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FSHR_BOVIN
ID   FSHR_BOVIN              Reviewed;         695 AA.
AC   P35376;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 148.
DE   RecName: Full=Follicle-stimulating hormone receptor;
DE            Short=FSH-R;
DE   AltName: Full=Follitropin receptor;
DE   Flags: Precursor;
GN   Name=FSHR;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Ovary, and Testis;
RX   PubMed=7826612; DOI=10.1002/mrd.1080390202;
RA   Houde A., Lambert A., Saumande J., Silversides D.W., Lussier J.G.;
RT   "Structure of the bovine follicle-stimulating hormone receptor
RT   complementary DNA and expression in bovine tissues.";
RL   Mol. Reprod. Dev. 39:127-135(1994).
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; L22319; AAC37324.1; -; mRNA.
DR   PIR; I45896; I45896.
DR   RefSeq; NP_776486.1; NM_174061.1.
DR   AlphaFoldDB; P35376; -.
DR   SMR; P35376; -.
DR   STRING; 9913.ENSBTAP00000048971; -.
DR   PaxDb; P35376; -.
DR   PRIDE; P35376; -.
DR   GeneID; 281172; -.
DR   KEGG; bta:281172; -.
DR   CTD; 2492; -.
DR   eggNOG; KOG2087; Eukaryota.
DR   InParanoid; P35376; -.
DR   OrthoDB; 257031at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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; 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; 2.
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; Reference proteome; Repeat;
KW   Signal; Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..695
FT                   /note="Follicle-stimulating hormone receptor"
FT                   /id="PRO_0000012768"
FT   TOPO_DOM        18..366
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..421
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..465
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        466..485
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..508
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..528
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        529..550
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        551..573
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..597
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..608
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        609..630
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        631..695
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         335
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        18..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        23..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        275..346
FT                   /evidence="ECO:0000250|UniProtKB:P23945"
FT   DISULFID        276..356
FT                   /evidence="ECO:0000250|UniProtKB:P23945"
FT   DISULFID        276..292
FT                   /evidence="ECO:0000250|UniProtKB:P23945"
FT   DISULFID        292..338
FT                   /evidence="ECO:0000250|UniProtKB:P23945"
FT   DISULFID        442..517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   695 AA;  78085 MW;  18F9DFEFC046380D CRC64;
     MALLLVALLA FLSLGSGCHH RLCHCSNGVF LCQESKVTEI PSDLPRDAVE LRFVLTKLRV
     IPKGAFSGFG DLEKIEISQN DVLEVIEANV FSNLPKLHEI RIEKANNLLY IDPDAFQNLP
     NLRYLLISNT GIKHLPAVHK IQSLQKVLLD IQDNINIHTV ERNSFMGLSF ESMTVWLSKN
     GIQEIHNCAF NGTQLDELNL SDNSNLEELP NDVFQGASGP VILDISRTRI RSLPSYGLEN
     LKKLRAKSTY RLKKLPSLEK FVTLVEASLT YPSHCCAFAN WRRQTSDLHP ICNKSILRQE
     VDDMTQARGQ RVSLAEDDEP SYAKGFDVMY SEFDYDLCNE VVDVTCSPEP DAFNPCEDIM
     GDDILRVLIW FISILAITGN ILVLVILITS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS
     VDVHTKTEYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TAITLERWHT ITHAMQLECK
     VQLRHAASIM LVGWIFAFAV ALFPIFGISS YMKVSICLPM DIDSPLSQLY VMSLLVLNVL
     AFVVICGCYT HIYLTVRNPN ITSSSSDTKI AKRMAMLIFT DFLCMAPISF FAISASLKVP
     LITVSKSKIL LVLFYPINSC ANPFLYAIFT KNFRRDFFIL LSKFGCYEVQ AQTYRSETSS
     TAHNFHPRNG HCPPAPRVTN GSNYTLIPLR HLAKN
 
 
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