FSHR_BOVIN
ID FSHR_BOVIN Reviewed; 695 AA.
AC P35376;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Ovary, and Testis;
RX PubMed=7826612; DOI=10.1002/mrd.1080390202;
RA Houde A., Lambert A., Saumande J., Silversides D.W., Lussier J.G.;
RT "Structure of the bovine follicle-stimulating hormone receptor
RT complementary DNA and expression in bovine tissues.";
RL Mol. Reprod. Dev. 39:127-135(1994).
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; L22319; AAC37324.1; -; mRNA.
DR PIR; I45896; I45896.
DR RefSeq; NP_776486.1; NM_174061.1.
DR AlphaFoldDB; P35376; -.
DR SMR; P35376; -.
DR STRING; 9913.ENSBTAP00000048971; -.
DR PaxDb; P35376; -.
DR PRIDE; P35376; -.
DR GeneID; 281172; -.
DR KEGG; bta:281172; -.
DR CTD; 2492; -.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; P35376; -.
DR OrthoDB; 257031at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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: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_0000012768"
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..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..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 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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:0000250"
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"
SQ SEQUENCE 695 AA; 78085 MW; 18F9DFEFC046380D CRC64;
MALLLVALLA FLSLGSGCHH RLCHCSNGVF LCQESKVTEI PSDLPRDAVE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDPDAFQNLP
NLRYLLISNT GIKHLPAVHK IQSLQKVLLD IQDNINIHTV ERNSFMGLSF ESMTVWLSKN
GIQEIHNCAF NGTQLDELNL SDNSNLEELP NDVFQGASGP VILDISRTRI RSLPSYGLEN
LKKLRAKSTY RLKKLPSLEK FVTLVEASLT YPSHCCAFAN WRRQTSDLHP ICNKSILRQE
VDDMTQARGQ RVSLAEDDEP SYAKGFDVMY SEFDYDLCNE VVDVTCSPEP DAFNPCEDIM
GDDILRVLIW FISILAITGN ILVLVILITS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS
VDVHTKTEYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TAITLERWHT ITHAMQLECK
VQLRHAASIM LVGWIFAFAV ALFPIFGISS YMKVSICLPM DIDSPLSQLY VMSLLVLNVL
AFVVICGCYT HIYLTVRNPN ITSSSSDTKI AKRMAMLIFT DFLCMAPISF FAISASLKVP
LITVSKSKIL LVLFYPINSC ANPFLYAIFT KNFRRDFFIL LSKFGCYEVQ AQTYRSETSS
TAHNFHPRNG HCPPAPRVTN GSNYTLIPLR HLAKN
