ID   TRHR_CHICK              Reviewed;         395 AA.
AC   O93603;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Thyrotropin-releasing hormone receptor;
DE            Short=TRH-R;
DE   AltName: Full=Thyroliberin receptor;
GN   Name=TRHR;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=9681487; DOI=10.1210/endo.139.8.6133;
RA   Sun Y.M., Millar R.P., Ho H., Gershengorn M.C., Illing N.;
RT   "Cloning and characterization of the chicken thyrotropin-releasing hormone
RT   receptor.";
RL   Endocrinology 139:3390-3398(1998).
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; Y18244; CAA77091.1; -; mRNA.
DR   RefSeq; NP_990261.1; NM_204930.1.
DR   AlphaFoldDB; O93603; -.
DR   SMR; O93603; -.
DR   STRING; 9031.ENSGALP00000035808; -.
DR   PaxDb; O93603; -.
DR   GeneID; 395770; -.
DR   KEGG; gga:395770; -.
DR   CTD; 7201; -.
DR   VEuPathDB; HostDB:geneid_395770; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; O93603; -.
DR   OrthoDB; 1255241at2759; -.
DR   PhylomeDB; O93603; -.
DR   PRO; PR:O93603; -.
DR   Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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..395
FT                   /note="Thyrotropin-releasing hormone receptor"
FT                   /id="PRO_0000070191"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..53
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..85
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..217
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..290
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..298
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..321
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..395
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        100..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   395 AA;  44698 MW;  291D9BD2718723CB CRC64;
     MENGTGDEQN HTGLLLSSQE FVTAEYQVVT ILLVLLICGL GIVGNIMVVL VVLRTKHMRT
     PTNCYLVSLA VADLMVLVAA GLPNITESLY KSWVYGYVGC LCITYLQYLG INASSFSITA
     FTIERYIAIC HPIKAQFLCT FSRAKKIIIF VWSFASVYCM LWFFLLDLNI AVYKDTTVVS
     CGYKVSRSYY SPIYMMDFGI FYVLPMVLAT VLYGLIARIL FLNPIPSDPK ENSNTWKNDM
     AQQNKTVNSK MTNKSFNSTI ASRRQVTKML AVVVVLFAFL WMPYRTLVVV NSFLSSPFQE
     NWFLLFCRIC IYLNSAINPV IYNLMSQKFR AAFRKLCNCH LKRDKKPANY SVALNYNVIK
     ESDHFSSEIE DITVTNTYLS SAKTSIGDTC LSSEA