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

 FSHR_HORSE              Reviewed;         694 AA.
P47799;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Follicle-stimulating hormone receptor;
Short=FSH-R;
AltName: Full=Follitropin receptor;
Flags: Precursor;
Name=FSHR;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Testis;
PubMed=8198575; DOI=10.1006/bbrc.1994.1689;
Robert P., Amsellem S., Christophe S., Benifla J.L., Bellet D.,
Koman A., Bidart J.-M.;
"Cloning and sequencing of the equine testicular follitropin
receptor.";
Biochem. Biophys. Res. Commun. 201:201-207(1994).
-!- 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 (By similarity). Among all mammalian FSH receptors, on
the horse receptor does not bind LH/chorionic gonadotropin (CG)
(PubMed:8198575). {ECO:0000250|UniProtKB:P23945,
ECO:0000269|PubMed:8198575}.
-!- 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; S70150; AAB30854.1; -; mRNA.
PIR; JC2237; JC2237.
UniGene; Eca.15982; -.
ProteinModelPortal; P47799; -.
SMR; P47799; -.
STRING; 9796.ENSECAP00000010338; -.
PaxDb; P47799; -.
eggNOG; KOG2087; Eukaryota.
eggNOG; ENOG410XR1T; LUCA.
HOGENOM; HOG000045902; -.
HOVERGEN; HBG003521; -.
InParanoid; P47799; -.
Proteomes; UP000002281; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004963; F:follicle-stimulating hormone receptor activity; ISS:UniProtKB.
GO; GO:0008528; F:G-protein coupled peptide receptor activity; IBA:GO_Central.
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:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISS:UniProtKB.
GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; ISS:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0001545; P:primary ovarian follicle growth; IBA:GO_Central.
GO; GO:0045670; P:regulation of osteoclast differentiation; IBA:GO_Central.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:UniProtKB.
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; IPR001611; Leu-rich_rpt.
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; 1.
Pfam; PF13855; LRR_8; 1.
Pfam; PF01462; LRRNT; 1.
PRINTS; PR01143; FSHRECEPTOR.
PRINTS; PR00373; GLYCHORMONER.
PRINTS; PR00237; GPCRRHODOPSN.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE; PS51450; LRR; 3.
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 18 694 Follicle-stimulating hormone receptor.
/FTId=PRO_0000012770.
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 630 694 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 268 268 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}.
SEQUENCE 694 AA; 78005 MW; E2F077C5E8CBCA54 CRC64;
MALLLVSLLA FLSLGSGCHH RVCHCSNRVF LCQESKVTEI PSDLPRNALE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDHDAFQNLP
NLQYLLISNT GIKHLPAVHK IQSLQKVLLD IQDNINIHTV ERNSFMGLSF ESTILRLSKN
GIQEIHNCAF NGTQLDELNL SYNNNLEELP NDVFQGASGP VILDISGTRI HSLPNYGLEN
LKKLRARSTY NLKKLPSLEK FVALMEANLT YPSHCCAFAN WRRQTSELQT TCNKSILRQE
VDMTQARGER VSLAEDDESS YPKGFDMMYS EFEYDLCNEV VDVTCSPKPD AFNPCEDIMG
YDILRVLIWF ISILAITGNI IVLVILITSQ YKLTVPRFLM CNLAFADLCI GIYLLLIASV
DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF ASELSVYTLT AITLERWHTI THAMQLECKV
QLRHAASVML VGWIFAFAVA LLPIFGISTY MKVSICLPMD IDSPLSQLYV MSLLVLNVLA
FVVICGCYIH IYLTVRNPNI VSSSSDTKIA KRMAILIFTD FLCMAPISFF AISASLKVPL
ITVSKSKILL VLFYPINSCA NPFLYAIFTK NFRRDFFILL SKFGCYEMQA QLYRTETSST
AHISHPRNGH CPPTPRVING ANCTLVPLSH LAQN


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