FSHR_NOTEU
ID FSHR_NOTEU Reviewed; 694 AA.
AC Q6YNB6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12211057; DOI=10.1002/mrd.10161;
RA Mattiske D., Pask A.J., Shaw J.M., Shaw G.;
RT "Structure and expression of the follicle-stimulating hormone receptor gene
RT in a marsupial, Macropus eugenii.";
RL Mol. Reprod. Dev. 63:24-31(2002).
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; AY082002; AAL99292.1; -; mRNA.
DR AlphaFoldDB; Q6YNB6; -.
DR SMR; Q6YNB6; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR TreeFam; TF316814; -.
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 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; Repeat; Signal; Sulfation;
KW 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_0000233343"
FT TOPO_DOM 18..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..422
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..466
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..509
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..551
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..598
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..631
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..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 336
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23945"
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 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..347
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..357
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..292
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 292..339
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 443..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 694 AA; 78480 MW; 9C754A595DE94468 CRC64;
MAFLWISFLV FLGSGSGCHH RICHCSDRVF ICQESKVTEI PSDIPRNTVE MRFVLTKLQV
IPRGAFSGFR DLEKIEISQN DALEVIEADV FSNLPKLHEI RIEKANNLVL IDPEAFWNLP
NLRYLLISNT GIKHLPAVYK IQSHQKVLLD IQDNINIRTI ERNSFAGLSS ESEILWLNKN
GIQEIQNQAF NGTQLDELNL SDNINLEDLP NGIFQGANGP VILDISRTRI HSLPSDGLKN
LKKLKARSAY NFKTLPNLDK FAELVEANLT YPSHCCAFAN WRRQAFELHP ICNKSFVRQD
SDDLAMDWGH RRRSVEEEYV SNLDKGFDIT DTELDYDLCN EVVDVACSPK PDAFNPCEDI
MGYNFLRVLI WFISILSITG NIVVLVILIT SQYKLTVPRF LMCNLAFADL CIGIYLLLIA
SVDIHTKSQY HNYAIDWQTG AGCDAAGFFT VFASELSVYT LTAITLERWH TITYAMQLDR
KVRLRHAASI MLIGWIFAFS VALLPIFGVS SYMKVSICLP MDIDSPLSQF YVISLLVLNV
LASVIICTCY THIYFTVRNP NIISSTSDAK IAKRMAMLIF TDFLCMAPIS FFAISASVKM
PLITVSKSKI LLVLFYPINS CANPFLYAVF TKTFRRDFFI LLSKFGCCEM QAQIYRTETS
STVHSSHPRN GQCPLMAKSN SGAVYKLVPL NHLS
