DRD2A_XENLA
ID DRD2A_XENLA Reviewed; 442 AA.
AC P24628;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=D(2) dopamine receptor A;
DE Short=D2R-A;
DE AltName: Full=D2R 1;
GN Name=drd2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1826663; DOI=10.1016/0014-5793(91)80364-9;
RA Martens G.J.M., Molhuizen H.O.F., Groeneveld D., Roubos E.W.;
RT "Cloning and sequence analysis of brain cDNA encoding a Xenopus D2 dopamine
RT receptor.";
RL FEBS Lett. 281:85-89(1991).
CC -!- FUNCTION: This is one of the five types (D1 to D5) of receptors for
CC dopamine. The activity of this receptor is mediated by G proteins which
CC inhibits adenylyl cyclase. In Xenopus D2R is involved in the regulation
CC of the melanotrope cells of the intermediate pituitary during
CC background adaptation of the animal.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14416};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain; pituitary.
CC -!- PTM: Palmitoylated. Palmitoylation is probably required for proper
CC localization to the plasma membrane and stability of the receptor.
CC {ECO:0000250|UniProtKB:P14416}.
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; X59500; CAA42088.1; -; mRNA.
DR PIR; S14827; DYXLD2.
DR RefSeq; NP_001095212.1; NM_001101742.1.
DR AlphaFoldDB; P24628; -.
DR SMR; P24628; -.
DR GeneID; 378584; -.
DR KEGG; xla:378584; -.
DR CTD; 378584; -.
DR Xenbase; XB-GENE-1005782; drd2.L.
DR OrthoDB; 1215361at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 378584; Expressed in brain.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:1903530; P:regulation of secretion by cell; IEA:UniProt.
DR InterPro; IPR001922; Dopamine_D2_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00567; DOPAMINED2R.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Golgi apparatus; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..442
FT /note="D(2) dopamine receptor A"
FT /id="PRO_0000069393"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 32..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 55..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 88..102
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 146..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 167..182
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 183..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 208..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 373..394
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 395..408
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 409..430
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 431..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 273..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 188
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT LIPID 442
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14416"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 398..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 442 AA; 49738 MW; 95AD1B779680C6BB CRC64;
MDPQNLSMYN DDINNGTNGT AVDQKPHYNY YAMLLTLLVF VIVFGNVLVC IAVSREKALQ
TTTNYLIVSL AVADLLVATL VMPWAVYMEV VGEWRFSRIH CDIFVTLDVM MCTASILNLC
AISIDRYTAV AMPMLYNTRY SSKRRVTVMI SVVWVLSFAI SCPLLFGLNN TGSKVCIIDN
PAFVIYSSIV SFYVPFIVTL LVYVQIYIVL RKRRKRVNTK RNSRGVAVDA HKDKCTHPED
VKLCSVFVKS NGSFPADKKK VILVQEAGKH PEDMEMEMMS STSPPEKTKH KSASPDHNQL
AVPATSNQCK NASLTSPVES PYKAEKNGHP KDSTKPAKVF EIQSMPNGKT RTSIKTMSKK
KLSQHKEKKA TQMLAIVLGV FIICWLPFFI IHILNMHCNC NIPQALYSAF TWLGYVNSAV
NPIIYTTFNV EFRKAFIKIL HC
