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GNRHR_MOUSE
ID   GNRHR_MOUSE             Reviewed;         327 AA.
AC   Q01776; Q61611;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Gonadotropin-releasing hormone receptor;
DE            Short=GnRH receptor;
DE            Short=GnRH-R;
GN   Name=Gnrhr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1324422; DOI=10.1210/mend.6.7.1324422;
RA   Tsutsumi M., Zhou W., Millar R.P., Mellon P.L., Roberts J.L.,
RA   Flanagan C.A., Dong K., Gillo B., Sealfon S.C.;
RT   "Cloning and functional expression of a mouse gonadotropin-releasing
RT   hormone receptor.";
RL   Mol. Endocrinol. 6:1163-1169(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1328228; DOI=10.1016/s0021-9258(19)36602-5;
RA   Reinhart J., Mertz L.M., Catt K.J.;
RT   "Molecular cloning and expression of cDNA encoding the murine gonadotropin-
RT   releasing hormone receptor.";
RL   J. Biol. Chem. 267:21281-21284(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RA   Clay C.M., Nelson S.E., Campion C.E., Digregorio G.B.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that
CC       mediates the action of GnRH to stimulate the secretion of the
CC       gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating
CC       hormone (FSH). This receptor mediates its action by association with G-
CC       proteins that activate a phosphatidylinositol-calcium second messenger
CC       system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Pituitary gland.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L01119; AAB59636.1; -; mRNA.
DR   EMBL; M93108; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L33789; AAA37716.1; -; Genomic_DNA.
DR   EMBL; L33778; AAA37716.1; JOINED; Genomic_DNA.
DR   EMBL; L33788; AAA37716.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS19379.1; -.
DR   PIR; A44013; A44013.
DR   RefSeq; NP_034453.1; NM_010323.2.
DR   AlphaFoldDB; Q01776; -.
DR   SMR; Q01776; -.
DR   CORUM; Q01776; -.
DR   STRING; 10090.ENSMUSP00000031172; -.
DR   BindingDB; Q01776; -.
DR   ChEMBL; CHEMBL3232679; -.
DR   DrugCentral; Q01776; -.
DR   GuidetoPHARMACOLOGY; 256; -.
DR   GlyGen; Q01776; 3 sites.
DR   iPTMnet; Q01776; -.
DR   PhosphoSitePlus; Q01776; -.
DR   PaxDb; Q01776; -.
DR   PRIDE; Q01776; -.
DR   Antibodypedia; 12675; 441 antibodies from 37 providers.
DR   DNASU; 14715; -.
DR   Ensembl; ENSMUST00000031172; ENSMUSP00000031172; ENSMUSG00000029255.
DR   GeneID; 14715; -.
DR   KEGG; mmu:14715; -.
DR   UCSC; uc008xxl.1; mouse.
DR   CTD; 2798; -.
DR   MGI; MGI:95790; Gnrhr.
DR   VEuPathDB; HostDB:ENSMUSG00000029255; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244841; -.
DR   HOGENOM; CLU_009579_15_2_1; -.
DR   InParanoid; Q01776; -.
DR   OMA; SEPVNHF; -.
DR   OrthoDB; 858238at2759; -.
DR   PhylomeDB; Q01776; -.
DR   TreeFam; TF106499; -.
DR   Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 14715; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Gnrhr; mouse.
DR   PRO; PR:Q01776; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q01776; protein.
DR   Bgee; ENSMUSG00000029255; Expressed in lumbar subsegment of spinal cord and 33 other tissues.
DR   ExpressionAtlas; Q01776; baseline and differential.
DR   Genevisible; Q01776; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0004968; F:gonadotropin-releasing hormone receptor activity; IBA:GO_Central.
DR   GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; ISO:MGI.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001658; GphnRH_fam_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00529; GNADOTRPHINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..327
FT                   /note="Gonadotropin-releasing hormone receptor"
FT                   /id="PRO_0000069489"
FT   TOPO_DOM        1..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..184
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..231
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..299
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        76
FT                   /note="M -> I (in Ref. 3; AAA37716)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  37684 MW;  FDDC7B985306FC9F CRC64;
     MANNASLEQD PNHCSAINNS IPLIQGKLPT LTVSGKIRVT VTFFLFLLST AFNASFLLKL
     QKWTQKRKKG KKLSRMKVLL KHLTLANLLE TLIVMPLDGM WNITVQWYAG EFLCKVLSYL
     KLFSMYAPAF MMVVISLDRS LAITQPLAVQ SNSKLEQSMI SLAWILSIVF AGPQLYIFRM
     IYLADGSGPT VFSQCVTHCS FPQWWHQAFY NFFTFGCLFI IPLLIMLICN AKIIFALTRV
     LHQDPRKLQL NQSKNNIPRA RLRTLKMTVA FATSFVVCWT PYYVLGIWYW FDPEMLNRVS
     EPVNHFFFLF AFLNPCFDPL IYGYFSL
 
 
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