FSHR_MOUSE
ID FSHR_MOUSE Reviewed; 692 AA.
AC P35378; Q9D4C2; Q9QWV8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=Fshr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/Sv; TISSUE=Testis;
RX PubMed=10330114; DOI=10.1095/biolreprod60.6.1515;
RA Tena-Sempere M., Manna P.R., Huhtaniemi I.T.;
RT "Molecular cloning of the mouse follicle-stimulating hormone receptor
RT complementary deoxyribonucleic acid: functional expression of alternatively
RT spliced variants and receptor inactivation by a C566T transition in exon 7
RT of the coding sequence.";
RL Biol. Reprod. 60:1515-1527(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-51.
RX PubMed=1459341; DOI=10.1016/0303-7207(92)90009-u;
RA Huhtaniemi I.T., Eskola V., Pakarinen P., Matikainen T., Sprengel R.;
RT "The murine luteinizing hormone and follicle-stimulating hormone receptor
RT genes: transcription initiation sites, putative promoter sequences and
RT promoter activity.";
RL Mol. Cell. Endocrinol. 88:55-66(1992).
CC -!- FUNCTION: G protein-coupled receptor for follitropin, the follicle-
CC stimulating hormone. Through cAMP production activates the downstream
CC PI3K-AKT and ERK1/ERK2 signaling pathways.
CC {ECO:0000250|UniProtKB:P23945}.
CC -!- SUBUNIT: Homotrimer. Functions as a homotrimer binding the FSH hormone
CC heterodimer composed of CGA and FSHB (By similarity). Interacts with
CC ARRB2 (By similarity). Interacts with APPL2; interaction is independent
CC of follicle stimulating hormone stimulation (By similarity).
CC {ECO:0000250|UniProtKB:P23945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23945};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P23945}.
CC -!- PTM: N-glycosylated; indirectly required for FSH-binding, possibly via
CC a conformational change that allows high affinity binding of hormone.
CC {ECO:0000250|UniProtKB:P20395}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P23945}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF095642; AAC67559.1; -; mRNA.
DR EMBL; AK016635; BAB30351.1; -; mRNA.
DR EMBL; S49632; AAB24401.1; -; Genomic_DNA.
DR EMBL; M87570; AAA37641.1; -; Genomic_DNA.
DR CCDS; CCDS29026.1; -.
DR PIR; I57670; I57670.
DR RefSeq; NP_038551.3; NM_013523.3.
DR AlphaFoldDB; P35378; -.
DR SMR; P35378; -.
DR STRING; 10090.ENSMUSP00000040477; -.
DR GlyGen; P35378; 3 sites.
DR PhosphoSitePlus; P35378; -.
DR PaxDb; P35378; -.
DR PRIDE; P35378; -.
DR Antibodypedia; 15300; 706 antibodies from 36 providers.
DR DNASU; 14309; -.
DR Ensembl; ENSMUST00000035701; ENSMUSP00000040477; ENSMUSG00000032937.
DR GeneID; 14309; -.
DR KEGG; mmu:14309; -.
DR UCSC; uc008dvx.1; mouse.
DR CTD; 2492; -.
DR MGI; MGI:95583; Fshr.
DR VEuPathDB; HostDB:ENSMUSG00000032937; -.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000158952; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR InParanoid; P35378; -.
DR OMA; DIMGHAI; -.
DR OrthoDB; 257031at2759; -.
DR PhylomeDB; P35378; -.
DR TreeFam; TF316814; -.
DR Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 14309; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Fshr; mouse.
DR PRO; PR:P35378; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P35378; protein.
DR Bgee; ENSMUSG00000032937; Expressed in cumulus cell and 15 other tissues.
DR ExpressionAtlas; P35378; baseline and differential.
DR Genevisible; P35378; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0004963; F:follicle-stimulating hormone receptor activity; IDA:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISS:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:MGI.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0022602; P:ovulation cycle process; IMP:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0001545; P:primary ovarian follicle growth; IMP:MGI.
DR GO; GO:0060408; P:regulation of acetylcholine metabolic process; IGI:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:MGI.
DR GO; GO:0032350; P:regulation of hormone metabolic process; IMP:MGI.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:MGI.
DR GO; GO:0035092; P:sperm DNA condensation; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:MGI.
DR GO; GO:0045056; P:transcytosis; ISO:MGI.
DR GO; GO:0060065; P:uterus development; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR002272; FSH_rcpt.
DR InterPro; IPR024635; GnHR_TM.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24372:SF5; PTHR24372:SF5; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF12369; GnHR_trans; 1.
DR Pfam; PF13306; LRR_5; 2.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR01143; FSHRECEPTOR.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..692
FT /note="Follicle-stimulating hormone receptor"
FT /id="PRO_0000012773"
FT TOPO_DOM 18..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..420
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..464
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..507
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..629
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..46
FT /note="LRRNT"
FT REPEAT 49..72
FT /note="LRR 1"
FT REPEAT 73..97
FT /note="LRR 2"
FT REPEAT 98..118
FT /note="LRR 3"
FT REPEAT 119..143
FT /note="LRR 4"
FT REPEAT 144..169
FT /note="LRR 5"
FT REPEAT 170..192
FT /note="LRR 6"
FT REPEAT 193..216
FT /note="LRR 7"
FT REPEAT 217..240
FT /note="LRR 8"
FT REPEAT 241..259
FT /note="LRR 9"
FT MOD_RES 334
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 18..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 23..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 275..345
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..355
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..292
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 292..337
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 441..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 436
FT /note="Q -> K (in Ref. 2; BAB30351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 77769 MW; 4B57229180563A44 CRC64;
MALLLVSLLA FLGSGSGCHH WLCHCSNRVF LCQDSKVTEI PPDLPRNAIE LRFVLTKLRV
IPKGSFSGFG DLEKIEISQN DVLEVIEADV FSNLPNLHEI RIEKANNLLY INPEAFQNLP
SLRYLLISNT GIKHLPAFHK IQSLQKVLLD IQDNINIHII ARNSFMGLSF ESVILWLNKN
GIQEIHNCAF NGTQLDELNL SDNNNLEELP DDVFQGASGP VVLDISRTKV YSLPNHGLEN
LKKLRARSTY RLKKLPSLDK FVMLIEASLT YPSHCCAFAN WRRQTSELHP ICNKSISRQD
IDDMTQPGDQ RVSLVDDEPS YGKGSDMLYS EFDYDLCNEF VDVTCSPKPD AFNPCEDIMG
YNILRVLIWF ISILAITGNT TVLVVLTTSQ YKLTVPRFLM CNLAFADLCI GIYLLLIASV
DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF ASELSVYTLA AITLERWHTI THAMQLECKV
QLCHAASIMV LGWAFAFAAA LFPIFGISSY MKVSICLPMD IDSPLSQLYV MALLVLNALA
FVVICGCYTH IYLTVRNPNI VSSSRDTKIA KRMATLIFTD FLCMAPILFF AISASLKVPL
ITVSKAKILL VLFYPINSCA NPFLYAIFTK NFRRDFFVLM SKFGCYEVQA QIYKTETSSI
THNFHSRKNP CSSAPRVTNS YVLVPLNHSV QN
