TRHR_MOUSE
ID TRHR_MOUSE Reviewed; 393 AA.
AC P21761;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Thyrotropin-releasing hormone receptor;
DE Short=TRH-R;
DE AltName: Full=Thyroliberin receptor;
GN Name=Trhr;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Pituitary;
RX PubMed=2175902; DOI=10.1073/pnas.87.24.9514;
RA Straub R.E., Frech G.C., Joho R.H., Gershengorn M.C.;
RT "Expression cloning of a cDNA encoding the mouse pituitary thyrotropin-
RT releasing hormone receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9514-9518(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1324930; DOI=10.1016/s0021-9258(18)41925-4;
RA Narayanan C.S., Fujimoto J., Geras-Raaka E., Gershengorn M.C.;
RT "Regulation by thyrotropin-releasing hormone (TRH) of TRH receptor mRNA
RT degradation in rat pituitary GH3 cells.";
RL J. Biol. Chem. 267:17296-17303(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-393.
RC TISSUE=Pituitary;
RX PubMed=9156522; DOI=10.1677/jme.0.0160197;
RA Jones K.E., Brubaker J.H., Chin W.W.;
RT "An alternative splice variant of the mouse TRH receptor mRNA is the major
RT form expressed in the mouse pituitary gland.";
RL J. Mol. Endocrinol. 16:197-204(1996).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11181534; DOI=10.1210/endo.142.3.8019;
RA Harder S., Lu X., Wang W., Buck F., Gershengorn M.C., Bruhn T.O.;
RT "Regulator of G protein signaling 4 suppresses basal and thyrotropin
RT releasing-hormone (TRH)-stimulated signaling by two mouse TRH receptors,
RT TRH-R(1) and TRH-R(2).";
RL Endocrinology 142:1188-1194(2001).
CC -!- FUNCTION: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand
CC binding, this G-protein-coupled receptor triggers activation of the
CC phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
CC {ECO:0000269|PubMed:11181534, ECO:0000269|PubMed:2175902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11181534,
CC ECO:0000269|PubMed:2175902}; Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M59811; AAA40480.1; -; mRNA.
DR EMBL; M94384; AAA40437.1; -; mRNA.
DR EMBL; L48936; AAA81559.1; -; mRNA.
DR CCDS; CCDS37068.1; -.
DR PIR; A39251; A39251.
DR RefSeq; NP_038724.1; NM_013696.2.
DR AlphaFoldDB; P21761; -.
DR SMR; P21761; -.
DR STRING; 10090.ENSMUSP00000036320; -.
DR BindingDB; P21761; -.
DR ChEMBL; CHEMBL2467; -.
DR DrugCentral; P21761; -.
DR GuidetoPHARMACOLOGY; 363; -.
DR GlyGen; P21761; 2 sites.
DR iPTMnet; P21761; -.
DR PhosphoSitePlus; P21761; -.
DR SwissPalm; P21761; -.
DR PaxDb; P21761; -.
DR PRIDE; P21761; -.
DR ProteomicsDB; 298291; -.
DR Antibodypedia; 13449; 308 antibodies from 31 providers.
DR DNASU; 22045; -.
DR Ensembl; ENSMUST00000038856; ENSMUSP00000036320; ENSMUSG00000038760.
DR Ensembl; ENSMUST00000110289; ENSMUSP00000105918; ENSMUSG00000038760.
DR Ensembl; ENSMUST00000226626; ENSMUSP00000154650; ENSMUSG00000038760.
DR GeneID; 22045; -.
DR KEGG; mmu:22045; -.
DR UCSC; uc007vpo.1; mouse.
DR CTD; 7201; -.
DR MGI; MGI:98824; Trhr.
DR VEuPathDB; HostDB:ENSMUSG00000038760; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; P21761; -.
DR OMA; SKTWRND; -.
DR OrthoDB; 1255241at2759; -.
DR PhylomeDB; P21761; -.
DR TreeFam; TF326170; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 22045; 3 hits in 71 CRISPR screens.
DR PRO; PR:P21761; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P21761; protein.
DR Bgee; ENSMUSG00000038760; Expressed in facial nucleus and 58 other tissues.
DR ExpressionAtlas; P21761; baseline and differential.
DR Genevisible; P21761; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004997; F:thyrotropin-releasing hormone receptor activity; ISO:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002120; TRH_rcpt_1.
DR PANTHER; PTHR46061; PTHR46061; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00751; THYROLIBRINR.
DR PRINTS; PR01846; TRHRFAMILY.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Thyrotropin-releasing hormone receptor"
FT /id="PRO_0000070188"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..288
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 393 AA; 44559 MW; 8739B75D1A0FCCFC CRC64;
MENDTVSEMN QTELQPQAAV ALEYQVVTIL LVVIICGLGI VGNIMVVLVV MRTKHMRTPT
NCYLVSLAVA DLMVLVAAGL PNITDSIYGS WVYGYVGCLC ITYLQYLGIN ASSCSITAFT
IERYIAICHP IKAQFLCTFS RAKKIIIFVW AFTSIYCMLW FFLLDLNIST YKNAVVVSCG
YKISRNYYSP IYLMDFGVFY VVPMILATVL YGFIARILFL NPIPSDPKEN SKMWKNDSIH
QNKNLNLNAT NRCFNSTVSS RKQVTKMLAV VVILFALLWM PYRTLVVVNS FLSSPFQENW
FLLFCRICIY LNSAINPVIY NLMSQKFRAA FRKLCNCKQK PTEKAANYSV ALNYSVIKES
DRFSTELEDI TVTDTYVSTT KVSFDDTCLA SEN
