DRD2B_XENLA
ID DRD2B_XENLA Reviewed; 345 AA.
AC P34973;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D(2) dopamine receptor B;
DE Short=D2R-B;
DE AltName: Full=D2R 2;
DE Flags: Fragment;
GN Name=drd2-b;
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=8504826; DOI=10.1111/j.1432-1033.1993.tb17887.x;
RA Martens G.J.M., Groenen P.M.A., Groeneveld D., van Riel M.C.H.M.;
RT "Expression of the Xenopus D2 dopamine receptor. Tissue-specific regulation
RT and two transcriptionally active genes but no evidence for alternative
RT splicing.";
RL Eur. J. Biochem. 213:1349-1354(1993).
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}.
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DR EMBL; X72902; CAA51412.1; -; mRNA.
DR PIR; S36959; S36959.
DR AlphaFoldDB; P34973; -.
DR SMR; P34973; -.
DR Proteomes; UP000186698; Genome assembly.
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..345
FT /note="D(2) dopamine receptor B"
FT /id="PRO_0000069394"
FT TOPO_DOM <1..10
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 11..32
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 33..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 54..74
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 75..90
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..115
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 276..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 298..311
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 334..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 166..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 345
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14416"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 9..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 301..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
SQ SEQUENCE 345 AA; 38996 MW; 1B1A492E0FB9A091 CRC64;
EWRFSRIHCD IFVTLDVMMC TASILNLCAI SIDRYTAVAM PMLYNTRYSS KRRVTVMISV
VWVLSFAISC PLLFGLNNTA STVCIIDNPA FVIYSSIVSF YVPFIVTLLV YVQIYIVLRK
RRKRVNTKRN SHGVGVDAHK DKCTHPEDVK LCAVFVKSNG SFPAEKKKVE AGNHPEDMEM
EMMSSTSPPE KTKHKSASPE HQLAVPATSN QCNNVNLPTP VNSPYKAENN GHSKDSTQPA
KVFEIQSMPN GKTRTSIKTM SKRKISQHKE KKATQMLAIV LGVFIICWLP FFITHILNMH
CNCNIPQALY SAFTWLGYVN SAVNPIIYTT FNVEFRKAFI KILHC
