FSHR_CHICK
ID FSHR_CHICK Reviewed; 693 AA.
AC P79763; Q90719;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=9332357; DOI=10.1016/s0378-1119(97)00250-3;
RA Wakabayashi N., Suzuki A., Hoshino H., Nishimori K., Mizuno S.;
RT "The cDNA cloning and transient expression of a chicken gene encoding a
RT follicle-stimulating hormone receptor.";
RL Gene 197:121-127(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=8902217; DOI=10.1095/biolreprod55.5.1055;
RA You S., Bridgham J.T., Foster D.N., Johnson A.L.;
RT "Characterization of the chicken follicle-stimulating hormone receptor
RT (cFSH-R) complementary deoxyribonucleic acid, and expression of cFSH-R
RT messenger ribonucleic acid in the ovary.";
RL Biol. Reprod. 55:1055-1062(1996).
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. {ECO:0000250|UniProtKB:P23945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23945};
CC Multi-pass membrane protein {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; D87871; BAA13487.1; -; mRNA.
DR EMBL; U51097; AAC60030.1; -; mRNA.
DR RefSeq; NP_990410.1; NM_205079.1.
DR AlphaFoldDB; P79763; -.
DR SMR; P79763; -.
DR STRING; 9031.ENSGALP00000014797; -.
DR PaxDb; P79763; -.
DR GeneID; 395962; -.
DR KEGG; gga:395962; -.
DR CTD; 2492; -.
DR VEuPathDB; HostDB:geneid_395962; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; P79763; -.
DR OrthoDB; 257031at2759; -.
DR PhylomeDB; P79763; -.
DR PRO; PR:P79763; -.
DR Proteomes; UP000000539; 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:0033686; P:positive regulation of luteinizing hormone secretion; IEP:AgBase.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24372:SF5; PTHR24372:SF5; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF12369; GnHR_trans; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 1.
DR PRINTS; PR01143; FSHRECEPTOR.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..693
FT /note="Follicle-stimulating hormone receptor"
FT /id="PRO_0000012777"
FT TOPO_DOM 19..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..421
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..465
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..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..597
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..630
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..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 CARBOHYD 47
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 268
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"
FT DISULFID 442..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 4
FT /note="G -> D (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="G -> A (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="K -> R (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="I -> T (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> S (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> L (in Ref. 2; AAC60030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 78698 MW; 46F98699635A1BEC CRC64;
MSLGLTCLLI LLASCSGCQH HTCLCEGRIF ICQEIKVVQL PRDIPTNATE LRFVLTKMRV
IPKGAFTGLH DLEKIEISQN DALEIIEGNV FSSLPKLHEI RIEKANKLMK IDQDAFQHLP
SLRYLLISNT GLSFLPVVHK VHSFQKVLLD VQDNIHIRTI ERNTFMGLSS ESVILRLNKN
GIQEIKDHAF NGTCLDELNL SDNYNLEKLP EKVFQGAIGP VVLDISRTRI SFLPSHGLEF
IKKLRARSTY KLKKLPDVNK FRSLIEANFT YPSHCCAFTN RKTQNTEFYP ICSMSPAKQD
LGEQTGKRKH RRSAAEDYIS HYGTRFGPVE NEFDYGLCNE VVDFVCSPKP DAFNPCEDIM
GYNVLRVLIW FINILAITGN TTVLIILISS QYKLTVPRFL MCNLAFADLC IGIYLLFIAS
VDIQTKSRYY NYAIDWQTGA GCNAAGFFTV FASELSVYTL TVITLERWHT ITYAMQLNRK
VRLRHAVIIM VFGWMFAFTV ALLPIFGISS YMKVSICLPM HIETPFSQAY VIFLLVLNVL
AFVIICICYI CIYFTVRNPN VISSNSDTKI AKRMAILIFT DFLCMAPISF FAISASLRVP
LITVSKSKIL LVLFYPINSC ANPFLYAIFT KTFRRDFFIL LSKFGCCEMQ AQIYRTETSS
SAHNFHTRNG HYPTASKNSD GTIYSLVPLN HLN
