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

 FSHR_FELCA              Reviewed;         695 AA.
Q5GJ04;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
22-NOV-2017, entry version 78.
RecName: Full=Follicle-stimulating hormone receptor;
Short=FSH-R;
AltName: Full=Follitropin receptor;
Flags: Precursor;
Name=FSHR;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Neubauer K., Fickel J., Jewgenow K.;
"Cloning and sequencing of cat FSH receptor cDNA.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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; AY521181; AAS98965.1; -; mRNA.
RefSeq; NP_001041479.1; NM_001048014.1.
ProteinModelPortal; Q5GJ04; -.
STRING; 9685.ENSFCAP00000001126; -.
GeneID; 554348; -.
KEGG; fca:554348; -.
CTD; 2492; -.
eggNOG; KOG2087; Eukaryota.
eggNOG; ENOG410XR1T; LUCA.
HOVERGEN; HBG003521; -.
InParanoid; Q5GJ04; -.
KO; K04247; -.
Proteomes; UP000011712; 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; 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 18 695 Follicle-stimulating hormone receptor.
/FTId=PRO_0000041831.
TOPO_DOM 18 366 Extracellular. {ECO:0000255}.
TRANSMEM 367 387 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 388 398 Cytoplasmic. {ECO:0000255}.
TRANSMEM 399 419 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 420 444 Extracellular. {ECO:0000255}.
TRANSMEM 445 465 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 466 487 Cytoplasmic. {ECO:0000255}.
TRANSMEM 488 508 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 509 528 Extracellular. {ECO:0000255}.
TRANSMEM 529 550 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 551 573 Cytoplasmic. {ECO:0000255}.
TRANSMEM 574 594 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 595 608 Extracellular. {ECO:0000255}.
TRANSMEM 609 629 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 630 695 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.
COMPBIAS 563 566 Poly-Ser.
MOD_RES 335 335 Sulfotyrosine.
{ECO:0000250|UniProtKB:P23945}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 18 25 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 23 32 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 695 AA; 78829 MW; 426C701B22FE4CFE CRC64;
MTFLLVSLLA FLSLGSGCHH RICHCWHRVF LCQESKVTEI PSDLPRNAVE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEVIEANV FFNLSKLHEI RIEKANNLLY IDTDAFQNLP
NLRYLLISNT GIKHFPAVHK IQSLQKVLLD IQDNINIHTV ERNSFMGLSF ESMILWLNKN
GIQEIHNCAF NGTQLDELNL SDNINLEELP NDVFQGASGP VILDISRTRI HSLPSYGLEN
IKKLRAKSTY NLKKLPSLDK FVALMEASLT YPSHCCAFAN WRRPISELHP ICNKSILRQE
VDDMTQARGQ RVSLAEDEES SYTKGFDMMY SEFDYDLCNE VVDVTCSPKP DAFNPCEDIM
GYDILRVLIW FISILAITGN IIVLMILITS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS
VDIYTKSQYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TVITLERWHT ITHAMQLECK
VQLRHAAIIM LLGWIFAFMV ALFPIFGISS YMKVSICLPM DIDSPLSQLY VMSLLVLNVL
AFVVICCCYA HIYLTVRNPN IVSSSSDTKI AKRMAMLIFT DFLCMAPISF FAISASLKVP
LITVSKSKIL LVLFYPINSC ANPFLYAIFT KNFRRDFFIL LSKFGCYEVQ AQTYRSETSS
TAHNFHPRNG HCPPAPRVTN SSNYILIPLR HLAKN


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