ID I3L9Z2_PIG Unreviewed; 695 AA.
AC I3L9Z2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 76.
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:ENSSSCP00000020856.2,
GN ECO:0000313|VGNC:VGNC:102568};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000020856.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000020856.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000020856.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000020856.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; NP_999551.2; NM_214386.3.
DR AlphaFoldDB; I3L9Z2; -.
DR SMR; I3L9Z2; -.
DR Ensembl; ENSSSCT00000024756.2; ENSSSCP00000020856.2; ENSSSCG00000029084.3.
DR GeneID; 397679; -.
DR KEGG; ssc:397679; -.
DR CTD; 2492; -.
DR VGNC; VGNC:102568; FSHR.
DR GeneTree; ENSGT00940000158952; -.
DR HOGENOM; CLU_006130_1_1_1; -.
DR InParanoid; I3L9Z2; -.
DR OMA; FINFSCG; -.
DR OrthoDB; 1202285at2759; -.
DR TreeFam; TF316814; -.
DR Reactome; R-SSC-375281; Hormone ligand-binding receptors.
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000029084; Expressed in granulosa cell and 2 other cell types or tissues.
DR ExpressionAtlas; I3L9Z2; baseline.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004963; F:follicle-stimulating hormone receptor activity; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0009992; P:intracellular water homeostasis; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001545; P:primary ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0060408; P:regulation of acetylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0033044; P:regulation of chromosome organization; IEA:Ensembl.
DR GO; GO:0032350; P:regulation of hormone metabolic process; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0035092; P:sperm DNA condensation; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
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; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
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 Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR01143; FSHRECEPTOR.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00013; LRRNT; 1.
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:UP000008227};
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..695
FT /note="Follicle-stimulating hormone receptor"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT /id="PRO_5011328719"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 400..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 486..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 529..554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 575..597
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 379..626
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 695 AA; 78131 MW; 6A71F8368F5FE73F CRC64;
MSLLLVSLLA FLTLGSGCHH RICHCSNGVF LCQESKVTEI PPDLPRNAVE LRFVLTKLRV
IPKGAFSGFG DLEKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDPDAFQNLP
NLRYLLISNT GVKHLPAVHK IQSLQKVLLD IQDNINIHTV ERNSFVGLSF ESMILWLSKN
GIREIHNCAF NGTQLDELNL SDNDNLEELP NDVFQGASGP VILDISRTRI HSLPSYGLEN
LKKLRAKSTY NLKKLPSLEK FVTLMEASLT YPSHCCAFAN WRRQISDLHP ICNKSILRQE
VDVMTQARGQ RVSLAEDGES SLAKEFDTMY SEFDYDLCNE VVDVICSPEP DAFNPCEDIM
GHDILRVLIW FISILATTGN IIVLVILITS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS
VDIHTKTQYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TAITLERWHT ITHAMQLQCK
VQLRHAASIM LVGWIFAFTV ALFPIFGISS YMKVSICLPM DIDSPLSQLY VVSLLVLNVL
AFVVICGCYT HIYLTVRNPN IMSSSSDTKI AKRMAMLIFT DFLCMAPISF FAISASLKVP
LITVSKSKIL LVLFYPINSC ANPFLYAIFT KNFRRDVFIL LSKFGCYEMQ AQTYRTENLS
TAHNIHPRNG HCPPAPRITN SSSYTLIPLS RLAQN
//
