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P35378 (FSHR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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:
Follicle-stimulating hormone receptor

Short name=FSH-R
Alternative name(s):
Follitropin receptor
Gene names
Name:Fshr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length692 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.

Subunit structure

Interacts with ARRB2 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone By similarity.

Sequence similarities

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

Contains 9 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell development

Inferred from mutant phenotype PubMed 14998910. Source: MGI

Sertoli cell proliferation

Inferred from mutant phenotype PubMed 11466221PubMed 18403489. Source: MGI

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 16630814. Source: MGI

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.1. Source: MGI

basement membrane organization

Inferred from mutant phenotype PubMed 9811848. Source: MGI

cellular water homeostasis

Inferred from mutant phenotype PubMed 14998910. Source: MGI

follicle-stimulating hormone signaling pathway

Inferred from direct assay Ref.1. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 14502087. Source: MGI

negative regulation of bone resorption

Inferred from mutant phenotype PubMed 11089565PubMed 17332067. Source: MGI

neuron projection development

Inferred from mutant phenotype PubMed 12204217. Source: MGI

ovarian follicle development

Inferred from mutant phenotype PubMed 10803590PubMed 11089565PubMed 11459817PubMed 12135868PubMed 12801993PubMed 9811848. Source: MGI

ovulation cycle process

Inferred from mutant phenotype PubMed 11089565. Source: MGI

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.1. Source: MGI

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 11089565. Source: MGI

primary ovarian follicle growth

Inferred from mutant phenotype PubMed 12801993. Source: MGI

regulation of MAPK cascade

Inferred from mutant phenotype PubMed 12204217. Source: MGI

regulation of acetylcholine metabolic process

Inferred from genetic interaction PubMed 12204217. Source: MGI

regulation of chromosome organization

Inferred from mutant phenotype PubMed 14680821. Source: MGI

regulation of hormone metabolic process

Inferred from mutant phenotype PubMed 12204217PubMed 12801993PubMed 14502087PubMed 14552897. Source: MGI

regulation of intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 18063689PubMed 18676690. Source: MGI

regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 16630814. Source: MGI

regulation of platelet-derived growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 16344272. Source: MGI

regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 12204217. Source: MGI

regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 18599597. Source: MGI

sperm chromatin condensation

Inferred from mutant phenotype PubMed 10775161. Source: MGI

spermatid development

Inferred from mutant phenotype PubMed 11466221PubMed 15973687. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 14680821PubMed 18403489PubMed 9811848. Source: MGI

spermatogenesis, exchange of chromosomal proteins

Inferred from mutant phenotype PubMed 14680821. Source: MGI

transcytosis

Inferred from electronic annotation. Source: Ensembl

uterus development

Inferred from mutant phenotype PubMed 10803590. Source: MGI

   Cellular_componentcell surface

Inferred from direct assay PubMed 16630814. Source: MGI

endosome

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfollicle-stimulating hormone receptor activity

Inferred from direct assay Ref.1PubMed 16630814PubMed 9206032. Source: MGI

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 692675Follicle-stimulating hormone receptor
PRO_0000012773

Regions

Topological domain18 – 365348Extracellular Potential
Transmembrane366 – 38621Helical; Name=1; Potential
Topological domain387 – 39711Cytoplasmic Potential
Transmembrane398 – 42023Helical; Name=2; Potential
Topological domain421 – 44222Extracellular Potential
Transmembrane443 – 46422Helical; Name=3; Potential
Topological domain465 – 48420Cytoplasmic Potential
Transmembrane485 – 50723Helical; Name=4; Potential
Topological domain508 – 52720Extracellular Potential
Transmembrane528 – 54922Helical; Name=5; Potential
Topological domain550 – 57223Cytoplasmic Potential
Transmembrane573 – 59624Helical; Name=6; Potential
Topological domain597 – 60711Extracellular Potential
Transmembrane608 – 62922Helical; Name=7; Potential
Topological domain630 – 69263Cytoplasmic Potential
Domain18 – 4629LRRNT
Repeat49 – 7224LRR 1
Repeat73 – 9725LRR 2
Repeat98 – 11821LRR 3
Repeat119 – 14325LRR 4
Repeat144 – 16926LRR 5
Repeat170 – 19223LRR 6
Repeat193 – 21624LRR 7
Repeat217 – 24024LRR 8
Repeat241 – 25919LRR 9

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) By similarity
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) By similarity
Disulfide bond18 ↔ 25 By similarity
Disulfide bond23 ↔ 32 By similarity
Disulfide bond441 ↔ 516 By similarity

Experimental info

Sequence conflict4361Q → K in BAB30351. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35378 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 4B57229180563A44

FASTA69277,769
        10         20         30         40         50         60 
MALLLVSLLA FLGSGSGCHH WLCHCSNRVF LCQDSKVTEI PPDLPRNAIE LRFVLTKLRV 

        70         80         90        100        110        120 
IPKGSFSGFG DLEKIEISQN DVLEVIEADV FSNLPNLHEI RIEKANNLLY INPEAFQNLP 

       130        140        150        160        170        180 
SLRYLLISNT GIKHLPAFHK IQSLQKVLLD IQDNINIHII ARNSFMGLSF ESVILWLNKN 

       190        200        210        220        230        240 
GIQEIHNCAF NGTQLDELNL SDNNNLEELP DDVFQGASGP VVLDISRTKV YSLPNHGLEN 

       250        260        270        280        290        300 
LKKLRARSTY RLKKLPSLDK FVMLIEASLT YPSHCCAFAN WRRQTSELHP ICNKSISRQD 

       310        320        330        340        350        360 
IDDMTQPGDQ RVSLVDDEPS YGKGSDMLYS EFDYDLCNEF VDVTCSPKPD AFNPCEDIMG 

       370        380        390        400        410        420 
YNILRVLIWF ISILAITGNT TVLVVLTTSQ YKLTVPRFLM CNLAFADLCI GIYLLLIASV 

       430        440        450        460        470        480 
DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF ASELSVYTLA AITLERWHTI THAMQLECKV 

       490        500        510        520        530        540 
QLCHAASIMV LGWAFAFAAA LFPIFGISSY MKVSICLPMD IDSPLSQLYV MALLVLNALA 

       550        560        570        580        590        600 
FVVICGCYTH IYLTVRNPNI VSSSRDTKIA KRMATLIFTD FLCMAPILFF AISASLKVPL 

       610        620        630        640        650        660 
ITVSKAKILL VLFYPINSCA NPFLYAIFTK NFRRDFFVLM SKFGCYEVQA QIYKTETSSI 

       670        680        690 
THNFHSRKNP CSSAPRVTNS YVLVPLNHSV QN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the mouse follicle-stimulating hormone receptor complementary deoxyribonucleic acid: functional expression of alternatively spliced variants and receptor inactivation by a C566T transition in exon 7 of the coding sequence."
Tena-Sempere M., Manna P.R., Huhtaniemi I.T.
Biol. Reprod. 60:1515-1527(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/Sv.
Tissue: Testis.
[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: Testis.
[3]"The murine luteinizing hormone and follicle-stimulating hormone receptor genes: transcription initiation sites, putative promoter sequences and promoter activity."
Huhtaniemi I.T., Eskola V., Pakarinen P., Matikainen T., Sprengel R.
Mol. Cell. Endocrinol. 88:55-66(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-51.
+Additional computationally mapped references.

Web resources

GRIS

Glycoprotein-hormone Receptors Information System

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095642 mRNA. Translation: AAC67559.1.
AK016635 mRNA. Translation: BAB30351.1.
S49632 Genomic DNA. Translation: AAB24401.1.
M87570 Genomic DNA. Translation: AAA37641.1.
CCDSCCDS29026.1.
PIRI57670.
RefSeqNP_038551.3. NM_013523.3.
UniGeneMm.57155.

3D structure databases

ProteinModelPortalP35378.
SMRP35378. Positions 18-358, 367-636.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY253.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35378.

Proteomic databases

PaxDbP35378.
PRIDEP35378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035701; ENSMUSP00000040477; ENSMUSG00000032937.
GeneID14309.
KEGGmmu:14309.
UCSCuc008dvx.1. mouse.

Organism-specific databases

CTD2492.
MGIMGI:95583. Fshr.

Phylogenomic databases

eggNOGNOG285844.
GeneTreeENSGT00730000110262.
HOGENOMHOG000045902.
HOVERGENHBG003521.
InParanoidP35378.
KOK04247.
OMASDTRIAK.
OrthoDBEOG73BVCG.
PhylomeDBP35378.
TreeFamTF316814.

Gene expression databases

ArrayExpressP35378.
BgeeP35378.
CleanExMM_FSHR.
GenevestigatorP35378.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR002272. FSH_rcpt.
IPR024635. GnHR_TM.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
[Graphical view]
PANTHERPTHR24372. PTHR24372. 1 hit.
PTHR24372:SF5. PTHR24372:SF5. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
PF12369. GnHR_trans. 1 hit.
PF13855. LRR_8. 2 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PRINTSPR01143. FSHRECEPTOR.
PR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
SMARTSM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285731.
PROP35378.
SOURCESearch...

Entry information

Entry nameFSHR_MOUSE
AccessionPrimary (citable) accession number: P35378
Secondary accession number(s): Q9D4C2, Q9QWV8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 135 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