FSHR_EQUAS
ID FSHR_EQUAS Reviewed; 687 AA.
AC Q95179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Follicle-stimulating hormone receptor;
DE Short=FSH-R;
DE AltName: Full=Follitropin receptor;
DE Flags: Precursor;
GN Name=FSHR;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9195473; DOI=10.1677/jme.0.0180193;
RA Richard F., Martinat N., Remy J.-J., Salesse R., Combarnous Y.;
RT "Cloning, sequencing and in vitro functional expression of recombinant
RT donkey follicle-stimulating hormone receptor: a new insight into the
RT binding specificity of gonadotrophin receptors.";
RL J. Mol. Endocrinol. 18:193-202(1997).
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; U73659; AAB18245.1; -; mRNA.
DR RefSeq; NP_001310711.1; NM_001323782.1.
DR AlphaFoldDB; Q95179; -.
DR SMR; Q95179; -.
DR GeneID; 106835472; -.
DR KEGG; eai:106835472; -.
DR CTD; 2492; -.
DR OrthoDB; 257031at2759; -.
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 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 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; Repeat; Signal; Sulfation;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..687
FT /note="Follicle-stimulating hormone receptor"
FT /id="PRO_0000012769"
FT TOPO_DOM 18..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..413
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..457
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..500
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..542
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..589
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..600
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..622
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..687
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 327
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 23..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 275..338
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..348
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 276..292
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 292..330
FT /evidence="ECO:0000250|UniProtKB:P23945"
FT DISULFID 434..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 687 AA; 76938 MW; FC3AF0B55531DA9A CRC64;
MALLLVSLLA FLSLGSGCHH QVCHYSNRVF LCQESKVTEI PSDLPRNALE LRFVLTKLRV
IPKGAFSGFG DLKKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDHDAFQNLP
NLQYLLISNT GIKHLPAVHK IQSLQKVLLD IQDNINIHIV ERNSFMGLSF ESMILRLSKN
GIQEIHNCAF NGTQLDELNL SDNNNLEELP NDVFQGASGP VILDISGTRI HSLPNYGLEN
LKKLRARSTY NLKKLPSLEK FVALMEASLT YPSHCCAFAN WRQQTSELQT TCNKSILRQE
VDMTQARGER VSLAEDDESM MYSEFDYDLC NEVVDVTCSP KPDAFNPCED IMGYDILRVL
IWFISILAIT GNIIVLVILI TSQYKLTVPR FLMCNLAFAD LCIGIYLLLI ASVDIHTKSQ
YHNYAIDWQT GAGCDAAGFF TVFGSELSVY TLTAITLERW HTITHAMQLE CKVQLRHAAS
VMLVGWIFGF GVGLLPIFGI STYMKVSICL PMDIDSPLSQ LYVMSLLVLN VLAFVVICGC
YTHIYLTVRN PNIVSSSSDT KIAKRMGILI FTDFLCMAPI SFFGISASLK VALITVSKSK
ILLVLFYPIN SCANPFLYAI FTKNFRRDFF ILLSKFGCYE MQAQTYRTET SSTGHISHPK
NGPCPPTPRV TNGANCTLVP LSHLAQN
