FSHR_FELCA
ID FSHR_FELCA Reviewed; 695 AA.
AC Q5GJ04;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Neubauer K., Fickel J., Jewgenow K.;
RT "Cloning and sequencing of cat FSH receptor cDNA.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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:P20395, 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; AY521181; AAS98965.1; -; mRNA.
DR RefSeq; NP_001041479.1; NM_001048014.1.
DR AlphaFoldDB; Q5GJ04; -.
DR SMR; Q5GJ04; -.
DR STRING; 9685.ENSFCAP00000001126; -.
DR GeneID; 554348; -.
DR KEGG; fca:554348; -.
DR CTD; 2492; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q5GJ04; -.
DR OrthoDB; 257031at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISS:UniProtKB.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 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; PTHR24372:SF5; 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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..695
FT /note="Follicle-stimulating hormone receptor"
FT /id="PRO_0000041831"
FT TOPO_DOM 18..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..695
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 335
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
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..346
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..356
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..292
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 292..338
FT /evidence="ECO:0000250|UniProtKB:P23945"
SQ 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
