ID A0A452FU22_CAPHI Unreviewed; 669 AA.
AC A0A452FU22;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Follicle-stimulating hormone receptor {ECO:0000256|ARBA:ARBA00021226, ECO:0000256|RuleBase:RU361222};
DE AltName: Full=Follitropin receptor {ECO:0000256|ARBA:ARBA00030636, ECO:0000256|RuleBase:RU361222};
GN Name=FSHR {ECO:0000256|RuleBase:RU361222,
GN ECO:0000313|Ensembl:ENSCHIP00000027719.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000027719.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000027719.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000027719.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU361222}.
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.
CC {ECO:0000256|ARBA:ARBA00025966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000256|RuleBase:RU361222}.
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DR EMBL; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FU22; -.
DR SMR; A0A452FU22; -.
DR Ensembl; ENSCHIT00000035587.1; ENSCHIP00000027719.1; ENSCHIG00000023353.1.
DR GeneTree; ENSGT00940000158952; -.
DR Proteomes; UP000291000; Chromosome 11.
DR Bgee; ENSCHIG00000023353; Expressed in testis and 1 other cell type or tissue.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004963; F:follicle-stimulating hormone receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR CDD; cd15360; 7tmA_FSH-R; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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 PANTHER; PTHR24372:SF5; FOLLICLE-STIMULATING HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF12369; GnHR_trans; 1.
DR Pfam; PF13306; LRR_5; 2.
DR PRINTS; PR01143; FSHRECEPTOR.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361222};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU361222};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361222};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361222};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361222};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU361222};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361222};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361222}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT CHAIN 18..669
FT /note="Follicle-stimulating hormone receptor"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT /id="PRO_5018816317"
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 460..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 503..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 353..600
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 669 AA; 75329 MW; 4F4927C203624B26 CRC64;
MALFLVALLA FLSLGSGCHH RLCHCSNGVF LCQESKVTEM PSDLPRDAVE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEAIEANV FSNLPKLHEI RIEKANNLLY IDPDAFQNLP
NLRYLLISNT GIKHLPAVHK IQSFQKVLLW LSKNGIQEIH NCAFNGTQLD ELNLSDNSNL
EELPNDVFQG ASGPVILDIS RTRIRSLPSY GLENLKKLRA KSTYHLKKLP SLEKFVTLVE
ASLTYPSHCC AFANWRRQTS DLHPICNKSI LRQEVDDMTQ ARGQRISLAE DDEPSYAKGF
DMMYSEFDYD LCNEMVDVTC SPEPDAFNPC EDIMGYDILR VLIWFISILA ITGNILVLVI
LITSQYKLTV PRFLMCNLAF ADLCIGIYLL LIASVDVHTK SQYHNYAIDW QTGAGCDAAG
FFTVFASELS VYTLTAITLE RWHTITHAMQ LECKVQLRHA ASIMLVGWVF AFAVALFPIF
GISSYMKVSI CLPMDIDSPL SQLYVMSLLV LNVLAFVVIC GCYTHIYLTV RNPNITSSSS
DTKIAKRMAM LIFTDFLCMA PISFFAISAS LKVPLITVSK SKILLVLFYP INSCANPFLY
AIFTRNFRRD FFILLSKFGC YEVQAQTYRS ETSFTAHNFH PRNGHCPPAP RVTNGSNYTL
IPLRHLAKN
//
