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Database: UniProt
Entry: F6TCJ6_CALJA
LinkDB: F6TCJ6_CALJA
Original site: F6TCJ6_CALJA 
ID   F6TCJ6_CALJA            Unreviewed;       670 AA.
AC   F6TCJ6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   11-DEC-2019, entry version 46.
DE   RecName: Full=Follicle-stimulating hormone receptor {ECO:0000256|RuleBase:RU361222};
DE   AltName: Full=Follitropin receptor {ECO:0000256|RuleBase:RU361222};
GN   Name=FSHR {ECO:0000256|RuleBase:RU361222,
GN   ECO:0000313|Ensembl:ENSCJAP00000019653};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000019653, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000019653, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000019653}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361222};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU361222}.
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   Ensembl; ENSCJAT00000020772; ENSCJAP00000019653; ENSCJAG00000010640.
DR   eggNOG; KOG2087; Eukaryota.
DR   eggNOG; ENOG410XR1T; LUCA.
DR   GeneTree; ENSGT00940000158952; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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; 2.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF12369; GnHR_trans; 1.
DR   Pfam; PF13306; LRR_5; 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.
DR   PROSITE; PS51450; LRR; 4.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU361222};
KW   G-protein coupled receptor {ECO:0000256|RuleBase:RU361222};
KW   Leucine-rich repeat {ECO:0000256|SAAS:SAAS00619388};
KW   Membrane {ECO:0000256|RuleBase:RU361222};
KW   Receptor {ECO:0000256|RuleBase:RU361222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Repeat {ECO:0000256|SAAS:SAAS00619387};
KW   Signal {ECO:0000256|RuleBase:RU361222};
KW   Transducer {ECO:0000256|RuleBase:RU361222};
KW   Transmembrane {ECO:0000256|RuleBase:RU361222};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361222}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   CHAIN           18..670
FT                   /note="Follicle-stimulating hormone receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT                   /id="PRO_5005129939"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        373..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        418..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        460..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        503..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        549..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   DOMAIN          353..600
FT                   /note="G_PROTEIN_RECEP_F1_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
SQ   SEQUENCE   670 AA;  75385 MW;  05EF6B990948F90C CRC64;
     MALLLASLLA FLSLGSGCHH RICHCSNRVF LCQESKVTEI PSDLPRNAVE LRFVLTKLRA
     IPKGAFSGFG DLERIEISQN DILEVIEADV FSNLPKLHEI RIEKANNLLY INAEAFQNLP
     NLRYLLISNT GIKHLPDVHK IHSLQKVILW LNKNGIQEIQ NCAFNGTQLD ELNLSNNNNL
     KELPNDVFHG ASGPVVLDIS RTRIHSLPSY GLENLKKLRA RSTYNLKRLP SLEELVALME
     ASLTYPSHCC AFANWRRQIS ELHPICNKSI LRQEVDDMTQ AKGQRVSLAE YDESSYSREF
     DMMYNEFDYG LCNEVVEVTC SPEPDAFNPC EDIMGYNILR ILIWFISILA ITGNIIVLVI
     LTTSQYKLTV PRFLMCNLAF ADLCIGIYLL LIASVDIHTK SQYHNYAIDW QTGGGCDAAG
     FFTVFASELS VYTLTAITLE RWYTITHAMQ LDCKVQLRHA ASVMVVGWIF AFAAALFPIF
     GISSYMKVSI CLPMDIDSPL SQLYVMSLLV LNVLAFVVIC GCYTHIYLTV RNPNIVSSSS
     DTRIAKRMAM LIFTDFVCMA PISFFAISAS LKVPLITVSK AKILLVLFYP VNSCANPFLY
     AIFTKNFRRD FFILLSKFGC YEMQAQIYKT ETSSTAHNSH PRNGHCSSAP RVTNGSSHIL
     VPLSHLTQKQ
//
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