ID   DRD4_MOUSE              Reviewed;         387 AA.
AC   P51436; O35838; Q7TT80; Q8BXS4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 193.
DE   RecName: Full=Dopamine receptor D4 {ECO:0000305};
DE   AltName: Full=D(2C) dopamine receptor;
DE   AltName: Full=Dopamine D4 receptor;
GN   Name=Drd4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=7698326; DOI=10.1016/0014-5793(95)00168-9;
RA   Fishburn C.S., Carmon S., Fuchs S.;
RT   "Molecular cloning and characterisation of the gene encoding the murine D4
RT   dopamine receptor.";
RL   FEBS Lett. 361:215-219(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8584230; DOI=10.1016/0304-3940(95)12021-u;
RA   Suzuki T., Kobayashi K., Nagatsu T.;
RT   "Genomic structure and tissue distribution of the mouse dopamine D4
RT   receptor.";
RL   Neurosci. Lett. 199:69-72(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9323127; DOI=10.1016/s0092-8674(00)80365-7;
RA   Rubinstein M., Phillips T.J., Bunzow J.R., Falzone T.L., Dziewczapolski G.,
RA   Zhang G., Fang Y., Larson J.L., McDougall J.A., Chester J.A., Saez C.,
RA   Pugsley T.A., Gershanik O., Low M.J., Grandy D.K.;
RT   "Mice lacking dopamine D4 receptors are supersensitive to ethanol, cocaine,
RT   and methamphetamine.";
RL   Cell 90:991-1001(1997).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10531457; DOI=10.1523/jneurosci.19-21-09550.1999;
RA   Dulawa S.C., Grandy D.K., Low M.J., Paulus M.P., Geyer M.A.;
RT   "Dopamine D4 receptor-knock-out mice exhibit reduced exploration of novel
RT   stimuli.";
RL   J. Neurosci. 19:9550-9556(1999).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=18303015; DOI=10.1074/jbc.m708473200;
RA   Rondou P., Haegeman G., Vanhoenacker P., Van Craenenbroeck K.;
RT   "BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by
RT   a Cul3-based E3 ligase.";
RL   J. Biol. Chem. 283:11083-11096(2008).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24048828; DOI=10.1523/jneurosci.2039-13.2013;
RA   Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R.,
RA   Iuvone P.M.;
RT   "Circadian rhythm of contrast sensitivity is regulated by a dopamine-
RT   neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in
RT   retinal ganglion cells.";
RL   J. Neurosci. 33:14989-14997(2013).
RN   [10] {ECO:0007744|PDB:6IQL}
RP   X-RAY CRYSTALLOGRAPHY AND 304-387, ACTIVITY REGULATION, AND DISULFIDE
RP   BONDS.
RX   PubMed=31750832; DOI=10.7554/elife.48822;
RA   Zhou Y., Cao C., He L., Wang X., Zhang X.C.;
RT   "Crystal structure of dopamine receptor D4 bound to the subtype selective
RT   ligand, L745870.";
RL   Elife 8:e48822-e48822(2019).
CC   -!- FUNCTION: G protein-coupled receptor for dopamine, a catecholamine
CC       neurotransmitter hormone that functions as the brain's 'reward
CC       chemical', driving motivation, reinforcement learning and pleasure (By
CC       similarity). In addition to dopamine, also activated by epinephrine and
CC       norepinephrine, and by numerous synthetic agonists and drugs (By
CC       similarity). Ligand binding causes a conformation change that triggers
CC       signaling via guanine nucleotide-binding proteins (G proteins) and
CC       modulates the activity of downstream effectors, such as adenylate
CC       cyclase (By similarity). Dopamine receptors can be classified in two
CC       categories: (1) DRD4 (together with DRD2 and DRD3) is a D2-type
CC       receptor and is coupled to G(i)/G(o) G proteins, mediating inhibition
CC       of adenylate cyclase activity, while D1-type receptors (DRD1 and DRD5)
CC       are coupled to G(s) G proteins and promote activation of adenylate
CC       cyclase activity (By similarity). D1- and D2-type dopamine receptors
CC       have antagonistic effects, particularly in the brain's striatum, where
CC       they govern voluntary movement and reward: D1-type receptors generally
CC       stimulate neural activity and promotes action, while D2-type receptors
CC       tend to inhibit neural activity and suppress movement (By similarity).
CC       DRD4 is expressed in the mesolimbic system of the brain, an area of the
CC       brain that regulates emotion and complex behavior (PubMed:10531457).
CC       Modulates the circadian rhythm of contrast sensitivity by regulating
CC       the rhythmic expression of NPAS2 in the retinal ganglion cells
CC       (PubMed:24048828). {ECO:0000250|UniProtKB:P21917,
CC       ECO:0000269|PubMed:10531457, ECO:0000269|PubMed:24048828}.
CC   -!- ACTIVITY REGULATION: Specifically inhibited by antagonist L745870.
CC       {ECO:0000269|PubMed:31750832}.
CC   -!- SUBUNIT: Forms homo- and heterooligomers with DRD2 (By similarity).
CC       Interacts with CLIC6 (By similarity). Interacts with GPRASP1 (By
CC       similarity). May interact with ADORA2A (By similarity).
CC       {ECO:0000250|UniProtKB:P21917, ECO:0000250|UniProtKB:P30729}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21917};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:31750832}.
CC   -!- TISSUE SPECIFICITY: Detected in olfactory bulb, hypothalamus, olfactory
CC       tubercle, brainstem and striatum. {ECO:0000269|PubMed:7698326}.
CC   -!- PTM: Ubiquitinated via both ester and isopeptide bonds; leading to its
CC       degradation. {ECO:0000250|UniProtKB:P21917}.
CC   -!- PTM: Palmitoylated. Palmitoylation of the C-terminal Cys is important
CC       for normal expression at the cell membrane.
CC       {ECO:0000250|UniProtKB:P21917}.
CC   -!- DISRUPTION PHENOTYPE: Mice display reduced behavioral responses to
CC       novelty, including lower exploration of new environments, decreased
CC       novelty-seeking, and increased sensitivity to anxiety-related stimuli
CC       (PubMed:10531457). They also show hypersensitivity to drugs,
CC       characterized by a dose-dependent, heightened locomotor response to
CC       stimulants such as cocaine, methamphetamine and 20% ethanol
CC       (PubMed:9323127). Mice show a significant reduction in daytime contrast
CC       sensitivity (PubMed:24048828). {ECO:0000269|PubMed:10531457,
CC       ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:9323127}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: In contrast to human protein, does not interact with KLHL12
CC       and is not ubiquitinated by the BCR(KLHL12) complex.
CC       {ECO:0000305|PubMed:18303015}.
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DR   EMBL; U19880; AAC52190.1; -; Genomic_DNA.
DR   EMBL; S80929; AAB50730.1; -; Genomic_DNA.
DR   EMBL; S80920; AAB50730.1; JOINED; Genomic_DNA.
DR   EMBL; S80927; AAB50730.1; JOINED; Genomic_DNA.
DR   EMBL; S80928; AAB50730.1; JOINED; Genomic_DNA.
DR   EMBL; AK044379; BAC31893.1; -; mRNA.
DR   EMBL; CH466531; EDL18041.1; -; Genomic_DNA.
DR   EMBL; BC016086; AAH16086.1; -; mRNA.
DR   EMBL; BC051421; AAH51421.2; -; mRNA.
DR   CCDS; CCDS22007.1; -.
DR   PIR; I49246; I49246.
DR   RefSeq; NP_031904.1; NM_007878.4.
DR   PDB; 6IQL; X-ray; 3.50 A; A/B=23-219, A/B=304-387.
DR   AlphaFoldDB; P51436; -.
DR   SMR; P51436; -.
DR   DIP; DIP-61454N; -.
DR   FunCoup; P51436; 498.
DR   IntAct; P51436; 3.
DR   STRING; 10090.ENSMUSP00000026569; -.
DR   BindingDB; P51436; -.
DR   ChEMBL; CHEMBL2574; -.
DR   DrugCentral; P51436; -.
DR   GlyCosmos; P51436; 1 site, No reported glycans.
DR   GlyGen; P51436; 2 sites.
DR   iPTMnet; P51436; -.
DR   PhosphoSitePlus; P51436; -.
DR   SwissPalm; P51436; -.
DR   PaxDb; 10090-ENSMUSP00000026569; -.
DR   Antibodypedia; 22579; 492 antibodies from 39 providers.
DR   DNASU; 13491; -.
DR   Ensembl; ENSMUST00000026569.6; ENSMUSP00000026569.5; ENSMUSG00000025496.6.
DR   GeneID; 13491; -.
DR   KEGG; mmu:13491; -.
DR   UCSC; uc009kkm.1; mouse.
DR   AGR; MGI:94926; -.
DR   CTD; 1815; -.
DR   MGI; MGI:94926; Drd4.
DR   VEuPathDB; HostDB:ENSMUSG00000025496; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000160974; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; P51436; -.
DR   OMA; AADYNFP; -.
DR   OrthoDB; 10010417at2759; -.
DR   PhylomeDB; P51436; -.
DR   Reactome; R-MMU-390651; Dopamine receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 13491; 4 hits in 79 CRISPR screens.
DR   PRO; PR:P51436; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P51436; protein.
DR   Bgee; ENSMUSG00000025496; Expressed in retinal neural layer and 50 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISO:GO_Central.
DR   GO; GO:0043679; C:axon terminus; ISO:GO_Central.
DR   GO; GO:0005938; C:cell cortex; ISO:GO_Central.
DR   GO; GO:0005813; C:centrosome; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:GO_Central.
DR   GO; GO:0044292; C:dendrite terminus; ISO:GO_Central.
DR   GO; GO:1901588; C:dendritic microtubule; ISO:GO_Central.
DR   GO; GO:0043198; C:dendritic shaft; ISO:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; ISO:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0043204; C:perikaryon; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:GO_Central.
DR   GO; GO:0098793; C:presynapse; ISO:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; ISO:GO_Central.
DR   GO; GO:0004935; F:adrenergic receptor activity; ISS:UniProtKB.
DR   GO; GO:0035240; F:dopamine binding; ISS:UniProtKB.
DR   GO; GO:0004952; F:dopamine neurotransmitter receptor activity; ISO:GO_Central.
DR   GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IMP:MGI.
DR   GO; GO:0051379; F:epinephrine binding; ISO:GO_Central.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:1901363; F:heterocyclic compound binding; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0051380; F:norepinephrine binding; ISO:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:GO_Central.
DR   GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0050482; P:arachidonate secretion; ISO:GO_Central.
DR   GO; GO:0008306; P:associative learning; ISO:GO_Central.
DR   GO; GO:0001662; P:behavioral fear response; ISO:GO_Central.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0007212; P:G protein-coupled dopamine receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:GO_Central.
DR   GO; GO:0035641; P:locomotory exploration behavior; IMP:UniProtKB.
DR   GO; GO:0098828; P:modulation of inhibitory postsynaptic potential; ISO:GO_Central.
DR   GO; GO:0050709; P:negative regulation of protein secretion; ISO:GO_Central.
DR   GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:GO_Central.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:GO_Central.
DR   GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:GO_Central.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:GO_Central.
DR   GO; GO:0008355; P:olfactory learning; ISO:GO_Central.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:GO_Central.
DR   GO; GO:0060406; P:positive regulation of penile erection; ISO:GO_Central.
DR   GO; GO:0060134; P:prepulse inhibition; ISO:GO_Central.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:GO_Central.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:GO_Central.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:GO_Central.
DR   GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:GO_Central.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0034776; P:response to histamine; ISO:GO_Central.
DR   GO; GO:0007614; P:short-term memory; ISO:GO_Central.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:GO_Central.
DR   FunFam; 1.20.1070.10:FF:000362; D(4) dopamine receptor; 1.
DR   FunFam; 1.20.1070.10:FF:000361; Dopamine receptor D4; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002185; Dopamine_D4_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF143; D(4) DOPAMINE RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00569; DOPAMINED4R.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Biological rhythms; Cell membrane; Disulfide bond;
KW   G protein-coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Receptor; Reference proteome; Sodium; Transducer;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..387
FT                   /note="Dopamine receptor D4"
FT                   /id="PRO_0000069402"
FT   TOPO_DOM        1..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        35..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        58..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        68..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        91..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        107..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        129..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        147..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        171..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        187..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        209..314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        315..337
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        338..346
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TRANSMEM        347..369
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   TOPO_DOM        370..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   REGION          224..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         77
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P21917"
FT   BINDING         112
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:P14416"
FT   BINDING         119
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P21917"
FT   BINDING         191
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:P14416"
FT   BINDING         195
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:P14416"
FT   BINDING         334
FT                   /ligand="dopamine"
FT                   /ligand_id="ChEBI:CHEBI:59905"
FT                   /evidence="ECO:0000250|UniProtKB:P14416"
FT   LIPID           387
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P21917"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|PubMed:31750832, ECO:0007744|PDB:6IQL"
FT   DISULFID        340..343
FT                   /evidence="ECO:0000269|PubMed:31750832,
FT                   ECO:0007744|PDB:6IQL"
FT   CONFLICT        1
FT                   /note="M -> L (in Ref. 3; BAC31893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="E -> K (in Ref. 3; BAC31893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="A -> T (in Ref. 2; AAB50730)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..46
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           65..83
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           85..93
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           102..129
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           159..162
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           166..171
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           188..192
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           193..197
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           198..219
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           304..339
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           347..366
FT                   /evidence="ECO:0007829|PDB:6IQL"
FT   HELIX           367..371
FT                   /evidence="ECO:0007829|PDB:6IQL"
SQ   SEQUENCE   387 AA;  41487 MW;  BEA306D5E8AA02E9 CRC64;
     MGNSSATEDG GLLAGRGPES LGTGAGLGGA GAAALVGGVL LIGLVLAGNS LVCVSVASER
     TLQTPTNYFI VSLAAADLLL AVLVLPLFVY SEVQGGVWLL SPRLCDTLMA MDVMLCTASI
     FNLCAISVDR FVAVTVPLRY NQQGQCQLLL IAATWLLSAA VASPVVCGLN DVPGRDPAVC
     CLENRDYVVY SSVCSFFLPC PLMLLLYWAT FRGLRRWEAA RHTKLHSRAP RRPSGPGPPV
     SDPTQGPFFP DCPPPLPSLR TSPSDSSRPE SELSQRPCSP GCLLADAALP QPPEPSSRRR
     RGAKITGRER KAMRVLPVVV GAFLVCWTPF FVVHITRALC PACFVSPRLV SAVTWLGYVN
     SALNPIIYTI FNAEFRSVFR KTLRLRC
//