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Follicle-stimulating hormone receptor (FSH-R) (Follitropin receptor)

 FSHR_MOUSE              Reviewed;         692 AA.
P35378; Q9D4C2; Q9QWV8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Follicle-stimulating hormone receptor;
Short=FSH-R;
AltName: Full=Follitropin receptor;
Flags: Precursor;
Name=Fshr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=129/Sv; TISSUE=Testis;
PubMed=10330114; DOI=10.1095/biolreprod60.6.1515;
Tena-Sempere M., Manna P.R., Huhtaniemi I.T.;
"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.";
Biol. Reprod. 60:1515-1527(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE OF 1-51.
PubMed=1459341; DOI=10.1016/0303-7207(92)90009-U;
Huhtaniemi I.T., Eskola V., Pakarinen P., Matikainen T., Sprengel R.;
"The murine luteinizing hormone and follicle-stimulating hormone
receptor genes: transcription initiation sites, putative promoter
sequences and promoter activity.";
Mol. Cell. Endocrinol. 88:55-66(1992).
-!- FUNCTION: Receptor for follicle-stimulating hormone or
follitropin. 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. {ECO:0000250|UniProtKB:P23945}.
-!- SUBUNIT: Interacts with ARRB2. {ECO:0000250|UniProtKB:P20395}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P23945}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23945}.
-!- PTM: N-glycosylated; indirectly required for FSH-binding, possibly
via a conformational change that allows high affinity binding of
hormone. {ECO:0000250|UniProtKB:P20395}.
-!- PTM: Sulfated. {ECO:0000250|UniProtKB:P23945}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AF095642; AAC67559.1; -; mRNA.
EMBL; AK016635; BAB30351.1; -; mRNA.
EMBL; S49632; AAB24401.1; -; Genomic_DNA.
EMBL; M87570; AAA37641.1; -; Genomic_DNA.
CCDS; CCDS29026.1; -.
PIR; I57670; I57670.
RefSeq; NP_038551.3; NM_013523.3.
UniGene; Mm.57155; -.
ProteinModelPortal; P35378; -.
SMR; P35378; -.
STRING; 10090.ENSMUSP00000040477; -.
PhosphoSitePlus; P35378; -.
PaxDb; P35378; -.
PRIDE; P35378; -.
Ensembl; ENSMUST00000035701; ENSMUSP00000040477; ENSMUSG00000032937.
GeneID; 14309; -.
KEGG; mmu:14309; -.
UCSC; uc008dvx.1; mouse.
CTD; 2492; -.
MGI; MGI:95583; Fshr.
eggNOG; KOG2087; Eukaryota.
eggNOG; ENOG410XR1T; LUCA.
GeneTree; ENSGT00760000119088; -.
HOGENOM; HOG000045902; -.
HOVERGEN; HBG003521; -.
InParanoid; P35378; -.
KO; K04247; -.
OMA; ISSYMKV; -.
OrthoDB; EOG091G02BV; -.
PhylomeDB; P35378; -.
TreeFam; TF316814; -.
Reactome; R-MMU-375281; Hormone ligand-binding receptors.
Reactome; R-MMU-418555; G alpha (s) signalling events.
PRO; PR:P35378; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000032937; -.
CleanEx; MM_FSHR; -.
ExpressionAtlas; P35378; baseline and differential.
Genevisible; P35378; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004963; F:follicle-stimulating hormone receptor activity; IDA:MGI.
GO; GO:0008528; F:G-protein coupled peptide receptor activity; IBA:GO_Central.
GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0071711; P:basement membrane organization; IMP:MGI.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISS:UniProtKB.
GO; GO:0009992; P:cellular water homeostasis; IMP:MGI.
GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IDA:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0022602; P:ovulation cycle process; IMP:MGI.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0001545; P:primary ovarian follicle growth; IMP:MGI.
GO; GO:0060408; P:regulation of acetylcholine metabolic process; IGI:MGI.
GO; GO:0033044; P:regulation of chromosome organization; IMP:MGI.
GO; GO:0032350; P:regulation of hormone metabolic process; IMP:MGI.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
GO; GO:0060011; P:Sertoli cell proliferation; IMP:MGI.
GO; GO:0035092; P:sperm chromatin condensation; IMP:MGI.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:MGI.
GO; GO:0045056; P:transcytosis; IEA:Ensembl.
GO; GO:0060065; P:uterus development; IMP:MGI.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR002272; FSH_rcpt.
InterPro; IPR024635; GnHR_TM.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR002131; Gphrmn_rcpt_fam.
InterPro; IPR026906; LRR_5.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
InterPro; IPR034298; TSHR/LHCGR/FSHR.
PANTHER; PTHR24372; PTHR24372; 1.
PANTHER; PTHR24372:SF5; PTHR24372:SF5; 1.
Pfam; PF00001; 7tm_1; 1.
Pfam; PF12369; GnHR_trans; 1.
Pfam; PF13306; LRR_5; 2.
Pfam; PF01462; LRRNT; 1.
PRINTS; PR01143; FSHRECEPTOR.
PRINTS; PR00373; GLYCHORMONER.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Leucine-rich repeat;
Membrane; Receptor; Reference proteome; Repeat; Signal; Sulfation;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 692 Follicle-stimulating hormone receptor.
/FTId=PRO_0000012773.
TOPO_DOM 18 365 Extracellular. {ECO:0000255}.
TRANSMEM 366 386 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 387 397 Cytoplasmic. {ECO:0000255}.
TRANSMEM 398 420 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 421 442 Extracellular. {ECO:0000255}.
TRANSMEM 443 464 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 465 484 Cytoplasmic. {ECO:0000255}.
TRANSMEM 485 507 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 508 527 Extracellular. {ECO:0000255}.
TRANSMEM 528 549 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 550 572 Cytoplasmic. {ECO:0000255}.
TRANSMEM 573 596 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 597 607 Extracellular. {ECO:0000255}.
TRANSMEM 608 629 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 630 692 Cytoplasmic. {ECO:0000255}.
DOMAIN 18 46 LRRNT.
REPEAT 49 72 LRR 1.
REPEAT 73 97 LRR 2.
REPEAT 98 118 LRR 3.
REPEAT 119 143 LRR 4.
REPEAT 144 169 LRR 5.
REPEAT 170 192 LRR 6.
REPEAT 193 216 LRR 7.
REPEAT 217 240 LRR 8.
REPEAT 241 259 LRR 9.
MOD_RES 334 334 Sulfotyrosine.
{ECO:0000250|UniProtKB:P23945}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 18 25 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 23 32 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 441 516 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 436 436 Q -> K (in Ref. 2; BAB30351).
{ECO:0000305}.
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


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