ID DRD2_HUMAN Reviewed; 443 AA. AC P14416; Q9NZR3; Q9UPA9; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 04-NOV-2026, entry version 255. DE RecName: Full=Dopamine receptor D2 {ECO:0000305}; DE AltName: Full=Dopamine D2 receptor; GN Name=DRD2 {ECO:0000303|PubMed:15389757, ECO:0000312|HGNC:HGNC:3023}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2533064; DOI=10.1089/dna.1.1989.8.683; RA Selbie L.A., Hayes G., Shine J.; RT "The major dopamine D2 receptor: molecular analysis of the human D2A RT subtype."; RL DNA 8:683-689(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE RP SPECIFICITY. RX PubMed=2531656; DOI=10.1002/j.1460-2075.1989.tb08585.x; RA Dal-Toso R., Sommer B., Ewert M., Herb A., Pritchett D.B., Bach A., RA Shivers B.D., Seeburg P.H.; RT "The dopamine D2 receptor: two molecular forms generated by alternative RT splicing."; RL EMBO J. 8:4025-4034(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=2138729; DOI=10.1093/nar/18.5.1299; RA Robakis N.K., Mohamadi M., Fu D.Y., Sambamurti K., Refolo L.M.; RT "Human retina D2 receptor cDNAs have multiple polyadenylation sites and RT differ from a pituitary clone at the 5' non-coding region."; RL Nucleic Acids Res. 18:1299-1299(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2532362; DOI=10.1073/pnas.86.24.9762; RA Grandy D.K., Marchionni M.A., Makam H., Stofko R.E., Alfano M., RA Frothingham L., Fischer J.B., Burke-Howie K.J., Bunzow J.R., Server A.C., RA Civelli O.; RT "Cloning of the cDNA and gene for a human D2 dopamine receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9762-9766(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=2137193; DOI=10.1016/s0026-895x(25)09942-0; RA Stormann T.M., Gdula D.C., Weiner D.M., Brann M.R.; RT "Molecular cloning and expression of a dopamine D2 receptor from human RT retina."; RL Mol. Pharmacol. 37:1-6(1990). RN [6] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RX PubMed=2144985; RA Selbie L.A., Hayes G., Shine J.; RT "DNA homology screening: isolation and characterization of the human D2A RT dopamine receptor subtype."; RL Adv. Second Messenger Phosphoprotein Res. 24:9-14(1990). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1363862; DOI=10.1016/0197-0186(92)90071-x; RA Araki K., Kuwano R., Morii K., Hayashi S., Minoshima S., Shimizu N., RA Katagiri T., Usui H., Kumanishi T., Takahashi Y.; RT "Structure and expression of human and rat D2 dopamine receptor genes."; RL Neurochem. Int. 21:91-98(1992). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=1835903; DOI=10.1007/bf00734808; RA Dearry A., Falardeau P., Shores C., Caron M.G.; RT "D2 dopamine receptors in the human retina: cloning of cDNA and RT localization of mRNA."; RL Cell. Mol. Neurobiol. 11:437-453(1991). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8471125; DOI=10.1038/npp.1993.15; RA Seeman P., Ohara K., Ulpian C., Seeman M.V., Jellinger K., Tol H.H., RA Niznik H.B.; RT "Schizophrenia: normal sequence in the dopamine D2 receptor region that RT couples to G-proteins. DNA polymorphisms in D2."; RL Neuropsychopharmacology 8:137-142(1993). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Corpus striatum; RX PubMed=10719223; DOI=10.1016/s0169-328x(99)00343-5; RA Seeman P., Nam D., Ulpian C., Liu I.S.C., Tallerico T.; RT "New dopamine receptor, D2(Longer), with unique TG splice site, in human RT brain."; RL Brain Res. Mol. Brain Res. 76:132-141(2000). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3). RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RA Kidd K.K.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [14] RP SUBCELLULAR LOCATION. RX PubMed=8413587; DOI=10.1038/365441a0; RA Seeman P., Guan H.C., Van Tol H.H.; RT "Dopamine D4 receptors elevated in schizophrenia."; RL Nature 365:441-445(1993). RN [15] RP PHOSPHORYLATION, AND PALMITOYLATION. RX PubMed=7931316; DOI=10.1046/j.1471-4159.1994.63051589.x; RA Ng G.Y., O'Dowd B.F., Caron M., Dennis M., Brann M.R., George S.R.; RT "Phosphorylation and palmitoylation of the human D2L dopamine receptor in RT Sf9 cells."; RL J. Neurochem. 63:1589-1595(1994). RN [16] RP PHOSPHORYLATION. RX PubMed=2953072; DOI=10.1126/science.2953072; RA Walters J.R., Bergstrom D.A., Carlson J.H., Chase T.N., Braun A.R.; RT "D1 dopamine receptor activation required for postsynaptic expression of D2 RT agonist effects."; RL Science 236:719-722(1987). RN [17] RP INTERACTION WITH CADPS AND CADPS2. RX PubMed=15857609; DOI=10.1016/j.bcp.2005.02.015; RA Binda A.V., Kabbani N., Levenson R.; RT "Regulation of dense core vesicle release from PC12 cells by interaction RT between the D2 dopamine receptor and calcium-dependent activator protein RT for secretion (CAPS)."; RL Biochem. Pharmacol. 69:1451-1461(2005). RN [18] RP INTERACTION WITH GNAI2. RX PubMed=17550964; DOI=10.1242/jcs.005611; RA Lopez-Aranda M.F., Acevedo M.J., Gutierrez A., Koulen P., Khan Z.U.; RT "Role of a Galphai2 protein splice variant in the formation of an RT intracellular dopamine D2 receptor pool."; RL J. Cell Sci. 120:2171-2178(2007). RN [19] RP HOMOOLIGOMERIZATION, AND INTERACTION WITH DRD4. RX PubMed=21184734; DOI=10.1016/j.bbrc.2010.12.083; RA Borroto-Escuela D.O., Van Craenenbroeck K., Romero-Fernandez W., RA Guidolin D., Woods A.S., Rivera A., Haegeman G., Agnati L.F., RA Tarakanov A.O., Fuxe K.; RT "Dopamine D2 and D4 receptor heteromerization and its allosteric receptor- RT receptor interactions."; RL Biochem. Biophys. Res. Commun. 404:928-934(2011). RN [20] RP INTERACTION WITH HTR2A, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21645528; DOI=10.1016/j.neuropharm.2011.05.023; RA Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.; RT "Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine RT D2 receptors."; RL Neuropharmacology 61:770-777(2011). RN [21] RP RETRACTED PAPER. RX PubMed=17264214; DOI=10.1073/pnas.0608599104; RA Johnston C.A., Siderovski D.P.; RT "Structural basis for nucleotide exchange on G alpha i subunits and RT receptor coupling specificity."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007). RN [22] RP RETRACTION NOTICE OF PUBMED:17264214. RX PubMed=22408789; DOI=10.1073/pnas.1200173109; RA Johnston C.A., Siderovski D.P.; RL Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=23493394; DOI=10.1074/jbc.m112.443945; RA Sharma M., Celver J., Octeau J.C., Kovoor A.; RT "Plasma membrane compartmentalization of D2 dopamine receptors."; RL J. Biol. Chem. 288:12554-12568(2013). RN [24] RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-443, AND MUTAGENESIS OF RP CYS-126; CYS-244; CYS-253 AND CYS-443. RX PubMed=26535572; DOI=10.1371/journal.pone.0140661; RA Ebersole B., Petko J., Woll M., Murakami S., Sokolina K., Wong V., RA Stagljar I., Luescher B., Levenson R.; RT "Effect of C-Terminal S-Palmitoylation on D2 Dopamine Receptor Trafficking RT and Stability."; RL PLoS ONE 10:e0140661-e0140661(2015). RN [25] RP PHOSPHORYLATION AT THR-287; SER-296; SER-317 AND THR-318. RX PubMed=33859231; DOI=10.1038/s41598-021-87417-2; RA Mann A., Keen A.C., Mark H., Dasgupta P., Javitch J.A., Canals M., RA Schulz S., Robert Lane J.; RT "New phosphosite-specific antibodies to unravel the role of GRK RT phosphorylation in dopamine D2 receptor regulation and signaling."; RL Sci. Rep. 11:8288-8288(2021). RN [26] RP PHOSPHORYLATION AT SER-285; SER-286; THR-287; SER-288; THR-293 AND SER-296, RP INTERACTION WITH ARRB2, AND MUTAGENESIS OF 285-SER--SER-296. RX PubMed=40781549; DOI=10.1038/s42003-025-08649-w; RA Kim K., Ji J.S., Kim H.R., Choi Y., Lee H.H., Inoue A., Chung K.Y.; RT "Molecular mechanism of beta-arrestin 2 interaction with phosphorylated RT intracellular loop 3 of dopamine receptor D2."; RL Commun. Biol. 8:1181-1181(2025). RN [27] {ECO:0007744|PDB:5AER} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NCS1. RX PubMed=25979333; DOI=10.1074/jbc.m114.627059; RA Pandalaneni S., Karuppiah V., Saleem M., Haynes L.P., Burgoyne R.D., RA Mayans O., Derrick J.P., Lian L.Y.; RT "Neuronal Calcium Sensor-1 Binds the D2 Dopamine Receptor and G-protein- RT coupled Receptor Kinase 1 (GRK1) Peptides Using Different Modes of RT Interactions."; RL J. Biol. Chem. 290:18744-18756(2015). RN [28] {ECO:0007744|PDB:6CM4} RP X-RAY CRYSTALLOGRAPHY AND 363-443 IN COMPLEX WITH INVERSE AGONIST RP RISPERIDONE, AND DISULFIDE BONDS. RX PubMed=29466326; DOI=10.1038/nature25758; RA Wang S., Che T., Levit A., Shoichet B.K., Wacker D., Roth B.L.; RT "Structure of the D2 dopamine receptor bound to the atypical antipsychotic RT drug risperidone."; RL Nature 555:269-273(2018). RN [29] {ECO:0007744|PDB:6LUQ} RP X-RAY CRYSTALLOGRAPHY AND 367-443, FUNCTIONM, ACTIVITY REGULATION, RP DISULFIDE BONDS, AND MUTAGENESIS OF PHE-110. RX PubMed=32103023; DOI=10.1038/s41467-020-14884-y; RA Fan L., Tan L., Chen Z., Qi J., Nie F., Luo Z., Cheng J., Wang S.; RT "Haloperidol bound D2 dopamine receptor structure inspired the discovery of RT subtype selective ligands."; RL Nat. Commun. 11:1074-1074(2020). RN [30] {ECO:0007744|PDB:7DFP} RP X-RAY CRYSTALLOGRAPHY AND 364-443, FUNCTION, ACTIVITY REGULATION, AND RP DISULFIDE BONDS. RX PubMed=33353947; DOI=10.1038/s41467-020-20221-0; RA Im D., Inoue A., Fujiwara T., Nakane T., Yamanaka Y., Uemura T., Mori C., RA Shiimura Y., Kimura K.T., Asada H., Nomura N., Tanaka T., Yamashita A., RA Nango E., Tono K., Kadji F.M.N., Aoki J., Iwata S., Shimamura T.; RT "Structure of the dopamine D2 receptor in complex with the antipsychotic RT drug spiperone."; RL Nat. Commun. 11:6442-6442(2020). RN [31] {ECO:0007744|PDB:6VMS} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GNB1; GNG2 AND RAT GNAI1, RP FUNCTION, AND DISULFIDE BONDS. RX PubMed=32528175; DOI=10.1038/s41586-020-2379-5; RA Yin J., Chen K.M., Clark M.J., Hijazi M., Kumari P., Bai X.C., RA Sunahara R.K., Barth P., Rosenbaum D.M.; RT "Structure of a D2 dopamine receptor-G-protein complex in a lipid RT membrane."; RL Nature 584:125-129(2020). RN [32] {ECO:0007744|PDB:7JVR} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GNB1; GNG2 AND GNAI1, RP FUNCTION, ACTIVITY REGULATION, AND DISULFIDE BONDS. RX PubMed=33571431; DOI=10.1016/j.cell.2021.01.027; RA Zhuang Y., Xu P., Mao C., Wang L., Krumm B., Zhou X.E., Huang S., Liu H., RA Cheng X., Huang X.P., Shen D.D., Xu T., Liu Y.F., Wang Y., Guo J., RA Jiang Y., Jiang H., Melcher K., Roth B.L., Zhang Y., Zhang C., Xu H.E.; RT "Structural insights into the human D1 and D2 dopamine receptor signaling RT complexes."; RL Cell 184:931-942(2021). RN [33] {ECO:0007744|PDB:8IRS} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GNB1; GNG2 AND GNAI1, RP FUNCTION, ACTIVITY REGULATION, DISULFIDE BONDS, AND MUTAGENESIS OF VAL-91. RX PubMed=37221270; DOI=10.1038/s41422-023-00808-0; RA Xu P., Huang S., Krumm B.E., Zhuang Y., Mao C., Zhang Y., Wang Y., RA Huang X.P., Liu Y.F., He X., Li H., Yin W., Jiang Y., Zhang Y., Roth B.L., RA Xu H.E.; RT "Structural genomics of the human dopamine receptor system."; RL Cell Res. 33:604-616(2023). RN [34] {ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GNAO1; GNB1; GNG2 AND RP DOPAMINE, FUNCTION, AND SUBUNIT. RX PubMed=39103320; DOI=10.1038/s41467-024-50964-z; RA Knight K.M., Krumm B.E., Kapolka N.J., Ludlam W.G., Cui M., Mani S., RA Prytkova I., Obarow E.G., Lefevre T.J., Wei W., Ma N., Huang X.P., RA Fay J.F., Vaidehi N., Smrcka A.V., Slesinger P.A., Logothetis D.E., RA Martemyanov K.A., Roth B.L., Dohlman H.G.; RT "A neurodevelopmental disorder mutation locks G proteins in the transitory RT pre-activated state."; RL Nat. Commun. 15:6643-6643(2024). RN [35] {ECO:0007744|PDB:9BS9, ECO:0007744|PDB:9BSB} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GNAO1, FUNCTION, AND RP DISULFIDE BONDS. RX PubMed=40683247; DOI=10.1016/j.neuron.2025.06.012; RA Jain M.K., Gumpper R.H., Slocum S.T., Schmitz G.P., Madsen J.S., RA Tummino T.A., Suomivuori C.M., Huang X.P., Shub L., DiBerto J.F., Kim K., RA DeLeon C., Krumm B.E., Fay J.F., Keiser M., Hauser A.S., Dror R.O., RA Shoichet B., Gloriam D.E., Nichols D.E., Roth B.L.; RT "The polypharmacology of psychedelics reveals multiple targets for RT potential therapeutics."; RL Neuron 113:3129-3142(2025). RN [36] RP VARIANT CYS-311. RX PubMed=7902708; DOI=10.1006/bbrc.1993.2404; RA Itokawa M., Arinami T., Futamura N., Hamaguchi H., Toru M.; RT "A structural polymorphism of human dopamine D2 receptor, RT D2(Ser311->Cys)."; RL Biochem. Biophys. Res. Commun. 196:1369-1375(1993). RN [37] RP VARIANT ILE-154. RX PubMed=10220438; DOI=10.1073/pnas.96.9.5173; RA Klein C., Brin M.F., Kramer P., Sena-Esteves M., de Leon D., Doheny D., RA Bressman S., Fahn S., Breakefield X.O., Ozelius L.J.; RT "Association of a missense change in the D2 dopamine receptor with RT myoclonus dystonia."; RL Proc. Natl. Acad. Sci. U.S.A. 96:5173-5176(1999). RN [38] RP INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM. RX PubMed=15389757; DOI=10.1002/ajmg.b.30085; RA Johann M., Putzhammer A., Eichhammer P., Wodarz N.; RT "Association of the -141C Del variant of the dopamine D2 receptor (DRD2) RT with positive family history and suicidality in German alcoholics."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 132:46-49(2005). RN [39] RP CHARACTERIZATION OF VARIANT ILE-154. RX PubMed=10716258; RX DOI=10.1002/1531-8249(200003)47:3<369::aid-ana14>3.3.co;2-0; RA Klein C., Gurvich N., Sena-Esteves M., Bressman S., Brin M.F., RA Ebersole B.J., Fink S., Forsgren L., Friedman J., Grimes D., Holmgren G., RA Kyllerman M., Lang A.E., de Leon D., Leung J., Prioleau C., Raymond D., RA Sanner G., Saunders-Pullman R., Vieregge P., Wahlstrom J., RA Breakefield X.O., Kramer P.L., Ozelius L.J., Sealfon S.C.; RT "Evaluation of the role of the D2 dopamine receptor in myoclonus RT dystonia."; RL Ann. Neurol. 47:369-373(2000). RN [40] RP VARIANT GLU-327. RX PubMed=21179162; DOI=10.1038/nature09629; RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., RA Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., RA Virkkunen M., Goldman D.; RT "A population-specific HTR2B stop codon predisposes to severe RT impulsivity."; RL Nature 468:1061-1066(2010). 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 CC (PubMed:21645528, PubMed:32103023, PubMed:32528175, PubMed:33353947, CC PubMed:33571431, PubMed:37221270, PubMed:39103320). Dopamine binding CC causes a conformation change that triggers signaling via guanine CC nucleotide-binding proteins (G proteins) and modulates the activity of CC downstream effectors, such as adenylate cyclase (PubMed:32103023, CC PubMed:32528175, PubMed:33353947, PubMed:33571431, PubMed:37221270). CC Dopamine receptors can be classified in two categories: (1) DRD2 CC (together with DRD3 and DRD4) is a D2-type receptor and is coupled to CC G(i)/G(o) G proteins, mediating inhibition of adenylate cyclase CC activity, while D1-type receptors (DRD1 and DRD5) are coupled to G(s) G CC proteins and promote activation of adenylate cyclase activity CC (PubMed:32103023, PubMed:32528175, PubMed:33353947, PubMed:33571431, CC PubMed:37221270). In the central nervous system, DRD2 is mainly coupled CC to G(o)/GNAO1 (By similarity). D1- and D2-type dopamine receptors have CC antagonistic effects, particularly in the brain's striatum, where they CC 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 DRD1 and DRD2 are the most abundant dopamine receptors in the central CC nervous system, especially in the basal ganglia and the prefrontal CC cortex (PubMed:33571431). DRD2 receptor plays a key role in risky CC decision-making by modulating reward sensitivity and executive control; CC DRD2 activation in nucleus accumbens cells leading to increased risk- CC taking and impulsivity (By similarity). DRD2 can also couple with G(q) CC by forming a heteromer with the ghrelin receptor GHSR in neurons CC independently of ghrelin (By similarity). Following DRD2 activation by CC dopamine in lumbosacral defecation centers, GHSR acts as a coreceptor CC promoting DRD2 coupling to G(q) at the expense of G(i)/G(o), regulating CC defecation (By similarity). In addition to dopamine, also acts as a CC receptor for tryptophan-derived metabolites in intestinal epithelial CC cells: activation by tryptophan metabolites produced by the gut CC microbiota initiates a phospholipase-C-dependent signaling that CC promotes colonization resistance by pathogens by controlling actin CC cytoskeletal organization in the gut epithelium (By similarity). CC Positively regulates postnatal regression of retinal hyaloid vessels CC via suppression of VEGFR2/KDR activity, downstream of OPN5 (By CC similarity). Also acts as a receptor for D-lysergic (LSD) psychedelic CC drug (PubMed:40683247). {ECO:0000250|UniProtKB:P61168, CC ECO:0000250|UniProtKB:P61169, ECO:0000269|PubMed:21645528, CC ECO:0000269|PubMed:32103023, ECO:0000269|PubMed:32528175, CC ECO:0000269|PubMed:33353947, ECO:0000269|PubMed:33571431, CC ECO:0000269|PubMed:37221270, ECO:0000269|PubMed:39103320, CC ECO:0000269|PubMed:40683247}. CC -!- ACTIVITY REGULATION: Activated by small-molecule agonist bromocriptine CC (PubMed:33571431). Activated by the pan-agonist rotigotine, which CC activates all five dopamine receptors (PubMed:37221270). Inhibited by CC antipsychotic drug haloperidol; which acts as an antagonist of DRD2 CC (PubMed:32103023). Specifically inhibited by antipsychotic drug CC spiperone; which acts as a specific and potent antagonist of DRD2 CC (PubMed:33353947). {ECO:0000269|PubMed:32103023, CC ECO:0000269|PubMed:33353947, ECO:0000269|PubMed:33571431, CC ECO:0000269|PubMed:37221270}. CC -!- SUBUNIT: Interacts with GNAO1, GNB1 and GNG2; interaction with a CC heterotrimeric G protein complex is essential for receptor activity CC (PubMed:39103320). Interacts with G(i) proteins, GNAI1, GNAI2 and GNAI3 CC (By similarity). Interacts with GNAI2 isoform sGi2; the interaction CC allows the creation of an intracellular pool of DRD2 that can be CC released to cell surface upon agonist stimulation (PubMed:17550964). CC Forms heteromers with DRD1 (By similarity). Forms heterooligomers with CC DRD4; the interaction with DRD4 may modulate agonist-induced downstream CC signaling (PubMed:21184734). Interacts with CADPS and CADPS2 CC (PubMed:15857609). Interacts with GPRASP1, PPP1R9B and CLIC6 (By CC similarity). Interacts with ARRB2; leading to receptor desensitization CC (PubMed:40781549). Interacts with HTR2A (PubMed:21645528). Interacts CC with KCNA2 (By similarity). Interacts with GHSR; forms a heteromer with CC GHSR in neurons (By similarity). {ECO:0000250|UniProtKB:P61168, CC ECO:0000250|UniProtKB:P61169, ECO:0000269|PubMed:15857609, CC ECO:0000269|PubMed:17550964, ECO:0000269|PubMed:21184734, CC ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:39103320, CC ECO:0000269|PubMed:40781549}. CC -!- INTERACTION: CC P14416; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-2928178, EBI-529989; CC P14416; P14416: DRD2; NbExp=9; IntAct=EBI-2928178, EBI-2928178; CC P14416; Q01959: SLC6A3; NbExp=4; IntAct=EBI-2928178, EBI-6661445; CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:P61169}; Multi-pass membrane protein CC {ECO:0000269|PubMed:32528175, ECO:0000269|PubMed:33571431}. Cell CC membrane {ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:23493394, CC ECO:0000269|PubMed:26535572, ECO:0000269|PubMed:8413587}; Multi-pass CC membrane protein {ECO:0000269|PubMed:32528175, CC ECO:0000269|PubMed:33571431}. Golgi apparatus membrane CC {ECO:0000269|PubMed:26535572}; Multi-pass membrane protein CC {ECO:0000269|PubMed:32528175, ECO:0000269|PubMed:33571431}. Note=Mainly CC active on postsynaptic membrane (By similarity). Specifically localizes CC to special plasma membrane microcompartments (PubMed:23493394). CC {ECO:0000250|UniProtKB:P61169, ECO:0000269|PubMed:23493394}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=D2(Long), D2A; CC IsoId=P14416-1; Sequence=Displayed; CC Name=2; Synonyms=D2(Short), D2B; CC IsoId=P14416-2; Sequence=VSP_001870; CC Name=3; Synonyms=D2(Longer); CC IsoId=P14416-3; Sequence=VSP_026455; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the anterior pituitary CC gland. {ECO:0000269|PubMed:2531656}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the anterior pituitary CC gland. {ECO:0000269|PubMed:2531656}. CC -!- PTM: Palmitoylated (PubMed:7931316, PubMed:26535572). Palmitoylation CC which is required for proper localization to the plasma membrane and CC stability of the receptor could be carried on by ZDHHC4, ZDHHC3 and CC ZDHHC8 (PubMed:26535572). {ECO:0000269|PubMed:26535572, CC ECO:0000269|PubMed:7931316}. CC -!- PTM: Phosphorylation of intracellular loop 3 by GRK2 and GRK3 following CC prolonged stimulation by dopamine, promoting association with beta- CC arrestin (ARRB1 or ARRB2), leading to receptor desensitization and CC negative regulation of G protein-coupled receptor signaling CC (PubMed:33859231, PubMed:40781549). Constitutive phosphorylation (in CC absence of dopamine activation) by some isoforms of PKC-beta (PRKCB) CC inhibits G protein-coupled receptor signaling (PubMed:2953072). CC {ECO:0000269|PubMed:2953072, ECO:0000269|PubMed:33859231, CC ECO:0000269|PubMed:40781549}. CC -!- POLYMORPHISM: Genetic variations in DRD2 may determine the genetic CC susceptibility to alcoholism [MIM:103780]. Genetic variations in DRD2 CC might be a protective factor against the development of withdrawal CC symptoms but might also be a risk factor in a highly burdened subgroup CC of alcoholics with a paternal and grandpaternal history of alcoholism CC and might contribute to suicide risk in alcoholics. CC {ECO:0000269|PubMed:15389757}. 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; M30625; AAA88024.1; -; mRNA. DR EMBL; X51645; CAB56463.1; -; mRNA. DR EMBL; X51646; CAB37869.1; -; Genomic_DNA. DR EMBL; X51362; CAA35746.1; -; mRNA. DR EMBL; M29066; AAA52761.1; -; mRNA. DR EMBL; S62137; AAB26819.1; -; mRNA. DR EMBL; S69899; AAB20571.1; -; mRNA. DR EMBL; S58589; AAB26274.1; -; Genomic_DNA. DR EMBL; S58577; AAB26274.1; JOINED; Genomic_DNA. DR EMBL; S58584; AAB26274.1; JOINED; Genomic_DNA. DR EMBL; S58586; AAB26274.1; JOINED; Genomic_DNA. DR EMBL; S58588; AAB26274.1; JOINED; Genomic_DNA. DR EMBL; AF176812; AAF61479.1; -; mRNA. DR EMBL; AB065860; BAC06078.1; -; Genomic_DNA. DR EMBL; AF050737; AAC78779.1; -; Genomic_DNA. DR EMBL; BC021195; AAH21195.1; -; mRNA. DR CCDS; CCDS8361.1; -. [P14416-1] DR CCDS; CCDS8362.1; -. [P14416-2] DR PIR; S08417; DYHUD2. DR RefSeq; NP_000786.1; NM_000795.4. [P14416-1] DR RefSeq; NP_057658.2; NM_016574.4. [P14416-2] DR RefSeq; XP_016872785.1; XM_017017296.3. [P14416-1] DR RefSeq; XP_047282467.1; XM_047426511.1. [P14416-2] DR RefSeq; XP_054223910.1; XM_054367935.1. [P14416-1] DR RefSeq; XP_054223911.1; XM_054367936.1. [P14416-2] DR PDB; 5AER; X-ray; 2.19 A; B/C=430-443. DR PDB; 6CM4; X-ray; 2.87 A; A=35-222, A=363-443. DR PDB; 6LUQ; X-ray; 3.10 A; A=35-222, A=367-443. DR PDB; 6VMS; EM; 3.80 A; R=29-443. DR PDB; 7DFP; X-ray; 3.10 A; A=35-238, A=364-443. DR PDB; 7JVR; EM; 2.80 A; R=1-443. DR PDB; 8IRS; EM; 3.00 A; R=1-443. DR PDB; 8TZQ; EM; 3.20 A; R=1-443. DR PDB; 8U02; EM; 3.28 A; R=1-443. DR PDB; 9BS9; EM; 2.28 A; R=1-443. DR PDB; 9BSB; EM; 2.32 A; R=1-443. DR AlphaFoldDB; P14416; -. DR EMDB; EMD-21243; -. DR EMDB; EMD-22511; -. DR EMDB; EMD-35684; -. DR EMDB; EMD-41766; -. DR EMDB; EMD-41776; -. DR EMDB; EMD-44865; -. DR EMDB; EMD-44866; -. DR MDRepo; P14416; -. DR SMR; P14416; -. DR BioGRID; 108147; 102. DR CORUM; P14416; -. DR DIP; DIP-5977N; -. DR FunCoup; P14416; 928. DR IntAct; P14416; 84. DR NDEx; IQUERY-CP-DRD2; 13 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000354859; -. DR BindingDB; P14416; -. DR ChEMBL; CHEMBL217; -. DR DrugBank; DB02565; 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide. DR DrugBank; DB19867; Abaperidone. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB01063; Acetophenazine. DR DrugBank; DB20244; Adoprazine. DR DrugBank; DB01425; Alizapride. DR DrugBank; DB00915; Amantadine. DR DrugBank; DB06288; Amisulpride. DR DrugBank; DB05964; Amitifadine. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB00182; Amphetamine. DR DrugBank; DB04599; Aniracetam. DR DrugBank; DB06620; Aplindore. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB09207; AS-8112. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB11376; Azaperone. DR DrugBank; DB01295; Bevantolol. DR DrugBank; DB04889; Bicifadine. DR DrugBank; DB04888; Bifeprunox. DR DrugBank; DB05687; BL-1020. DR DrugBank; DB09223; Blonanserin. DR DrugBank; DB04857; Brasofensine. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB09018; Bromopride. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB20952; Carmoxirole. DR DrugBank; DB01038; Carphenazine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB13511; Clebopride. DR DrugBank; DB15971; Clorotepine. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00298; Dapiprazole. DR DrugBank; DB06421; Declopramide. DR DrugBank; DB21277; Denopamine. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB11274; Dihydro-alpha-ergocryptine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB16602; Dihydroergotoxine. DR DrugBank; DB18046; Docarpamine. DR DrugBank; DB01184; Domperidone. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB16144; Dopastatin. DR DrugBank; DB12313; Dopexamine. DR DrugBank; DB14844; Dordaviprone. DR DrugBank; DB00450; Droperidol. DR DrugBank; DB19875; Elopiprazole. DR DrugBank; DB01364; Ephedrine. DR DrugBank; DB11275; Epicriptine. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB01253; Ergometrine. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB01175; Escitalopram. DR DrugBank; DB15492; Eticlopride. DR DrugBank; DB09194; Etoperidone. DR DrugBank; DB01463; Fencamfamin. DR DrugBank; DB13665; Fluanisone. DR DrugBank; DB00875; Flupentixol. DR DrugBank; DB00623; Fluphenazine. DR DrugBank; DB04842; Fluspirilene. DR DrugBank; DB19975; Fosopamine. DR DrugBank; DB01296; Glucosamine. DR DrugBank; DB00502; Haloperidol. DR DrugBank; DB09352; Hydroxyamphetamine. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB04924; Itopride. DR DrugBank; DB12579; JNJ-37822681. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB20964; Lensiprazine. DR DrugBank; DB01235; Levodopa. DR DrugBank; DB16021; Levosulpiride. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB06077; Lumateperone. DR DrugBank; DB08815; Lurasidone. DR DrugBank; DB00934; Maprotiline. DR DrugBank; DB20960; Mazapertine. DR DrugBank; DB09224; Melperone. DR DrugBank; DB01043; Memantine. DR DrugBank; DB01365; Mephentermine. DR DrugBank; DB00933; Mesoridazine. DR DrugBank; DB01577; Metamfetamine. DR DrugBank; DB00610; Metaraminol. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB00968; Methyldopa. DR DrugBank; DB01233; Metoclopramide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB24348; Milsaperidone. DR DrugBank; DB00805; Minaprine. DR DrugBank; DB01618; Molindone. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB06711; Naphazoline. DR DrugBank; DB19314; Nemonapride. DR DrugBank; DB04821; Nomifensine. DR DrugBank; DB05766; Norclozapine. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB06229; Ocaperidone. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB05196; Ordopidine. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB12061; Pardoprunox. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB12710; Perazine. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB08922; Perospirone. DR DrugBank; DB00850; Perphenazine. DR DrugBank; DB12998; PF-00217830. DR DrugBank; DB00925; Phenoxybenzamine. DR DrugBank; DB00692; Phentolamine. DR DrugBank; DB00388; Phenylephrine. DR DrugBank; DB11160; Phenyltoloxamine. DR DrugBank; DB01100; Pimozide. DR DrugBank; DB09286; Pipamperone. DR DrugBank; DB06808; Piperacetazine. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB12478; Piribedil. DR DrugBank; DB00413; Pramipexole. DR DrugBank; DB20444; Preclamol. DR DrugBank; DB11947; Pridopidine. DR DrugBank; DB00433; Prochlorperazine. DR DrugBank; DB00420; Promazine. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB00852; Pseudoephedrine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB09097; Quinagolide. DR DrugBank; DB19663; Quinpirole. DR DrugBank; DB12518; Raclopride. DR DrugBank; DB00409; Remoxipride. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB01549; Rolicyclidine. DR DrugBank; DB20790; Romergoline. DR DrugBank; DB00268; Ropinirole. DR DrugBank; DB05271; Rotigotine. DR DrugBank; DB19883; Roxindole. DR DrugBank; DB16927; S-Apomorphine. DR DrugBank; DB06454; Sarizotan. DR DrugBank; DB06144; Sertindole. DR DrugBank; DB20962; Sibenadet. DR DrugBank; DB17056; Spiperone. DR DrugBank; DB00391; Sulpiride. DR DrugBank; DB06477; Sumanirole. DR DrugBank; DB20211; Talipexole. DR DrugBank; DB04844; Tetrabenazine. DR DrugBank; DB12093; Tetrahydropalmatine. DR DrugBank; DB00372; Thiethylperazine. DR DrugBank; DB01622; Thioproperazine. DR DrugBank; DB00679; Thioridazine. DR DrugBank; DB01623; Thiothixene. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00797; Tolazoline. DR DrugBank; DB18794; Trazpiroben. DR DrugBank; DB00831; Trifluoperazine. DR DrugBank; DB00508; Triflupromazine. DR DrugBank; DB00662; Trimethobenzamide. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB20674; Umespirone. DR DrugBank; DB06109; YKP-1358. DR DrugBank; DB01392; Yohimbine. DR DrugBank; DB12188; Zicronapine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB09225; Zotepine. DR DrugBank; DB01624; Zuclopenthixol. DR DrugCentral; P14416; -. DR GuidetoPHARMACOLOGY; 215; -. DR TCDB; 9.A.14.3.10; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P14416; 3 sites, No reported glycans. DR GlyGen; P14416; 3 sites. DR iPTMnet; P14416; -. DR PhosphoSitePlus; P14416; -. DR SwissPalm; P14416; -. DR BioMuta; DRD2; -. DR DMDM; 118206; -. DR MassIVE; P14416; -. DR PaxDb; 9606-ENSP00000354859; -. DR PeptideAtlas; P14416; -. DR ProteomicsDB; 53055; -. [P14416-3] DR ABCD; P14416; 3 sequenced antibodies. DR Antibodypedia; 2801; 387 antibodies from 43 providers. DR DNASU; 1813; -. DR Ensembl; ENST00000346454.7; ENSP00000278597.5; ENSG00000149295.15. [P14416-2] DR Ensembl; ENST00000362072.8; ENSP00000354859.3; ENSG00000149295.15. [P14416-1] DR Ensembl; ENST00000538967.5; ENSP00000438215.1; ENSG00000149295.15. [P14416-3] DR Ensembl; ENST00000542968.5; ENSP00000442172.1; ENSG00000149295.15. [P14416-1] DR Ensembl; ENST00000907485.1; ENSP00000577544.1; ENSG00000149295.15. [P14416-1] DR Ensembl; ENST00000907486.1; ENSP00000577545.1; ENSG00000149295.15. [P14416-1] DR Ensembl; ENST00000907487.1; ENSP00000577546.1; ENSG00000149295.15. [P14416-1] DR GeneID; 1813; -. DR KEGG; hsa:1813; -. DR MANE-Select; ENST00000362072.8; ENSP00000354859.3; NM_000795.4; NP_000786.1. DR UCSC; uc001pnz.4; human. [P14416-1] DR AGR; HGNC:3023; -. DR ClinPGx; PA27478; -. DR CTD; 1813; -. DR DisGeNET; 1813; -. DR GeneCards; DRD2; -. DR HGNC; HGNC:3023; DRD2. DR HPA; ENSG00000149295; Group enriched (brain, pituitary gland). DR MalaCards; DRD2; -. DR MIM; 103780; phenotype. DR MIM; 126450; gene. DR OpenTargets; ENSG00000149295; -. DR Orphanet; 36899; Myoclonus-dystonia syndrome. DR VEuPathDB; HostDB:ENSG00000149295; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000155539; -. DR HOGENOM; CLU_009579_11_1_1; -. DR InParanoid; P14416; -. DR OMA; ADQKPQF; -. DR OrthoDB; 10034726at2759; -. DR PAN-GO; P14416; 11 GO annotations based on evolutionary models. DR PhylomeDB; P14416; -. DR PathwayCommons; P14416; -. DR Reactome; R-HSA-390651; Dopamine receptors. DR SignaLink; P14416; -. DR SIGNOR; P14416; -. DR Agora; ENSG00000149295; -. DR BioGRID-ORCS; 1813; 13 hits in 1171 CRISPR screens. DR ChiTaRS; DRD2; human. DR EvolutionaryTrace; P14416; -. DR GeneWiki; Dopamine_receptor_D2; -. DR GenomeRNAi; 1813; -. DR Pharos; P14416; Tclin. DR PRO; PR:P14416; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P14416; protein. DR Bgee; ENSG00000149295; Expressed in putamen and 123 other cell types or tissues. DR ExpressionAtlas; P14416; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0030424; C:axon; ISS:BHF-UCL. DR GO; GO:0043679; C:axon terminus; IEA:Ensembl. DR GO; GO:0060170; C:ciliary membrane; IDA:SYSCILIA_CCNET. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl. DR GO; GO:0097648; C:G protein-coupled receptor complex; IDA:ARUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl. DR GO; GO:0097730; C:non-motile cilium; IDA:SYSCILIA_CCNET. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB. DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central. DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0035240; F:dopamine binding; IEA:Ensembl. DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:UniProt. DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IDA:BHF-UCL. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:ARUK-UCL. DR GO; GO:0032795; F:heterotrimeric G-protein binding; IDA:ARUK-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl. DR GO; GO:0015459; F:potassium channel regulator activity; NAS:BHF-UCL. DR GO; GO:0046717; P:acid secretion; IEA:Ensembl. DR GO; GO:0021984; P:adenohypophysis development; ISS:BHF-UCL. DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0007628; P:adult walking behavior; ISS:BHF-UCL. DR GO; GO:0050482; P:arachidonate secretion; IDA:BHF-UCL. DR GO; GO:0008306; P:associative learning; ISS:BHF-UCL. DR GO; GO:0031223; P:auditory behavior; IEA:Ensembl. DR GO; GO:0006914; P:autophagy; IEA:Ensembl. DR GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL. DR GO; GO:0048148; P:behavioral response to cocaine; ISS:BHF-UCL. DR GO; GO:0048149; P:behavioral response to ethanol; ISS:BHF-UCL. DR GO; GO:0160213; P:beta-arrestin-dependent dopamine receptor signaling pathway; NAS:ParkinsonsUK-UCL. DR GO; GO:0048755; P:branching morphogenesis of a nerve; ISS:BHF-UCL. DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; ISS:BHF-UCL. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:BHF-UCL. DR GO; GO:0042417; P:dopamine metabolic process; IC:BHF-UCL. DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl. DR GO; GO:0060079; P:excitatory postsynaptic potential; NAS:ParkinsonsUK-UCL. DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl. DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:BHF-UCL. DR GO; GO:0008104; P:intracellular protein localization; ISS:BHF-UCL. DR GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL. DR GO; GO:0007626; P:locomotory behavior; ISS:BHF-UCL. DR GO; GO:0007616; P:long-term memory; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; ISS:BHF-UCL. DR GO; GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:BHF-UCL. DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl. DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0035305; P:negative regulation of dephosphorylation; IEA:Ensembl. DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl. DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:BHF-UCL. DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL. DR GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; ISS:BHF-UCL. DR GO; GO:0007270; P:neuron-neuron synaptic transmission; ISS:BHF-UCL. DR GO; GO:0021769; P:orbitofrontal cortex development; IEA:Ensembl. DR GO; GO:0030432; P:peristalsis; ISS:BHF-UCL. DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IGI:MGI. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:2000987; P:positive regulation of behavioral fear response; IEA:Ensembl. DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; ISS:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:1900168; P:positive regulation of glial cell-derived neurotrophic factor production; IDA:CACAO. DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISS:BHF-UCL. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:BHF-UCL. DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL. DR GO; GO:2000292; P:regulation of defecation; ISS:UniProtKB. DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; IC:BHF-UCL. DR GO; GO:0002027; P:regulation of heart rate; ISS:BHF-UCL. DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IEA:Ensembl. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS:BHF-UCL. DR GO; GO:0043266; P:regulation of potassium ion transport; ISS:BHF-UCL. DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL. DR GO; GO:0051823; P:regulation of synapse structural plasticity; IEA:Ensembl. DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:BHF-UCL. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:BHF-UCL. DR GO; GO:0001975; P:response to amphetamine; ISS:BHF-UCL. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; ISS:BHF-UCL. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0034776; P:response to histamine; IDA:BHF-UCL. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0014854; P:response to inactivity; IEA:Ensembl. DR GO; GO:0010039; P:response to iron ion; IEA:Ensembl. DR GO; GO:0009416; P:response to light stimulus; ISS:BHF-UCL. DR GO; GO:0043278; P:response to morphine; ISS:BHF-UCL. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:BHF-UCL. DR GO; GO:0007608; P:sensory perception of smell; ISS:BHF-UCL. DR GO; GO:0021756; P:striatum development; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL. DR GO; GO:0001659; P:temperature homeostasis; ISS:BHF-UCL. DR GO; GO:0008542; P:visual learning; ISS:BHF-UCL. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl. DR CDD; cd15309; 7tmA_D2_dopamine_R; 1. DR FunFam; 1.20.1070.10:FF:000099; D(2) dopamine receptor; 1. DR FunFam; 1.20.1070.10:FF:000086; Dopamine D2 receptor 2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2. DR InterPro; IPR001922; Dopamine_D2_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:SF87; D(2) DOPAMINE RECEPTOR; 1. 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 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; Alternative splicing; Cell membrane; Disulfide bond; KW G protein-coupled receptor; Glycoprotein; Golgi apparatus; Lipoprotein; KW Membrane; Palmitate; Phosphoprotein; Postsynaptic cell membrane; KW Proteomics identification; Receptor; Reference proteome; Synapse; KW Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..443 FT /note="Dopamine receptor D2" FT /id="PRO_0000069387" FT TOPO_DOM 1..37 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 38..60 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 61..70 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 71..93 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 94..108 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 109..130 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 131..151 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 152..172 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 173..188 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 189..213 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 214..373 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 374..395 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 396..409 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TRANSMEM 410..431 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT TOPO_DOM 432..443 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32528175, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:8TZQ, FT ECO:0007744|PDB:8U02" FT REGION 281..332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 323..332 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 114 FT /ligand="dopamine" FT /ligand_id="ChEBI:CHEBI:59905" FT /evidence="ECO:0000269|PubMed:39103320, FT ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02" FT BINDING 193 FT /ligand="dopamine" FT /ligand_id="ChEBI:CHEBI:59905" FT /evidence="ECO:0000269|PubMed:39103320, FT ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02" FT BINDING 197 FT /ligand="dopamine" FT /ligand_id="ChEBI:CHEBI:59905" FT /evidence="ECO:0000269|PubMed:39103320, FT ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02" FT BINDING 393 FT /ligand="dopamine" FT /ligand_id="ChEBI:CHEBI:59905" FT /evidence="ECO:0000269|PubMed:39103320, FT ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61169" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61169" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:40781549" FT MOD_RES 286 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:40781549" FT MOD_RES 287 FT /note="Phosphothreonine; by GRK2 and GRK3" FT /evidence="ECO:0000269|PubMed:33859231, FT ECO:0000305|PubMed:40781549" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:40781549" FT MOD_RES 293 FT /note="Phosphothreonine" FT /evidence="ECO:0000305|PubMed:40781549" FT MOD_RES 296 FT /note="Phosphoserine; by GRK2 and GRK3" FT /evidence="ECO:0000269|PubMed:33859231, FT ECO:0000305|PubMed:40781549" FT MOD_RES 317 FT /note="Phosphoserine; by GRK2 and GRK3" FT /evidence="ECO:0000269|PubMed:33859231" FT MOD_RES 318 FT /note="Phosphothreonine; by GRK2 and GRK3" FT /evidence="ECO:0000269|PubMed:33859231" FT MOD_RES 351 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P61169" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P61169" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61169" FT LIPID 443 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:26535572" FT CARBOHYD 5 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 17 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 107..182 FT /evidence="ECO:0000269|PubMed:25979333, FT ECO:0000269|PubMed:29466326, ECO:0000269|PubMed:32103023, FT ECO:0000269|PubMed:32528175, ECO:0000269|PubMed:33353947, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0000269|PubMed:39103320, ECO:0000269|PubMed:40683247, FT ECO:0007744|PDB:6CM4, ECO:0007744|PDB:6LUQ, FT ECO:0007744|PDB:6VMS, ECO:0007744|PDB:7DFP, FT ECO:0007744|PDB:7JVR, ECO:0007744|PDB:8IRS, FT ECO:0007744|PDB:8TZQ, ECO:0007744|PDB:8U02, FT ECO:0007744|PDB:9BS9, ECO:0007744|PDB:9BSB" FT DISULFID 399..401 FT /evidence="ECO:0000269|PubMed:29466326, FT ECO:0000269|PubMed:32528175, ECO:0000269|PubMed:33353947, FT ECO:0000269|PubMed:33571431, ECO:0000269|PubMed:37221270, FT ECO:0007744|PDB:6CM4, ECO:0007744|PDB:6VMS, FT ECO:0007744|PDB:7DFP, ECO:0007744|PDB:7JVR, FT ECO:0007744|PDB:8IRS" FT VAR_SEQ 242..270 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2531656" FT /id="VSP_001870" FT VAR_SEQ 270 FT /note="V -> VVQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10719223" FT /id="VSP_026455" FT VARIANT 154 FT /note="V -> I (found in patients with alcohol-responsive FT myoclonus-dystonia; uncertain significance; the mutation FT does not affect functional properties; dbSNP:rs104894220)" FT /evidence="ECO:0000269|PubMed:10220438, FT ECO:0000269|PubMed:10716258" FT /id="VAR_017143" FT VARIANT 310 FT /note="P -> S (in dbSNP:rs1800496)" FT /id="VAR_014674" FT VARIANT 311 FT /note="S -> C (in dbSNP:rs1801028)" FT /evidence="ECO:0000269|PubMed:7902708" FT /id="VAR_003462" FT VARIANT 327 FT /note="K -> E (in dbSNP:rs71653614)" FT /evidence="ECO:0000269|PubMed:21179162" FT /id="VAR_064579" FT MUTAGEN 91 FT /note="V->A: Does not affect activation by rotigotine." FT /evidence="ECO:0000269|PubMed:37221270" FT MUTAGEN 110 FT /note="F->A,L: Enhanced-binding to antagonist haloperidol." FT /evidence="ECO:0000269|PubMed:32103023" FT MUTAGEN 110 FT /note="F->W,Y: Reduced-binding to antagonist haloperidol." FT /evidence="ECO:0000269|PubMed:32103023" FT MUTAGEN 126 FT /note="C->S: No effect on palmitoylation; no effect on FT localization to the plasma membrane." FT /evidence="ECO:0000269|PubMed:26535572" FT MUTAGEN 244 FT /note="C->S: No effect on palmitoylation; no effect on FT localization to the plasma membrane." FT /evidence="ECO:0000269|PubMed:26535572" FT MUTAGEN 253 FT /note="C->S: No effect on palmitoylation; no effect on FT localization to the plasma membrane." FT /evidence="ECO:0000269|PubMed:26535572" FT MUTAGEN 285..296 FT /note="SSTSPPERTRYS->AAAAPPERARYA: Decreased FT phosphorylation and desensitization." FT /evidence="ECO:0000269|PubMed:40781549" FT MUTAGEN 443 FT /note="Missing: Decreased palmitoylation; decreased FT localization to the plasma membrane; decreased stability." FT /evidence="ECO:0000269|PubMed:26535572" FT CONFLICT 40 FT /note="L -> R (in Ref. 7; AAB26819)" FT /evidence="ECO:0000305" FT HELIX 36..61 FT /evidence="ECO:0007829|PDB:9BS9" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 68..82 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 83..87 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 88..97 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 104..137 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 139..143 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 145..167 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 168..172 FT /evidence="ECO:0007829|PDB:9BS9" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:7JVR" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:6CM4" FT HELIX 187..194 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 195..199 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 200..222 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 366..397 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 405..427 FT /evidence="ECO:0007829|PDB:9BS9" FT HELIX 431..442 FT /evidence="ECO:0007829|PDB:5AER" SQ SEQUENCE 443 AA; 50619 MW; 9BF8EA36C988A2E2 CRC64; MDPLNLSWYD DDLERQNWSR PFNGSDGKAD RPHYNYYATL LTLLIAVIVF GNVLVCMAVS REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMISIVW VLSFTISCPL LFGLNNADQN ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRAHLRAPL KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKDHPKIAKI FEIQTMPNGK TRTSLKTMSR RKLSQQKEKK ATQMLAIVLG VFIICWLPFF ITHILNIHCD CNIPPVLYSA FTWLGYVNSA VNPIIYTTFN IEFRKAFLKI LHC //