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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)DescriptionActionsGraphical viewLength
Topological domaini18 – 365ExtracellularSequence analysisAdd BLAST348
Transmembranei366 – 386Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini387 – 397CytoplasmicSequence analysisAdd BLAST11
Transmembranei398 – 420Helical; Name=2Sequence analysisAdd BLAST23
Topological domaini421 – 442ExtracellularSequence analysisAdd BLAST22
Transmembranei443 – 464Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini465 – 484CytoplasmicSequence analysisAdd BLAST20
Transmembranei485 – 507Helical; Name=4Sequence analysisAdd BLAST23
Topological domaini508 – 527ExtracellularSequence analysisAdd BLAST20
Transmembranei528 – 549Helical; Name=5Sequence analysisAdd BLAST22
Topological domaini550 – 572CytoplasmicSequence analysisAdd BLAST23
Transmembranei573 – 596Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini597 – 607ExtracellularSequence analysisAdd BLAST11
Transmembranei608 – 629Helical; Name=7Sequence analysisAdd BLAST22
Topological domaini630 – 692CytoplasmicSequence analysisAdd BLAST63

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)DescriptionActionsGraphical viewLength
Mutagenesisi191N → Q: Reduces N-glycosylation level. 1 Publication1
Mutagenesisi199N → Q: Does not affect N-glycosylation level. 1 Publication1
Mutagenesisi293N → Q: Reduces N-glycosylation level. 1 Publication1
Mutagenesisi387T → I: Reduces interaction with ARRB2; when associated with I-389 and N-394. 1 Publication1
Mutagenesisi389S → I: Reduces interaction with ARRB2; when associated with I-387 and N-394. 1 Publication1
Mutagenesisi394T → N: Reduces interaction with ARRB2; when associated with I-387 and I-389. 1 Publication1
Mutagenesisi407D → N: Reduces interaction with ARRB2. 1 Publication1
Mutagenesisi548Y → F: Reduces interaction with ARRB2. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000001277518 – 692Follicle-stimulating hormone receptorAdd BLAST675

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi18 ↔ 25PROSITE-ProRule annotation
Disulfide bondi23 ↔ 32PROSITE-ProRule annotation
Glycosylationi191N-linked (GlcNAc...)1 Publication1
Glycosylationi199N-linked (GlcNAc...)Sequence analysis1
Glycosylationi293N-linked (GlcNAc...)1 Publication1
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.
PhosphoSitePlusiP20395.

Expressioni

Tissue specificityi

Sertoli cells and ovarian granulosa cells.

Gene expression databases

BgeeiENSRNOG00000016783.

Interactioni

Subunit structurei

Interacts with ARRB2.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022802.

Chemistry databases

BindingDBiP20395.

Structurei

3D structure databases

ProteinModelPortaliP20395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 46LRRNTAdd BLAST29
Repeati49 – 72LRR 1Add BLAST24
Repeati73 – 97LRR 2Add BLAST25
Repeati98 – 118LRR 3Add BLAST21
Repeati119 – 143LRR 4Add BLAST25
Repeati144 – 169LRR 5Add BLAST26
Repeati170 – 192LRR 6Add BLAST23
Repeati193 – 216LRR 7Add BLAST24
Repeati217 – 240LRR 8Add BLAST24
Repeati241 – 259LRR 9Add BLAST19

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.
OMAiFILLSKC.
OrthoDBiEOG091G02BV.
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)DescriptionActionsGraphical viewLength
Sequence conflicti172 – 175Missing in AAB21415 (PubMed:1738373).Curated4
Sequence conflicti252L → W in AAB21415 (PubMed:1738373).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022802.

Chemistry databases

BindingDBiP20395.
ChEMBLiCHEMBL4288.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP20395.
PhosphoSitePlusiP20395.

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.
OMAiFILLSKC.
OrthoDBiEOG091G02BV.
PhylomeDBiP20395.
TreeFamiTF316814.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP20395.

Gene expression databases

BgeeiENSRNOG00000016783.

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...

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: November 2, 2016
This is version 159 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.