GP135_RAT
ID GP135_RAT Reviewed; 457 AA.
AC Q7TQN7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=G-protein coupled receptor 135;
GN Name=Gpr135;
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].
RX PubMed=14623098; DOI=10.1016/s0014-5793(03)01196-7;
RA Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C.,
RA Schioeth H.B.;
RT "Seven evolutionarily conserved human rhodopsin G protein-coupled receptors
RT lacking close relatives.";
RL FEBS Lett. 554:381-388(2003).
CC -!- FUNCTION: Orphan receptor. Has spontaneous activity for beta-arrestin
CC recruitment. Shows a reciprocal regulatory interaction with the
CC melatonin receptor MTNR1B most likely through receptor heteromerization
CC (By similarity). {ECO:0000250|UniProtKB:Q8IZ08}.
CC -!- SUBUNIT: Interacts with MTNR1B (By similarity). Interacts with ARRB1
CC and ARRB2 in a spontaneous and agonist-independent manner; leading to
CC the internalization of GPR135 in the endosomal compartment (By
CC similarity). {ECO:0000250|UniProtKB:Q8IZ08}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IZ08};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8IZ08}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with ARRB2/beta-arrestin-2 in the
CC endosome. {ECO:0000250|UniProtKB:Q8IZ08}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY288430; AAP72139.1; -; mRNA.
DR RefSeq; NP_861436.1; NM_181771.1.
DR AlphaFoldDB; Q7TQN7; -.
DR SMR; Q7TQN7; -.
DR STRING; 10116.ENSRNOP00000005933; -.
DR GlyGen; Q7TQN7; 1 site.
DR PhosphoSitePlus; Q7TQN7; -.
DR PaxDb; Q7TQN7; -.
DR Ensembl; ENSRNOT00000005933; ENSRNOP00000005933; ENSRNOG00000004499.
DR GeneID; 314213; -.
DR KEGG; rno:314213; -.
DR UCSC; RGD:727844; rat.
DR CTD; 64582; -.
DR RGD; 727844; Gpr135.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182998; -.
DR HOGENOM; CLU_048891_0_0_1; -.
DR InParanoid; Q7TQN7; -.
DR OMA; EVAMWAC; -.
DR OrthoDB; 770796at2759; -.
DR PhylomeDB; Q7TQN7; -.
DR TreeFam; TF333332; -.
DR PRO; PR:Q7TQN7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004499; Expressed in frontal cortex and 6 other tissues.
DR Genevisible; Q7TQN7; RN.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:1990763; F:arrestin family protein binding; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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; 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; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..457
FT /note="G-protein coupled receptor 135"
FT /id="PRO_0000069614"
FT TOPO_DOM 1..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 49581 MW; 879BE6477F8EC0BA CRC64;
MEEQARPPSR PAASATLPGS AHPGGAASTA TAAALSFSSV ATVTLGNQSD AGRPEAAGSR
GPAPLLWHGA AVAAQALVLL LIFLLSSLGN CAVMGVIVKH RQLRTVTNAF ILSLSLSDLL
TALLCLPAAF LDLFAPPGDS GPWRSFCAAS RFFSSCFGIV STFSVALISL DRYCAIVRPP
RDKLGRRRAL QLLAGAWLAA LGFSLPWELL RAPREPPTPQ SFHRCLYRTS PDPAQLGAAY
SVGLVVACYL LPFLLMCFCR YHICKTVRLS DVRVRPMTTY ARVLRFFSEV RTATTVLIMI
VFVICCWGPY CFLVLLAATR QGQTTQAPSL LNVAAVWLTW ANGAINPVIY AIRNPNISMF
LGRNREEGYR TRNMDVFLPS QGLGFQARSR NRLRNGCANR LGACSRMPSS NPASGSGGEV
VMWARKNPVV LFFREDPPDP VMAVYKQHKS ETRDSSI
