GPR26_RAT
ID GPR26_RAT Reviewed; 337 AA.
AC Q9QXI3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=G-protein coupled receptor 26;
GN Name=Gpr26;
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=Brain;
RX PubMed=10684976; DOI=10.1016/s0167-4781(99)00241-9;
RA Lee D.K., Lynch K.R., Nguyen T., Im D.-S., Cheng R., Saldivia V.R., Liu Y.,
RA Liu I.S.C., Heng H.H.Q., Seeman P., George S.R., O'Dowd B.F., Marchese A.;
RT "Cloning and characterization of additional members of the G protein-
RT coupled receptor family.";
RL Biochim. Biophys. Acta 1490:311-323(2000).
CC -!- FUNCTION: Orphan receptor. Displays a significant level of constitutive
CC activity. Its effect is mediated by G(s)-alpha protein that stimulate
CC adenylate cyclase, resulting in an elevation of intracellular cAMP (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in extracts of several brain regions
CC including striatum, pons, cerebellum and cortex. Not detected in
CC numerous peripheral tissue extracts, except in testis. In the brain,
CC detected in cortical structures including the anterior cingulate area,
CC posterior cingulate and the frontoparietal, somatosensory and piriform
CC cortices. Prominent also in the olfactory tubercle, the islands of
CC Calleja, ventromedial and posterior nuclei of the hypothalamus, the
CC medial septal nucleus, nucleus of the diagonal band and the ventral
CC tegmental area. Localized also to hippocampal structures, with signals
CC strongest over the CA2 and CA3 regions of Ammon's horn and less so over
CC the dentate gyrus. Expressed in the caudate putamen only in its most
CC caudal portion, with a decreasing gradient of signal from the dorsal to
CC ventral aspect. Strong expression associated with a single pontine
CC structure, the inferior olivary nucleus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF208288; AAF21012.1; -; mRNA.
DR RefSeq; NP_620196.1; NM_138841.1.
DR AlphaFoldDB; Q9QXI3; -.
DR SMR; Q9QXI3; -.
DR STRING; 10116.ENSRNOP00000067319; -.
DR PaxDb; Q9QXI3; -.
DR Ensembl; ENSRNOT00000075540; ENSRNOP00000067319; ENSRNOG00000047057.
DR GeneID; 192153; -.
DR KEGG; rno:192153; -.
DR CTD; 2849; -.
DR RGD; 619843; Gpr26.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000183001; -.
DR HOGENOM; CLU_009579_3_5_1; -.
DR InParanoid; Q9QXI3; -.
DR OMA; HQYKKTW; -.
DR OrthoDB; 1039292at2759; -.
DR PhylomeDB; Q9QXI3; -.
DR PRO; PR:Q9QXI3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000047057; Expressed in frontal cortex and 2 other tissues.
DR Genevisible; Q9QXI3; RN.
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:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="G-protein coupled receptor 26"
FT /id="PRO_0000069547"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 79..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 337 AA; 37805 MW; CD7E2381F085F2DD CRC64;
MNSWDAGLAG LLVGTIGVSL LSNGLVLLCL LHSADIRRQA PALFTLNLTC GNLLCTVVNM
PLTLAGVVAQ RQPAGDRLCR LAAFLDTFLA ANSMLSMAAL SIDRWVAVVF PLSYRAKMRL
RDAAFMVAYT WLHALTFPAT ALALSWLGFH QLYASCTLCS RRPDERLRFA VFTSAFHALS
FLLSFIVLCF TYLKVLKVAR FHCKRIDVIT MQTLVLLVDI HPSVRERCLE EQKRRRQRAT
KKISTFIGTF LVCFAPYVIT RLVELFSTAP IDSHWGVLSK CLAYSKAASD PFVYSLLRHQ
YRRSCKELLN RIFNRRSIHS VGLTGDSHSQ NILPVSE
