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   24-JAN-2024, entry version 195.
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   GlyCosmos; P35378; 3 sites, No reported glycans.
DR   GlyGen; P35378; 3 sites.
DR   PhosphoSitePlus; P35378; -.
DR   PaxDb; 10090-ENSMUSP00000040477; -.
DR   Antibodypedia; 15300; 838 antibodies from 36 providers.
DR   DNASU; 14309; -.
DR   Ensembl; ENSMUST00000035701.6; ENSMUSP00000040477.5; ENSMUSG00000032937.6.
DR   GeneID; 14309; -.
DR   KEGG; mmu:14309; -.
DR   UCSC; uc008dvx.1; mouse.
DR   AGR; MGI:95583; -.
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; 1202285at2759; -.
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 78 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 cell types or tissues.
DR   ExpressionAtlas; P35378; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
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: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: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:0009992; P:intracellular water homeostasis; IMP:MGI.
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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0014070; P:response to organic cyclic compound; IEA:Ensembl.
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:0045056; P:transcytosis; ISO:MGI.
DR   GO; GO:0060065; P:uterus development; IMP:MGI.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; FOLLICLE-STIMULATING HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P35378; MM.
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
//