TRHR_SHEEP
ID TRHR_SHEEP Reviewed; 398 AA.
AC Q28596;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thyrotropin-releasing hormone receptor;
DE Short=TRH-R;
DE AltName: Full=Thyroliberin receptor;
GN Name=TRHR;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=9048604; DOI=10.1210/endo.138.3.5007;
RA Bockmann J., Boeckers T.M., Winter C., Wittkowski W., Winterhoff H.,
RA Deufel T., Kreutz M.R.;
RT "Thyrotropin expression in hypophyseal pars tuberalis-specific cells is
RT 3,5,3'-triiodothyronine, thyrotropin-releasing hormone, and pit-1
RT independent.";
RL Endocrinology 138:1019-1028(1997).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X95285; CAA64606.1; -; mRNA.
DR RefSeq; NP_001009407.1; NM_001009407.1.
DR RefSeq; XP_012038762.1; XM_012183372.2.
DR AlphaFoldDB; Q28596; -.
DR SMR; Q28596; -.
DR STRING; 9940.ENSOARP00000015611; -.
DR PRIDE; Q28596; -.
DR Ensembl; ENSOART00000015842; ENSOARP00000015611; ENSOARG00000014552.
DR Ensembl; ENSOART00020022654; ENSOARP00020018778; ENSOARG00020014776.
DR GeneID; 443425; -.
DR KEGG; oas:443425; -.
DR CTD; 7201; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_5_1; -.
DR OMA; SKTWRND; -.
DR OrthoDB; 1255241at2759; -.
DR Proteomes; UP000002356; Chromosome 9.
DR Bgee; ENSOARG00000014552; Expressed in pituitary gland and 3 other tissues.
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:0004997; F:thyrotropin-releasing hormone receptor activity; IEA:InterPro.
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..398
FT /note="Thyrotropin-releasing hormone receptor"
FT /id="PRO_0000070190"
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..398
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 398 AA; 45089 MW; 375A311D3DD2A61A CRC64;
MENETGSELN QTQLQPRAVV ALEYQVVTIL LVLIICGLGI VGNIMVVLVV MRTKHMRTPT
NCYLVSLAVA DLMVLVAAGL PNITDSIYGS WVYGYVGCLC ITYLQYLGIN ASSCSITAFT
IERYIAICHP IKAQFLCTFS RAKKIIIFVW AFTSIYCMLW FFLLDLNIST YKDAIVVSCG
YKISRNYYSP IYLMDFGVFY VVPMILATVL YGFIARILFL SPIPSDPKEN SNTWKNDSTH
QNKNLNSKTS NRYFNSTVSS RKQVTKMLAV VVILFALLWM PYRTLVVVNS FLSSPFQENW
FLLFCRICIY LNSAINPVIY NLMSQKFRAA FRKLCNCKQK PVEKPANYSV ALNYSVIKES
DHFSTELDDI TVTDTYLSAT KVSFDDTCLA SEVTFSQS
