ID   GPR52_BOVIN             Reviewed;         361 AA.
AC   A6QLE7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=G-protein coupled receptor 52 {ECO:0000250|UniProtKB:Q9Y2T5};
GN   Name=GPR52 {ECO:0000250|UniProtKB:Q9Y2T5};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: G- protein coupled receptor activated by antipsychotics
CC       reserpine leading to an increase in intracellular cAMP and its
CC       internalization. May play a role in locomotor activity through
CC       modulation of dopamine, NMDA and ADORA2A-induced locomotor activity.
CC       These behavioral changes are accompanied by modulation of the dopamine
CC       receptor signaling pathway in striatum. Modulates HTT level via cAMP-
CC       dependent but PKA independent mechanisms throught activation of RAB39B
CC       that translocates HTT to the endoplasmic reticulum, thus avoiding
CC       proteasome degradation. {ECO:0000250|UniProtKB:Q9Y2T5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; BC147938; AAI47939.1; -; mRNA.
DR   RefSeq; NP_001093774.1; NM_001100304.1.
DR   AlphaFoldDB; A6QLE7; -.
DR   SMR; A6QLE7; -.
DR   STRING; 9913.ENSBTAP00000052985; -.
DR   PaxDb; A6QLE7; -.
DR   PRIDE; A6QLE7; -.
DR   GeneID; 506159; -.
DR   KEGG; bta:506159; -.
DR   CTD; 9293; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; A6QLE7; -.
DR   OrthoDB; 1099557at2759; -.
DR   Proteomes; UP000009136; 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:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="G-protein coupled receptor 52"
FT                   /id="PRO_0000307679"
FT   TOPO_DOM        1..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   361 AA;  41172 MW;  833BA5B36D5E8F0B CRC64;
     MNDSRWTEWR ILNTSSGILN VSERHSCPLG FGHYSAVDVC IFETIVIVLL TFLIIAGNLT
     VIFVFHCAPL LHHYTTSYFI QTMAYADLFV GVSCLVPTLS LLHYSTGIHE SLTCQVFGYI
     ISVLKSVSMA CLACISVDRY LAITKPLSYN QLVTPCRLRI CIILIWIYSC LIFLPSFFGW
     GKPGYHGDIF EWCATSWLTS AYFTGFIVCL LYAPAALVVC FTYFHIFKIC RQHTKEINDR
     RARFPSHEAA ASRDAGHSPD RRYAMVLFRI TSVFYMLWLP YIIYFLLESS RVLDNPTLSF
     LTTWLAISNS FCNCVIYSLS NSVFRLGLRR LSETMCTSCM CVKDKEARDP KPRKRANSCS
     I