FSHR_HORSE
ID FSHR_HORSE Reviewed; 694 AA.
AC P47799;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8198575; DOI=10.1006/bbrc.1994.1689;
RA Robert P., Amsellem S., Christophe S., Benifla J.L., Bellet D., Koman A.,
RA Bidart J.-M.;
RT "Cloning and sequencing of the equine testicular follitropin receptor.";
RL Biochem. Biophys. Res. Commun. 201:201-207(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; S70150; AAB30854.1; -; mRNA.
DR PIR; JC2237; JC2237.
DR AlphaFoldDB; P47799; -.
DR SMR; P47799; -.
DR STRING; 9796.ENSECAP00000010338; -.
DR PaxDb; P47799; -.
DR PRIDE; P47799; -.
DR InParanoid; P47799; -.
DR Proteomes; UP000002281; 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; IPR001611; Leu-rich_rpt.
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; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 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.
DR PROSITE; PS51450; LRR; 3.
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..694
FT /note="Follicle-stimulating hormone receptor"
FT /id="PRO_0000012770"
FT TOPO_DOM 18..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..420
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..464
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..507
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..629
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..694
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 334
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 268
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..345
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..355
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..292
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 292..337
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 441..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 694 AA; 78005 MW; E2F077C5E8CBCA54 CRC64;
MALLLVSLLA FLSLGSGCHH RVCHCSNRVF LCQESKVTEI PSDLPRNALE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDHDAFQNLP
NLQYLLISNT GIKHLPAVHK IQSLQKVLLD IQDNINIHTV ERNSFMGLSF ESTILRLSKN
GIQEIHNCAF NGTQLDELNL SYNNNLEELP NDVFQGASGP VILDISGTRI HSLPNYGLEN
LKKLRARSTY NLKKLPSLEK FVALMEANLT YPSHCCAFAN WRRQTSELQT TCNKSILRQE
VDMTQARGER VSLAEDDESS YPKGFDMMYS EFEYDLCNEV VDVTCSPKPD AFNPCEDIMG
YDILRVLIWF ISILAITGNI IVLVILITSQ YKLTVPRFLM CNLAFADLCI GIYLLLIASV
DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF ASELSVYTLT AITLERWHTI THAMQLECKV
QLRHAASVML VGWIFAFAVA LLPIFGISTY MKVSICLPMD IDSPLSQLYV MSLLVLNVLA
FVVICGCYIH IYLTVRNPNI VSSSSDTKIA KRMAILIFTD FLCMAPISFF AISASLKVPL
ITVSKSKILL VLFYPINSCA NPFLYAIFTK NFRRDFFILL SKFGCYEMQA QLYRTETSST
AHISHPRNGH CPPTPRVING ANCTLVPLSH LAQN
