TRHR_RAT
ID TRHR_RAT Reviewed; 412 AA.
AC Q01717; Q63948; Q63949;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Thyrotropin-releasing hormone receptor;
DE Short=TRH-R;
DE AltName: Full=Thyroliberin receptor;
GN Name=Trhr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=1317787; DOI=10.1210/endo.130.6.1317787;
RA Zhao D., Yang J., Jones K.E., Gerald C., Suzuki Y., Hogan P.G., Chin W.W.,
RA Tashjian A.H. Jr.;
RT "Molecular cloning of a complementary deoxyribonucleic acid encoding the
RT thyrotropin-releasing hormone receptor and regulation of its messenger
RT ribonucleic acid in rat GH cells.";
RL Endocrinology 130:3529-3536(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=1377915; DOI=10.1042/bj2840891;
RA de la Pena P., Delgado L.M., del Camino D., Barros F.;
RT "Cloning and expression of the thyrotropin-releasing hormone receptor from
RT GH3 rat anterior pituitary cells.";
RL Biochem. J. 284:891-899(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=8387312; DOI=10.1677/jme.0.0100199;
RA Sellar R.E., Taylor P.L., Lamb R.F., Zabavnik J., Anderson L., Eidne K.A.;
RT "Functional expression and molecular characterization of the thyrotrophin-
RT releasing hormone receptor from the rat anterior pituitary gland.";
RL J. Mol. Endocrinol. 10:199-206(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=1338727; DOI=10.1016/0303-7207(92)90116-n;
RA Eidne K.A., Sellar R.E., Couper G., Anderson L., Taylor P.L.;
RT "Molecular cloning and characterisation of the rat pituitary gonadotropin-
RT releasing hormone (GnRH) receptor.";
RL Mol. Cell. Endocrinol. 90:R5-R9(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8275956; DOI=10.1210/endo.134.1.8275956;
RA Kimura N., Arai K., Sahara Y., Suzuki H., Kimura N.;
RT "Estradiol transcriptionally and posttranscriptionally up-regulates
RT thyrotropin-releasing hormone receptor messenger ribonucleic acid in rat
RT pituitary cells.";
RL Endocrinology 134:432-440(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TRH-R(412) AND TRH-R(387)).
RC TISSUE=Pituitary;
RX PubMed=7509436; DOI=10.1016/0169-328x(93)90062-t;
RA Satoh T., Feng P., Wilber J.F.;
RT "A truncated isoform of the thyrotropin-releasing hormone receptor is
RT expressed in the rat central nervous system as well as in the pituitary
RT gland.";
RL Brain Res. Mol. Brain Res. 20:353-356(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-261.
RC STRAIN=Wistar;
RX PubMed=1373613; DOI=10.1016/0006-291x(92)91202-2;
RA Yamada M., Monden T., Satoh T., Iizuka M., Murakami M., Iriuchijima T.,
RA Mori M.;
RT "Differential regulation of thyrotropin-releasing hormone receptor mRNA
RT levels by thyroid hormone in vivo and in vitro (GH3 cells).";
RL Biochem. Biophys. Res. Commun. 184:367-372(1992).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=1334485; DOI=10.1016/s0021-9258(18)35664-3;
RA de la Pena P., Delgado L.M., del Camino D., Barros F.;
RT "Two isoforms of the thyrotropin-releasing hormone receptor generated by
RT alternative splicing have indistinguishable functional properties.";
RL J. Biol. Chem. 267:25703-25708(1992).
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:0000250|UniProtKB:P34981}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P34981};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=TRH-R(412);
CC IsoId=Q01717-1; Sequence=Displayed;
CC Name=TRH-R(387);
CC IsoId=Q01717-2; Sequence=VSP_001952;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M90308; AAA42277.1; -; mRNA.
DR EMBL; X64630; CAA45913.1; -; mRNA.
DR EMBL; X66726; CAA47263.1; -; mRNA.
DR EMBL; D17469; BAA04289.1; -; mRNA.
DR EMBL; S60053; AAB26491.1; -; mRNA.
DR EMBL; S69160; AAB29945.2; -; mRNA.
DR EMBL; S69161; AAB29946.2; -; mRNA.
DR EMBL; S51512; AAB24549.1; -; mRNA.
DR PIR; I56444; I56444.
DR PIR; S23436; S23436.
DR RefSeq; NP_037179.1; NM_013047.3. [Q01717-1]
DR AlphaFoldDB; Q01717; -.
DR SMR; Q01717; -.
DR BioGRID; 247601; 5.
DR DIP; DIP-41967N; -.
DR STRING; 10116.ENSRNOP00000006783; -.
DR BindingDB; Q01717; -.
DR ChEMBL; CHEMBL4553; -.
DR DrugCentral; Q01717; -.
DR GuidetoPHARMACOLOGY; 363; -.
DR GlyGen; Q01717; 2 sites.
DR iPTMnet; Q01717; -.
DR PhosphoSitePlus; Q01717; -.
DR PaxDb; Q01717; -.
DR GeneID; 25570; -.
DR KEGG; rno:25570; -.
DR UCSC; RGD:3904; rat. [Q01717-1]
DR CTD; 7201; -.
DR RGD; 3904; Trhr.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q01717; -.
DR OrthoDB; 1255241at2759; -.
DR PhylomeDB; Q01717; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q01717; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0004997; F:thyrotropin-releasing hormone receptor activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:RGD.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..412
FT /note="Thyrotropin-releasing hormone receptor"
FT /id="PRO_0000070189"
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..412
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"
FT VAR_SEQ 376..412
FT /note="YVSTTKVSFDDTCLASEKNGPSSCTYGYSLTAKQEKI -> RMDPVLVHMDI
FT L (in isoform TRH-R(387))"
FT /evidence="ECO:0000305"
FT /id="VSP_001952"
FT CONFLICT 59
FT /note="A -> P (in Ref. 6 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="I -> T (in Ref. 6 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="N -> T (in Ref. 6; AAB29945/AAB29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="Missing (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46609 MW; 52B35C9849D48A72 CRC64;
MENETVSELN QTELPPQVAV ALEYQVVTIL LVVVICGLGI VGNIMVVLVV MRTKHMRTAT
NCYLVSLAVA DLMVLVAAGL PNITDSIYGS WVYGYVGCLC ITYLQYLGIN ASSCSITAFT
IERYIAICHP IKAQFLCTFS RAKKIIIFVW AFTSIYCMLW FFLLDLNIST YKDAIVISCG
YKISRNYYSP IYLMDFGVFY VMPMILATVL YGFIARILFL NPIPSDPKEN SKTWKNDSTH
QNKNMNLNTT NRCFNSTVSS RKQVTKMLAV VVILFALLWM PYRTLVVVNS FLSSPFQENW
FLLFCRICIY LNSAINPVIY NLMSQKFRAA FRKLCNCKQK PTEKAANYSV ALNYSVIKES
DRFSTELDDI TVTDTYVSTT KVSFDDTCLA SEKNGPSSCT YGYSLTAKQE KI
