P35378 (FSHR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Follicle-stimulating hormone receptor
Short name=FSH-R

Alternative name(s):
Follitropin receptor

Gene names

Name:

Fshr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for follicle-stimulating hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subunit structure	Interacts with ARRB2 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone By similarity.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily. Contains 9 LRR (leucine-rich) repeats. Contains 1 LRRNT domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Sertoli cell development Inferred from mutant phenotype PubMed 14998910. Source: MGI Sertoli cell proliferation Inferred from mutant phenotype PubMed 11466221PubMed 18403489. Source: MGI adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 16630814. Source: MGI basement membrane organization Inferred from mutant phenotype PubMed 9811848. Source: MGI behavior Inferred from mutant phenotype PubMed 14502087. Source: MGI cellular water homeostasis Inferred from mutant phenotype PubMed 14998910. Source: MGI negative regulation of bone resorption Inferred from mutant phenotype PubMed 11089565PubMed 17332067. Source: MGI neuron projection development Inferred from mutant phenotype PubMed 12204217. Source: MGI phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from direct assay Ref.1. Source: MGI positive regulation of intracellular estrogen receptor signaling pathway Inferred from mutant phenotype PubMed 11089565. Source: MGI primary ovarian follicle growth Inferred from mutant phenotype PubMed 12801993. Source: MGI regulation of MAPK cascade Inferred from mutant phenotype PubMed 12204217. Source: MGI regulation of acetylcholine metabolic process Inferred from genetic interaction PubMed 12204217. Source: MGI regulation of chromosome organization Inferred from mutant phenotype PubMed 14680821. Source: MGI regulation of hormone metabolic process Inferred from mutant phenotype PubMed 12204217PubMed 12801993PubMed 14502087PubMed 14552897. Source: MGI regulation of osteoclast differentiation Inferred from mutant phenotype PubMed 16630814. Source: MGI regulation of platelet-derived growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 16344272. Source: MGI regulation of protein phosphorylation Inferred from mutant phenotype PubMed 12204217. Source: MGI regulation of systemic arterial blood pressure Inferred from mutant phenotype PubMed 18599597. Source: MGI spermatogenesis, exchange of chromosomal proteins Inferred from mutant phenotype PubMed 14680821. Source: MGI transcytosis Inferred from electronic annotation. Source: Compara uterus development Inferred from mutant phenotype PubMed 10803590. Source: MGI
Cellular_component	cell surface Inferred from direct assay PubMed 16630814. Source: MGI endosome Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	follicle-stimulating hormone receptor activity Inferred from direct assay Ref.1PubMed 16630814PubMed 9206032. Source: MGI peptide hormone binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 692	675	Follicle-stimulating hormone receptor		PRO_0000012773
Regions
	Topological domain	18 – 365	348	Extracellular Potential
	Transmembrane	366 – 386	21	Helical; Name=1; Potential
	Topological domain	387 – 397	11	Cytoplasmic Potential
	Transmembrane	398 – 420	23	Helical; Name=2; Potential
	Topological domain	421 – 442	22	Extracellular Potential
	Transmembrane	443 – 464	22	Helical; Name=3; Potential
	Topological domain	465 – 484	20	Cytoplasmic Potential
	Transmembrane	485 – 507	23	Helical; Name=4; Potential
	Topological domain	508 – 527	20	Extracellular Potential
	Transmembrane	528 – 549	22	Helical; Name=5; Potential
	Topological domain	550 – 572	23	Cytoplasmic Potential
	Transmembrane	573 – 596	24	Helical; Name=6; Potential
	Topological domain	597 – 607	11	Extracellular Potential
	Transmembrane	608 – 629	22	Helical; Name=7; Potential
	Topological domain	630 – 692	63	Cytoplasmic Potential
	Domain	18 – 46	29	LRRNT
	Repeat	49 – 72	24	LRR 1
	Repeat	73 – 97	25	LRR 2
	Repeat	98 – 118	21	LRR 3
	Repeat	119 – 143	25	LRR 4
	Repeat	144 – 169	26	LRR 5
	Repeat	170 – 192	23	LRR 6
	Repeat	193 – 216	24	LRR 7
	Repeat	217 – 240	24	LRR 8
	Repeat	241 – 259	19	LRR 9
Amino acid modifications
	Glycosylation	191	1	N-linked (GlcNAc...) By similarity
	Glycosylation	199	1	N-linked (GlcNAc...) Potential
	Glycosylation	293	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	18 ↔ 25		By similarity
	Disulfide bond	23 ↔ 32		By similarity
	Disulfide bond	441 ↔ 516		By similarity
Experimental info
	Sequence conflict	436	1	Q → K in BAB30351. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P35378 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 4B57229180563A44	FASTA	692	77,769
	10 20 30 40 50 60 MALLLVSLLA FLGSGSGCHH WLCHCSNRVF LCQDSKVTEI PPDLPRNAIE LRFVLTKLRV 70 80 90 100 110 120 IPKGSFSGFG DLEKIEISQN DVLEVIEADV FSNLPNLHEI RIEKANNLLY INPEAFQNLP 130 140 150 160 170 180 SLRYLLISNT GIKHLPAFHK IQSLQKVLLD IQDNINIHII ARNSFMGLSF ESVILWLNKN 190 200 210 220 230 240 GIQEIHNCAF NGTQLDELNL SDNNNLEELP DDVFQGASGP VVLDISRTKV YSLPNHGLEN 250 260 270 280 290 300 LKKLRARSTY RLKKLPSLDK FVMLIEASLT YPSHCCAFAN WRRQTSELHP ICNKSISRQD 310 320 330 340 350 360 IDDMTQPGDQ RVSLVDDEPS YGKGSDMLYS EFDYDLCNEF VDVTCSPKPD AFNPCEDIMG 370 380 390 400 410 420 YNILRVLIWF ISILAITGNT TVLVVLTTSQ YKLTVPRFLM CNLAFADLCI GIYLLLIASV 430 440 450 460 470 480 DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF ASELSVYTLA AITLERWHTI THAMQLECKV 490 500 510 520 530 540 QLCHAASIMV LGWAFAFAAA LFPIFGISSY MKVSICLPMD IDSPLSQLYV MALLVLNALA 550 560 570 580 590 600 FVVICGCYTH IYLTVRNPNI VSSSRDTKIA KRMATLIFTD FLCMAPILFF AISASLKVPL 610 620 630 640 650 660 ITVSKAKILL VLFYPINSCA NPFLYAIFTK NFRRDFFVLM SKFGCYEVQA QIYKTETSSI 670 680 690 THNFHSRKNP CSSAPRVTNS YVLVPLNHSV QN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Tena-Sempere M., Manna P.R., Huhtaniemi I.T. Biol. Reprod. 60:1515-1527(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 129/Sv. Tissue: Testis.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[3]	"The murine luteinizing hormone and follicle-stimulating hormone receptor genes: transcription initiation sites, putative promoter sequences and promoter activity." Huhtaniemi I.T., Eskola V., Pakarinen P., Matikainen T., Sprengel R. Mol. Cell. Endocrinol. 88:55-66(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-51.
+	Additional computationally mapped references.

Web resources

GRIS

Glycoprotein-hormone Receptors Information System

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF095642 mRNA. Translation: AAC67559.1. AK016635 mRNA. Translation: BAB30351.1. S49632 Genomic DNA. Translation: AAB24401.1. M87570 Genomic DNA. Translation: AAA37641.1.
IPI	IPI00117530.
PIR	I57670.
RefSeq	NP_038551.3. NM_013523.3.
UniGene	Mm.57155.
3D structure databases
ProteinModelPortal	P35378.
SMR	P35378. Positions 18-358, 367-636.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P35378.
Proteomic databases
PaxDb	P35378.
PRIDE	P35378.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035701; ENSMUSP00000040477; ENSMUSG00000032937.
GeneID	14309.
KEGG	mmu:14309.
Organism-specific databases
CTD	2492.
MGI	MGI:95583. Fshr.
Phylogenomic databases
eggNOG	NOG285844.
GeneTree	ENSGT00650000092962.
HOGENOM	HOG000045902.
HOVERGEN	HBG003521.
InParanoid	P35378.
KO	K04247.
OMA	SDTRIAK.
OrthoDB	EOG4N30P0.
Gene expression databases
ArrayExpress	P35378.
Bgee	P35378.
CleanEx	MM_FSHR.
Genevestigator	P35378.
GermOnline	ENSMUSG00000032937. Mus musculus.
Family and domain databases
InterPro	IPR002272. FSH_rcpt. IPR024635. GnHR_TM. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR002131. Gphrmn_rcpt. IPR000372. LRR-contain_N. [Graphical view]
PANTHER	PTHR24372:SF5. PTHR24372:SF5. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. PF12369. GnHR_trans. 1 hit. PF01462. LRRNT. 1 hit. [Graphical view]
PRINTS	PR01143. FSHRECEPTOR. PR00373. GLYCHORMONER. PR00237. GPCRRHODOPSN.
SMART	SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285731.
SOURCE	Search...

Entry information

Entry name

FSHR_MOUSE

Accession

Primary (citable) accession number: P35378
Secondary accession number(s): Q9D4C2, Q9QWV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program