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D(3) dopamine receptor (Dopamine D3 receptor)

 DRD3_HUMAN              Reviewed;         400 AA.
P35462; A1A4V5; Q4VBM8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
25-OCT-2017, entry version 175.
RecName: Full=D(3) dopamine receptor;
AltName: Full=Dopamine D3 receptor;
Name=DRD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2129115;
Giros B., Martres M.-P., Sokoloff P., Schwartz J.-C.;
"Gene cloning of human dopaminergic D3 receptor and identification of
its chromosome.";
C. R. Acad. Sci. III, Sci. Vie 311:501-508(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=8415635; DOI=10.1073/pnas.90.19.8942;
Schmauss C., Haroutunian V., Davis K.L., Davidson M.;
"Selective loss of dopamine D3-type receptor mRNA expression in
parietal and motor cortices of patients with chronic schizophrenia.";
Proc. Natl. Acad. Sci. U.S.A. 90:8942-8946(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=7961889;
Liu K., Bergson C., Levenson R., Schmauss C.;
"On the origin of mRNA encoding the truncated dopamine D3-type
receptor D3nf and detection of D3nf-like immunoreactivity in human
brain.";
J. Biol. Chem. 269:29220-29226(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Fishburn C.S., Park B.-H., Fuchs S.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-9.
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-9.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH PALM.
PubMed=16386234; DOI=10.1016/j.abb.2005.10.027;
Basile M., Lin R., Kabbani N., Karpa K., Kilimann M., Simpson I.,
Kester M.;
"Paralemmin interacts with D3 dopamine receptors: implications for
membrane localization and cAMP signaling.";
Arch. Biochem. Biophys. 446:60-68(2006).
[9]
PHOSPHORYLATION BY GRK4, SUBCELLULAR LOCATION, INTERACTION WITH GRK4,
AND FUNCTION.
PubMed=19520868; DOI=10.1074/jbc.M109.003665;
Villar V.A.M., Jones J.E., Armando I., Palmes-Saloma C., Yu P.,
Pascua A.M., Keever L., Arnaldo F.B., Wang Z., Luo Y., Felder R.A.,
Jose P.A.;
"G protein-coupled receptor kinase 4 (GRK4) regulates the
phosphorylation and function of the dopamine D3 receptor.";
J. Biol. Chem. 284:21425-21434(2009).
[10]
INTERACTION WITH FLNA.
PubMed=26460884; DOI=10.1021/acs.biochem.5b00975;
Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J.,
Karnik S.S.;
"G Protein-Coupled Receptors Directly Bind Filamin A with High
Affinity and Promote Filamin Phosphorylation.";
Biochemistry 54:6673-6683(2015).
[11]
X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH THE ANTAGONIST
ETICLOPRIDE, DISULFIDE BONDS, AND MEMBRANE TOPOLOGY.
PubMed=21097933; DOI=10.1126/science.1197410;
Chien E.Y., Liu W., Zhao Q., Katritch V., Han G.W., Hanson M.A.,
Shi L., Newman A.H., Javitch J.A., Cherezov V., Stevens R.C.;
"Structure of the human dopamine D3 receptor in complex with a D2/D3
selective antagonist.";
Science 330:1091-1095(2010).
[12]
VARIANT GLY-9.
Lannfelt T., Sokoloff P., Martres M.-P., Pilon C., Giros B.,
Joensson E., Sedvall G., Schwartz J.-C.;
"Amino-acid substitution in the dopamine D3 receptor as useful
polymorphism for investigating psychiatric disorders.";
Psychiatr. Genet. 2:249-256(1992).
[13]
VARIANT GLY-9.
PubMed=9034004;
DOI=10.1002/(SICI)1096-8628(19970221)74:1<40::AID-AJMG9>3.0.CO;2-Z;
Chen C.-H., Liu M.-Y., Wei F.-C., Koong F.-J., Hwu H.-G., Hsiao K.-J.;
"Further evidence of no association between Ser9Gly polymorphism of
dopamine D3 receptor gene and schizophrenia.";
Am. J. Med. Genet. 74:40-43(1997).
[14]
VARIANT GLY-9.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[15]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[16]
VARIANT GLY-9, AND INVOLVEMENT IN SUSCEPTIBILITY TO ETM1.
PubMed=16650084; DOI=10.1111/j.1399-0004.2006.00600.x;
Lucotte G., Lagarde J.-P., Funalot B., Sokoloff P.;
"Linkage with the Ser9Gly DRD3 polymorphism in essential tremor
families.";
Clin. Genet. 69:437-440(2006).
[17]
VARIANT GLY-9, CHARACTERIZATION OF VARIANT GLY-9, AND INVOLVEMENT IN
SUSCEPTIBILITY TO ETM1.
PubMed=16809426; DOI=10.1073/pnas.0508189103;
Jeanneteau F., Funalot B., Jankovic J., Deng H., Lagarde J.-P.,
Lucotte G., Sokoloff P.;
"A functional variant of the dopamine D3 receptor is associated with
risk and age-at-onset of essential tremor.";
Proc. Natl. Acad. Sci. U.S.A. 103:10753-10758(2006).
-!- FUNCTION: Dopamine receptor whose activity is mediated by G
proteins which inhibit adenylyl cyclase. Promotes cell
proliferation. {ECO:0000269|PubMed:19520868}.
-!- SUBUNIT: Interacts with CLIC6 (By similarity). Interacts with GRK4
(PubMed:19520868). Interacts with PALM (PubMed:16386234).
Interacts with FLNA (via filamin repeat 21); increases PKA-
mediated phosphorylation of FLNA (PubMed:26460884).
{ECO:0000250|UniProtKB:P19020, ECO:0000269|PubMed:16386234,
ECO:0000269|PubMed:19520868, ECO:0000269|PubMed:26460884}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19520868};
Multi-pass membrane protein {ECO:0000269|PubMed:19520868}.
Note=Both membrane-bound and scattered in the cytoplasm during
basal conditions. Receptor stimulation results in the rapid
internalization and sequestration of the receptors at the
perinuclear area (5 and 15 minutes), followed by the dispersal of
the receptors to the membrane (30 minutes). DRD3 and GRK4 co-
localize in lipid rafts of renal proximal tubule cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=D3;
IsoId=P35462-1; Sequence=Displayed;
Name=3;
IsoId=P35462-3; Sequence=VSP_040570;
-!- TISSUE SPECIFICITY: Brain.
-!- PTM: Phosphorylated by GRK4 (GRK4-alpha and GRK4-gamma).
{ECO:0000269|PubMed:19520868}.
-!- DISEASE: Tremor, hereditary essential 1 (ETM1) [MIM:190300]: A
common movement disorder mainly characterized by postural tremor
of the arms. Head, legs, trunk, voice, jaw, and facial muscles
also may be involved. The condition can be aggravated by emotions,
hunger, fatigue and temperature extremes, and may cause a
functional disability or even incapacitation. Inheritance is
autosomal dominant. {ECO:0000269|PubMed:16650084,
ECO:0000269|PubMed:16809426}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=AAA03543.1; Type=Frameshift; Positions=288; Evidence={ECO:0000305};
Sequence=AAA64369.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=DRD3";
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EMBL; L20469; AAA03543.1; ALT_FRAME; mRNA.
EMBL; AH003061; AAA64369.1; ALT_SEQ; Genomic_DNA.
EMBL; U32499; AAA73929.1; -; mRNA.
EMBL; AC092896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79610.1; -; Genomic_DNA.
EMBL; BC095510; AAH95510.1; -; mRNA.
EMBL; BC128123; AAI28124.1; -; mRNA.
CCDS; CCDS2978.1; -. [P35462-1]
CCDS; CCDS33829.1; -. [P35462-3]
PIR; A48258; A48258.
PIR; A55419; A55419.
PIR; G01977; G01977.
RefSeq; NP_000787.2; NM_000796.5.
RefSeq; NP_001269492.1; NM_001282563.2.
RefSeq; NP_001277738.1; NM_001290809.1.
RefSeq; NP_387512.3; NM_033663.5.
UniGene; Hs.121478; -.
PDB; 3PBL; X-ray; 2.89 A; A/B=2-221, A/B=319-400.
PDBsum; 3PBL; -.
ProteinModelPortal; P35462; -.
SMR; P35462; -.
BioGrid; 108148; 10.
DIP; DIP-5976N; -.
IntAct; P35462; 6.
STRING; 9606.ENSP00000373169; -.
BindingDB; P35462; -.
ChEMBL; CHEMBL234; -.
DrugBank; DB05766; ACP-104.
DrugBank; DB06288; Amisulpride.
DrugBank; DB00543; Amoxapine.
DrugBank; DB00714; Apomorphine.
DrugBank; DB01238; Aripiprazole.
DrugBank; DB09207; AS-8112.
DrugBank; DB06216; Asenapine.
DrugBank; DB01200; Bromocriptine.
DrugBank; DB00248; Cabergoline.
DrugBank; DB09014; Captodiame.
DrugBank; DB06016; Cariprazine.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB01239; Chlorprothixene.
DrugBank; DB00363; Clozapine.
DrugBank; DB01184; Domperidone.
DrugBank; DB00988; Dopamine.
DrugBank; DB00502; Haloperidol.
DrugBank; DB04946; Iloperidone.
DrugBank; DB01235; Levodopa.
DrugBank; DB00589; Lisuride.
DrugBank; DB00408; Loxapine.
DrugBank; DB01403; Methotrimeprazine.
DrugBank; DB06148; Mianserin.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB00334; Olanzapine.
DrugBank; DB01267; Paliperidone.
DrugBank; DB01186; Pergolide.
DrugBank; DB01100; Pimozide.
DrugBank; DB00413; Pramipexole.
DrugBank; DB01224; Quetiapine.
DrugBank; DB00409; Remoxipride.
DrugBank; DB00734; Risperidone.
DrugBank; DB00268; Ropinirole.
DrugBank; DB05271; Rotigotine.
DrugBank; DB05280; SLV 308.
DrugBank; DB00391; Sulpiride.
DrugBank; DB13025; Tiapride.
DrugBank; DB01392; Yohimbine.
DrugBank; DB00246; Ziprasidone.
GuidetoPHARMACOLOGY; 216; -.
TCDB; 9.A.14.3.9; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P35462; -.
PhosphoSitePlus; P35462; -.
SwissPalm; P35462; -.
DMDM; 1169206; -.
PaxDb; P35462; -.
PeptideAtlas; P35462; -.
PRIDE; P35462; -.
DNASU; 1814; -.
Ensembl; ENST00000383673; ENSP00000373169; ENSG00000151577.
Ensembl; ENST00000460779; ENSP00000419402; ENSG00000151577.
Ensembl; ENST00000467632; ENSP00000420662; ENSG00000151577.
GeneID; 1814; -.
KEGG; hsa:1814; -.
CTD; 1814; -.
DisGeNET; 1814; -.
EuPathDB; HostDB:ENSG00000151577.12; -.
GeneCards; DRD3; -.
H-InvDB; HIX0030774; -.
H-InvDB; HIX0163472; -.
HGNC; HGNC:3024; DRD3.
MalaCards; DRD3; -.
MIM; 126451; gene.
MIM; 190300; phenotype.
neXtProt; NX_P35462; -.
Orphanet; 862; Hereditary essential tremor.
PharmGKB; PA27479; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000239242; -.
HOVERGEN; HBG106962; -.
InParanoid; P35462; -.
KO; K04146; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P35462; -.
TreeFam; TF334382; -.
Reactome; R-HSA-390651; Dopamine receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SignaLink; P35462; -.
GenomeRNAi; 1814; -.
PRO; PR:P35462; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000151577; -.
CleanEx; HS_DRD3; -.
ExpressionAtlas; P35462; baseline and differential.
Genevisible; P35462; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0042995; C:cell projection; IEA:Ensembl.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
GO; GO:0035240; F:dopamine binding; IEA:Ensembl.
GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IDA:BHF-UCL.
GO; GO:0008144; F:drug binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046717; P:acid secretion; ISS:BHF-UCL.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
GO; GO:0048148; P:behavioral response to cocaine; IEP:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:BHF-UCL.
GO; GO:0042417; P:dopamine metabolic process; IC:BHF-UCL.
GO; GO:0002031; P:G-protein coupled receptor internalization; IDA:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0035483; P:gastric emptying; IEA:Ensembl.
GO; GO:0007612; P:learning; NAS:BHF-UCL.
GO; GO:0007611; P:learning or memory; NAS:BHF-UCL.
GO; GO:0007626; P:locomotory behavior; ISS:BHF-UCL.
GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; ISS:BHF-UCL.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:BHF-UCL.
GO; GO:0045776; P:negative regulation of blood pressure; ISS:BHF-UCL.
GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IEA:Ensembl.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:BHF-UCL.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:BHF-UCL.
GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:BHF-UCL.
GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0060134; P:prepulse inhibition; IMP:BHF-UCL.
GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; IEA:Ensembl.
GO; GO:0030814; P:regulation of cAMP metabolic process; IDA:BHF-UCL.
GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; ISS:BHF-UCL.
GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; IC:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEP:BHF-UCL.
GO; GO:0042493; P:response to drug; ISS:BHF-UCL.
GO; GO:0034776; P:response to histamine; IDA:BHF-UCL.
GO; GO:0043278; P:response to morphine; ISS:BHF-UCL.
GO; GO:0035176; P:social behavior; NAS:BHF-UCL.
GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0008542; P:visual learning; ISS:BHF-UCL.
CDD; cd15310; 7tmA_D3_dopamine_R; 1.
InterPro; IPR001620; Dopamine_D3_rcpt.
InterPro; IPR000929; Dopamine_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00568; DOPAMINED3R.
PRINTS; PR00242; DOPAMINER.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 400 D(3) dopamine receptor.
/FTId=PRO_0000069397.
TOPO_DOM 1 32 Extracellular. {ECO:0000305}.
TRANSMEM 33 55 Helical; Name=1.
TOPO_DOM 56 65 Cytoplasmic.
TRANSMEM 66 88 Helical; Name=2.
TOPO_DOM 89 104 Extracellular.
TRANSMEM 105 126 Helical; Name=3.
TOPO_DOM 127 149 Cytoplasmic.
TRANSMEM 150 170 Helical; Name=4.
TOPO_DOM 171 187 Extracellular.
TRANSMEM 188 212 Helical; Name=5.
TOPO_DOM 213 329 Cytoplasmic.
TRANSMEM 330 351 Helical; Name=6.
TOPO_DOM 352 366 Extracellular.
TRANSMEM 367 388 Helical; Name=7.
TOPO_DOM 389 400 Cytoplasmic.
REGION 189 196 Agonist binding.
REGION 342 350 Agonist binding.
BINDING 110 110 Agonist.
CARBOHYD 12 12 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 19 19 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 103 181 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:21097933}.
DISULFID 355 358 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:21097933}.
VAR_SEQ 287 320 SPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGV -> M
(in isoform 3).
{ECO:0000303|PubMed:8415635}.
/FTId=VSP_040570.
VARIANT 9 9 S -> G (associated with susceptibility to
ETM1; gain of function; dbSNP:rs6280).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16641997,
ECO:0000269|PubMed:16650084,
ECO:0000269|PubMed:16809426,
ECO:0000269|PubMed:9034004,
ECO:0000269|Ref.12}.
/FTId=VAR_003463.
CONFLICT 396 396 K -> L (in Ref. 7; AAH95510).
{ECO:0000305}.
HELIX 35 56 {ECO:0000244|PDB:3PBL}.
HELIX 63 81 {ECO:0000244|PDB:3PBL}.
HELIX 83 91 {ECO:0000244|PDB:3PBL}.
HELIX 100 133 {ECO:0000244|PDB:3PBL}.
HELIX 135 140 {ECO:0000244|PDB:3PBL}.
STRAND 143 145 {ECO:0000244|PDB:3PBL}.
HELIX 147 169 {ECO:0000244|PDB:3PBL}.
TURN 170 172 {ECO:0000244|PDB:3PBL}.
HELIX 186 196 {ECO:0000244|PDB:3PBL}.
HELIX 198 216 {ECO:0000244|PDB:3PBL}.
HELIX 322 353 {ECO:0000244|PDB:3PBL}.
HELIX 362 386 {ECO:0000244|PDB:3PBL}.
HELIX 388 398 {ECO:0000244|PDB:3PBL}.
SEQUENCE 400 AA; 44225 MW; 2CDA789D78378DDA CRC64;
MASLSQLSSH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL
QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN
LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV
CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ
QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK
LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV
SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC


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