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P47750 (TSHR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyrotropin receptor
Alternative name(s):
Thyroid-stimulating hormone receptor
Short name=TSH-R
Gene names
Name:Tshr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Involvement in disease

Defects in Tshr are the cause of hyt/hyt hypothyroidism, an autosomal recessive, fetal-onset, severe hypothyroidism related to TSH hyporesponsiveness and associated with elevated TSH.

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 By similarity
Chain22 – 764743Thyrotropin receptor
PRO_0000012787

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
Repeat200 – 22324LRR 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

Natural variations

Natural variant5561P → L in hypothyroidism.

Experimental info

Sequence conflict3121R → S in BAB29408. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P47750 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 6ADD2CC72F018317

FASTA76486,583
        10         20         30         40         50         60 
MRPGSLLLLV LLLALSRSLR GKECASPPCE CHQEDDFRVT CKELHRIPSL PPSTQTLKLI 

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

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

       190        200        210        220        230        240 
TLKLYNNGFT SVQGHAFNGT KLDAVYLNKN KYLTAIDNDA FGGVYSGPTL LDVSSTSVTA 

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

       310        320        330        340        350        360 
CNESSIRNLR QRKSVNILRG PIYQEYEEDP GDNSVGYKQN SKFQESPSNS HYYVFFEEQE 

       370        380        390        400        410        420 
DEVVGFGQEL KNPQEETLQA FESHYDYTVC GDNEDMVCTP KSDEFNPCED IMGYRFLRIV 

       430        440        450        460        470        480 
VWFVSLLALL GNIFVLLILL TSHYKLTVPR FLMCNLAFAD FCMGVYLLLI ASVDLYTHSE 

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

       550        560        570        580        590        600 
IMAGGWVSCF LLALLPMVGI SSYAKVSICL PMDTDTPLAL AYIVLVLLLN VVAFVVVCSC 

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

       670        680        690        700        710        720 
ILLVLFYPLN SCANPFLYAI FTKAFQRDVF ILLSKFGICK RQAQAYQGQR VCPNNSTGIQ 

       730        740        750        760 
IQKIPQDTRQ SLPNMQDTYE LLGNSQLAPK LQGQISEEYK QTAL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a point mutation in the thyrotropin receptor of the hyt/hyt hypothyroid mouse."
Stein S.A., Oates E.L., Hall C.R., Grumbles R.M., Fernandez L.M., Taylor N.A., Puett D., Jin S.
Mol. Endocrinol. 8:129-138(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Thyroid.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Web resources

GRIS

Glycoprotein-hormone Receptors Information System

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02601 mRNA. Translation: AAA53209.1.
U02602 mRNA. Translation: AAB60455.1.
AK014519 mRNA. Translation: BAB29408.1.
AK029084 mRNA. Translation: BAC26286.1.
BC086691 mRNA. Translation: AAH86691.1.
BC092523 mRNA. Translation: AAH92523.1.
PIRI48882.
RefSeqNP_035778.3. NM_011648.5.
UniGeneMm.173847.

3D structure databases

ProteinModelPortalP47750.
SMRP47750. Positions 24-305, 411-686.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY255.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP47750.

Proteomic databases

PaxDbP47750.
PRIDEP47750.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021346; ENSMUSP00000021346; ENSMUSG00000020963.
GeneID22095.
KEGGmmu:22095.
UCSCuc007okq.2. mouse.

Organism-specific databases

CTD7253.
MGIMGI:98849. Tshr.

Phylogenomic databases

eggNOGNOG285844.
GeneTreeENSGT00730000110262.
HOGENOMHOG000045902.
HOVERGENHBG003521.
InParanoidQ562E4.
KOK04249.
OMASCYVKIY.
OrthoDBEOG73BVCG.
PhylomeDBP47750.
TreeFamTF316814.

Gene expression databases

BgeeP47750.
CleanExMM_TSHR.
GenevestigatorP47750.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR026906. LRR_5.
IPR002274. TSH_rcpt.
[Graphical view]
PANTHERPTHR24372. PTHR24372. 1 hit.
PTHR24372:SF0. PTHR24372:SF0. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
PF13306. LRR_5. 2 hits.
[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

NextBio301940.
PROP47750.
SOURCESearch...

Entry information

Entry nameTSHR_MOUSE
AccessionPrimary (citable) accession number: P47750
Secondary accession number(s): Q562E4, Q9D697
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 127 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries