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Protein

Follicle-stimulating hormone receptor

Gene

Fshr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Induces cAMP production through the activation of PI3K-AKT and SRC-ERK1/2 signaling pathways.By similarity

GO - Molecular functioni

  • follicle-stimulating hormone receptor activity Source: RGD
  • G-protein coupled peptide receptor activity Source: GO_Central
  • G-protein coupled receptor activity Source: RGD
  • peptide hormone binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-RNO-375281. Hormone ligand-binding receptors.
R-RNO-418555. G alpha (s) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Follicle-stimulating hormone receptor
Short name:
FSH-R
Alternative name(s):
Follitropin receptor
Gene namesi
Name:Fshr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi2632. Fshr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 365348ExtracellularSequence analysisAdd
BLAST
Transmembranei366 – 38621Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini387 – 39711CytoplasmicSequence analysisAdd
BLAST
Transmembranei398 – 42023Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini421 – 44222ExtracellularSequence analysisAdd
BLAST
Transmembranei443 – 46422Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini465 – 48420CytoplasmicSequence analysisAdd
BLAST
Transmembranei485 – 50723Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini508 – 52720ExtracellularSequence analysisAdd
BLAST
Transmembranei528 – 54922Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini550 – 57223CytoplasmicSequence analysisAdd
BLAST
Transmembranei573 – 59624Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini597 – 60711ExtracellularSequence analysisAdd
BLAST
Transmembranei608 – 62922Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini630 – 69263CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: RGD
  • endosome Source: RGD
  • integral component of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911N → Q: Reduces N-glycosylation level. 1 Publication
Mutagenesisi199 – 1991N → Q: Does not affect N-glycosylation level. 1 Publication
Mutagenesisi293 – 2931N → Q: Reduces N-glycosylation level. 1 Publication
Mutagenesisi387 – 3871T → I: Reduces interaction with ARRB2; when associated with I-389 and N-394. 1 Publication
Mutagenesisi389 – 3891S → I: Reduces interaction with ARRB2; when associated with I-387 and N-394. 1 Publication
Mutagenesisi394 – 3941T → N: Reduces interaction with ARRB2; when associated with I-387 and I-389. 1 Publication
Mutagenesisi407 – 4071D → N: Reduces interaction with ARRB2. 1 Publication
Mutagenesisi548 – 5481Y → F: Reduces interaction with ARRB2. 1 Publication

Chemistry

ChEMBLiCHEMBL4288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 692675Follicle-stimulating hormone receptorPRO_0000012775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 ↔ 25PROSITE-ProRule annotation
Disulfide bondi23 ↔ 32PROSITE-ProRule annotation
Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)1 Publication
Disulfide bondi441 ↔ 516PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP20395.
PRIDEiP20395.

PTM databases

iPTMnetiP20395.
PhosphoSiteiP20395.

Expressioni

Tissue specificityi

Sertoli cells and ovarian granulosa cells.

Interactioni

Subunit structurei

Interacts with ARRB2.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022802.

Chemistry

BindingDBiP20395.

Structurei

3D structure databases

ProteinModelPortaliP20395.
SMRiP20395. Positions 18-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 4629LRRNTAdd
BLAST
Repeati49 – 7224LRR 1Add
BLAST
Repeati73 – 9725LRR 2Add
BLAST
Repeati98 – 11821LRR 3Add
BLAST
Repeati119 – 14325LRR 4Add
BLAST
Repeati144 – 16926LRR 5Add
BLAST
Repeati170 – 19223LRR 6Add
BLAST
Repeati193 – 21624LRR 7Add
BLAST
Repeati217 – 24024LRR 8Add
BLAST
Repeati241 – 25919LRR 9Add
BLAST

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.PROSITE-ProRule annotation
Contains 9 LRR (leucine-rich) repeats.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2087. Eukaryota.
ENOG410XR1T. LUCA.
GeneTreeiENSGT00760000119088.
HOGENOMiHOG000045902.
HOVERGENiHBG003521.
InParanoidiP20395.
KOiK04247.
OMAiRNGHCSS.
OrthoDBiEOG73BVCG.
PhylomeDBiP20395.
TreeFamiTF316814.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR002272. FSH_rcpt.
IPR024635. GnHR_TM.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR026906. LRR_5.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24372. PTHR24372. 1 hit.
PTHR24372:SF5. PTHR24372:SF5. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
PF12369. GnHR_trans. 1 hit.
PF13306. LRR_5. 2 hits.
[Graphical view]
PRINTSiPR01143. FSHRECEPTOR.
PR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS51450. LRR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLLVSLLA FLGTGSGCHH WLCHCSNRVF LCQDSKVTEI PTDLPRNAIE
60 70 80 90 100
LRFVLTKLRV IPKGSFAGFG DLEKIEISQN DVLEVIEADV FSNLPKLHEI
110 120 130 140 150
RIEKANNLLY INPEAFQNLP SLRYLLISNT GIKHLPAVHK IQSLQKVLLD
160 170 180 190 200
IQDNINIHIV ARNSFMGLSF ESVILWLSKN GIEEIHNCAF NGTQLDELNL
210 220 230 240 250
SDNNNLEELP NDVFQGASGP VILDISRTKV HSLPNHGLEN LKKLRARSTY
260 270 280 290 300
RLKKLPNLDK FVTLMEASLT YPSHCCAFAN LKRQISELHP ICNKSILRQD
310 320 330 340 350
IDDMTQIGDQ RVSLIDDEPS YGKGSDMMYN EFDYDLCNEV VDVTCSPKPD
360 370 380 390 400
AFNPCEDIMG YNILRVLIWF ISILAITGNT TVLVVLTTSQ YKLTVPRFLM
410 420 430 440 450
CNLAFADLCI GIYLLLIASV DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF
460 470 480 490 500
ASELSVYTLT AITLERWHTI THAMQLECKV QLRHAASVMV LGWTFAFAAA
510 520 530 540 550
LFPIFGISSY MKVSICLPMD IDSPLSQLYV MALLVLNVLA FVVICGCYTH
560 570 580 590 600
IYLTVRNPTI VSSSSDTKIA KRMATLIFTD FLCMAPISFF AISASLKVPL
610 620 630 640 650
ITVSKAKILL VLFYPINSCA NPFLYAIFTK NFRRDFFILL SKFGCYEMQA
660 670 680 690
QIYRTETSSA THNFHARKSH CSSAPRVTNS YVLVPLNHSS QN
Length:692
Mass (Da):77,681
Last modified:February 1, 1991 - v1
Checksum:i267EA78C7CFD8EC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1754Missing in AAB21415 (PubMed:1738373).Curated
Sequence conflicti252 – 2521L → W in AAB21415 (PubMed:1738373).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02842 mRNA. Translation: AAA41175.1.
S81198
, S81117, S81119, S81171, S81121, S81174, S81183, S81194, S81185, S81178 Genomic DNA. Translation: AAB21415.2.
PIRiA34548.
RefSeqiNP_954707.1. NM_199237.1.
UniGeneiRn.162843.

Genome annotation databases

EnsembliENSRNOT00000022802; ENSRNOP00000022802; ENSRNOG00000016783.
GeneIDi25449.
KEGGirno:25449.
UCSCiRGD:2632. rat.

Cross-referencesi

Web resourcesi

Sequence-structure-function-analysis of glycoprotein hormone receptors

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02842 mRNA. Translation: AAA41175.1.
S81198
, S81117, S81119, S81171, S81121, S81174, S81183, S81194, S81185, S81178 Genomic DNA. Translation: AAB21415.2.
PIRiA34548.
RefSeqiNP_954707.1. NM_199237.1.
UniGeneiRn.162843.

3D structure databases

ProteinModelPortaliP20395.
SMRiP20395. Positions 18-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022802.

Chemistry

BindingDBiP20395.
ChEMBLiCHEMBL4288.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP20395.
PhosphoSiteiP20395.

Proteomic databases

PaxDbiP20395.
PRIDEiP20395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022802; ENSRNOP00000022802; ENSRNOG00000016783.
GeneIDi25449.
KEGGirno:25449.
UCSCiRGD:2632. rat.

Organism-specific databases

CTDi2492.
RGDi2632. Fshr.

Phylogenomic databases

eggNOGiKOG2087. Eukaryota.
ENOG410XR1T. LUCA.
GeneTreeiENSGT00760000119088.
HOGENOMiHOG000045902.
HOVERGENiHBG003521.
InParanoidiP20395.
KOiK04247.
OMAiRNGHCSS.
OrthoDBiEOG73BVCG.
PhylomeDBiP20395.
TreeFamiTF316814.

Enzyme and pathway databases

ReactomeiR-RNO-375281. Hormone ligand-binding receptors.
R-RNO-418555. G alpha (s) signalling events.

Miscellaneous databases

PROiP20395.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR002272. FSH_rcpt.
IPR024635. GnHR_TM.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002131. Gphrmn_rcpt_fam.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR026906. LRR_5.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24372. PTHR24372. 1 hit.
PTHR24372:SF5. PTHR24372:SF5. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
PF12369. GnHR_trans. 1 hit.
PF13306. LRR_5. 2 hits.
[Graphical view]
PRINTSiPR01143. FSHRECEPTOR.
PR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
SMARTiSM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS51450. LRR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The testicular receptor for follicle stimulating hormone: structure and functional expression of cloned cDNA."
    Sprengel R., Braun T., Nikolics K., Segaloff D.L., Seeburg P.H.
    Mol. Endocrinol. 4:525-530(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Sertoli cell.
  2. "Structural organization of the follicle-stimulating hormone receptor gene."
    Heckert L.L., Daley I.J., Griswold M.D.
    Mol. Endocrinol. 6:70-80(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assessment of their role in FSH receptor function."
    Davis D., Liu X., Segaloff D.L.
    Mol. Endocrinol. 9:159-170(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-191 AND ASN-293, MUTAGENESIS OF ASN-191; ASN-199 AND ASN-293.
  4. "The association of arrestin-3 with the follitropin receptor depends on receptor activation and phosphorylation."
    Krishnamurthy H., Galet C., Ascoli M.
    Mol. Cell. Endocrinol. 204:127-140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2, MUTAGENESIS OF THR-387; SER-389; THR-394; ASP-407 AND TYR-548.

Entry informationi

Entry nameiFSHR_RAT
AccessioniPrimary (citable) accession number: P20395
Secondary accession number(s): Q64183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 156 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

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  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.