ID A0A3L8SRY6_CHLGU Unreviewed; 665 AA.
AC A0A3L8SRY6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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 ORFNames=DV515_00004178 {ECO:0000313|EMBL:RLW07191.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW07191.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW07191.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW07191.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW07191.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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|ARBA:ARBA00003266, ECO:0000256|RuleBase:RU361222}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW07191.1}.
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DR EMBL; QUSF01000008; RLW07191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SRY6; -.
DR STRING; 44316.ENSEGOP00005003757; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
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; 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; 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; 1.
DR Pfam; PF13855; LRR_8; 1.
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|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:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 372..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 458..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 501..526
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 547..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 351..598
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 665 AA; 74893 MW; 9D864B639525DD92 CRC64;
MTQDRGEENG YQGDQRILTQ EEQVVPKWLR IASGLSRVLP HPYGMVLPEG SPSKGWIQPE
DFLVKAPQEE KAFVCLVLLQ SGEQSSGYSN LLGNGVRCAE RQLLPASSEE ISQNDALEVI
EANVFSNLPK LHEIRIEKAN SLVYIDKDAF QHLPSLRYLL ISNTGLRFLP AVHKVHSFQK
VLLDIQDNIN IRTIERNSFM NLSSESVILW LNKNGIQDIE DHAFNGTYLD ELNLSDNHNL
EKLPNEVFQG ANGPIVLTEL HPICSISHVK QDFEEKPGKK LRRRSAAEDY ISNYGIGFDP
AENEFDYGLC NEVVNVACSP KPDAFNPCED IMGYNILRVL IWFINILAIT GNTVVLIILI
SSQYKLTVPR FLMCNLAFAD LCIGIYLLFI ASVDIQTKSQ YYNYAIDWQT GAGCNAAGFF
AVFASELSVY TLTVITVERW HTITYAMQLH RKVRLRHAVI VMIFGWVFAF TVALLPIFGV
SSYMKVSICL PMDIETLFAQ AYVMFLLVLN VLAFVVICIC YTCIYFTVRN PNVVSSNSDT
KIAKRMAVLI FTDFLCMAPI SFFAISASLK VPLITVSNSK ILLVLFYPIN SCANPFLYAI
FTKTFRRDFF ILLSKFGCCE MQAQIYRTEI SSSAHTFHTR NGHCPPASKN GDGTIYSLVP
LNHLN
//
