         90        100        110        120 
ETHLKTIPSL AFSSLPNISR IYLSIDATLQ RLEPHSFYNL SKMTHIEIRN TRSLTYIDPD 

       130        140        150        160        170        180 
ALTELPLLKF LGIFNTGLRI FPDLTKIYST DVFFILEITD NPYMTSVPEN AFQGLCNETL 

       190        200        210        220        230        240 
TLKLYNNGFT SIQGHAFNGT KLDAVYLNKN KYLTAIDKDA FGGVYSGPTL LDVSSTSVTA 

       250        260        270        280        290        300 
LPSKGLEHLK ELIAKNTWTL KKLPLSLSFL HLTRADLSYP SHCCAFKNQK KIRGILESLM 

       310        320        330        340        350        360 
CNESSIRNLR QRKSVNVMRG PVYQEYEEGL GDNHVGYKQN SKFQEGPSNS HYYVFFEEQE 

       370        380        390        400        410        420 
DEIIGFGQEL KNPQEETLQA FDSHYDYTVC GDNEDMVCTP KSDEFNPCED IMGYKFLRIV 

       430        440        450        460        470        480 
VWFVSPMALL GNVFVLFVLL TSHYKLTVPR FLMCNLAFAD FCMGVYLLLI ASVDLYTHTE 

       490        500        510        520        530        540 
YYNHAIDWQT GPGCNTAGFF TVFASELSVY TLTVITLERW YAITFAMRLD RKIRLRHAYT 

       550        560        570        580        590        600 
IMAGGWVSCF LLALLPMVGI SSYAKVSICL PMDTDTPLAL AYIALVLLLN VVAFVIVCSC 

       610        620        630        640        650        660 
YVKIYITVRN PQYNPRDKDT KIAKRMAVLI FTDFMCMAPI SFYALSALMN KPLITVTNSG 

       670        680        690        700        710        720 
VLLVLFYPLN SCANPFLYAI FTKAFQRDVF ILLSKFGLCK HQAQAYQAQR VCPNNNTGIQ 

       730        740        750        760 
IQKIPQDTRQ SLPNVQDTYE PLGSSHLTPK LQGRISEEYT QTAL

« Hide

References

[1]"Cloning, chromosomal assignment, and regulation of the rat thyrotropin receptor: expression of the gene is regulated by thyrotropin, agents that increase cAMP levels, and thyroid autoantibodies."
Akamizu T., Ikuyama S., Saji M., Kosugi S., Kozak C., McBride O.W., Kohn L.D.
Proc. Natl. Acad. Sci. U.S.A. 87:5677-5681(1990) [PubMed: 1696008] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mutation of alanine 623 in the third cytoplasmic loop of the rat thyrotropin (TSH) receptor results in a loss in the phosphoinositide but not cAMP signal induced by TSH and receptor autoantibodies."
Kosugi S., Okajima F., Ban T., Hidaka A., Shenker A., Kohn L.D.
J. Biol. Chem. 267:24153-24156(1992) [PubMed: 1332945] [Abstract]
Cited for: MUTAGENESIS OF ALA-623.
+Additional computationally mapped references.

Web resources

GRIS

Glycoprotein-hormone Receptors Information System

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34842 mRNA. Translation: AAA42302.1.
IPIIPI00203293.
PIRA35956.
RefSeqNP_037020.1. NM_012888.1.
UniGeneRn.87913.

3D structure databases

ProteinModelPortalP21463.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21463.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP21463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25360.
KEGGrno:25360.
UCSCNM_012888. rat.

Organism-specific databases

CTD7253.
RGD3911. Tshr.

Phylogenomic databases

eggNOGmaNOG09655.
HOVERGENHBG003521.
InParanoidP21463.
OrthoDBEOG4S1T6J.

Gene expression databases

ArrayExpressP21463.
GenevestigatorP21463.
GermOnlineENSRNOG00000003972. Rattus norvegicus.

Family and domain databases

InterProIPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
IPR002131. Gphrmn_rcpt.
IPR002274. TSH_rcpt.
[Graphical view]
KOK04249.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
PR01145. TSHRECEPTOR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606337.

Entry information

Entry nameTSHR_RAT
AccessionPrimary (citable) accession number: P21463
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

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