DRD2_HUMAN
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 03-AUG-2022, entry version 236.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=DRD2;
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;
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;
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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21] {ECO:0007744|PDB:5AER}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 430-443 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 [22] {ECO:0007744|PDB:6CM4}
RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 35-222 AND 363-443 IN COMPLEX
RP WITH INVERSE AGONIST 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 [23]
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 [24]
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 [25]
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 [26]
RP CHARACTERIZATION OF VARIANT ILE-154.
RX PubMed=10716258;
RX DOI=10.1002/1531-8249(200003)47:3<369::aid-ana14>3.0.co;2-9;
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 [27]
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: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase (PubMed:21645528). Positively regulates
CC postnatal regression of retinal hyaloid vessels via suppression of
CC VEGFR2/KDR activity, downstream of OPN5 (By similarity).
CC {ECO:0000250|UniProtKB:P61168, ECO:0000269|PubMed:21645528}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DRD4 (PubMed:21184734).
CC 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 (By similarity). Interacts with HTR2A
CC (PubMed:21645528). 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 Interacts with DRD1 (By similarity). Interacts with KCNA2 (By
CC similarity). {ECO:0000250|UniProtKB:P61168,
CC ECO:0000250|UniProtKB:P61169}.
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: Cell membrane {ECO:0000269|PubMed:21645528,
CC ECO:0000269|PubMed:26535572}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26535572};
CC Multi-pass membrane protein {ECO:0000255}.
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. Palmitoylation which is required for proper
CC localization to the plasma membrane and stability of the receptor could
CC be carried on by ZDHHC4, ZDHHC3 and ZDHHC8.
CC {ECO:0000269|PubMed:26535572}.
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:0000305|PubMed:15389757}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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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_000795.3. [P14416-1]
DR RefSeq; NP_057658.2; NM_016574.3. [P14416-2]
DR RefSeq; XP_016872785.1; XM_017017296.1. [P14416-1]
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=34-238, A=364-443.
DR PDB; 7JVR; EM; 2.80 A; R=1-443.
DR PDBsum; 5AER; -.
DR PDBsum; 6CM4; -.
DR PDBsum; 6LUQ; -.
DR PDBsum; 6VMS; -.
DR PDBsum; 7DFP; -.
DR PDBsum; 7JVR; -.
DR AlphaFoldDB; P14416; -.
DR SMR; P14416; -.
DR BioGRID; 108147; 98.
DR CORUM; P14416; -.
DR DIP; DIP-5977N; -.
DR IntAct; P14416; 77.
DR MINT; P14416; -.
DR STRING; 9606.ENSP00000354859; -.
DR BindingDB; P14416; -.
DR ChEMBL; CHEMBL217; -.
DR DrugBank; DB01614; Acepromazine.
DR DrugBank; DB01063; Acetophenazine.
DR DrugBank; DB05766; ACP-104.
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; DB00714; Apomorphine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB09207; AS-8112.
DR DrugBank; DB06216; Asenapine.
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; DB01038; Carphenazine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB11274; Dihydro-alpha-ergocryptine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB01184; Domperidone.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB00450; Droperidol.
DR DrugBank; DB11275; Epicriptine.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00696; Ergotamine.
DR DrugBank; DB01175; Escitalopram.
DR DrugBank; DB09194; Etoperidone.
DR DrugBank; DB00875; Flupentixol.
DR DrugBank; DB00623; Fluphenazine.
DR DrugBank; DB04842; Fluspirilene.
DR DrugBank; DB00502; Haloperidol.
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; DB01235; Levodopa.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB06077; Lumateperone.
DR DrugBank; DB08815; Lurasidone.
DR DrugBank; DB00934; Maprotiline.
DR DrugBank; DB09224; Melperone.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00933; Mesoridazine.
DR DrugBank; DB01403; Methotrimeprazine.
DR DrugBank; DB01233; Metoclopramide.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB01618; Molindone.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB06229; Ocaperidone.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB01267; Paliperidone.
DR DrugBank; DB12061; Pardoprunox.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01186; Pergolide.
DR DrugBank; DB08922; Perospirone.
DR DrugBank; DB00850; Perphenazine.
DR DrugBank; DB01100; Pimozide.
DR DrugBank; DB09286; Pipamperone.
DR DrugBank; DB01621; Pipotiazine.
DR DrugBank; DB12478; Piribedil.
DR DrugBank; DB00413; Pramipexole.
DR DrugBank; DB00433; Prochlorperazine.
DR DrugBank; DB00420; Promazine.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB00777; Propiomazine.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB09097; Quinagolide.
DR DrugBank; DB12518; Raclopride.
DR DrugBank; DB00409; Remoxipride.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB01549; Rolicyclidine.
DR DrugBank; DB00268; Ropinirole.
DR DrugBank; DB05271; Rotigotine.
DR DrugBank; DB06454; Sarizotan.
DR DrugBank; DB06144; Sertindole.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB06477; Sumanirole.
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; DB00831; Trifluoperazine.
DR DrugBank; DB00508; Triflupromazine.
DR DrugBank; DB00726; Trimipramine.
DR DrugBank; DB06109; YKP-1358.
DR DrugBank; DB01392; Yohimbine.
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 GlyGen; P14416; 3 sites.
DR iPTMnet; P14416; -.
DR PhosphoSitePlus; P14416; -.
DR SwissPalm; P14416; -.
DR BioMuta; DRD2; -.
DR DMDM; 118206; -.
DR MassIVE; P14416; -.
DR PaxDb; P14416; -.
DR PeptideAtlas; P14416; -.
DR PRIDE; P14416; -.
DR ProteomicsDB; 53053; -. [P14416-1]
DR ProteomicsDB; 53054; -. [P14416-2]
DR ProteomicsDB; 53055; -. [P14416-3]
DR ABCD; P14416; 2 sequenced antibodies.
DR Antibodypedia; 2801; 374 antibodies from 40 providers.
DR DNASU; 1813; -.
DR Ensembl; ENST00000346454.7; ENSP00000278597.5; ENSG00000149295.14. [P14416-2]
DR Ensembl; ENST00000362072.8; ENSP00000354859.3; ENSG00000149295.14. [P14416-1]
DR Ensembl; ENST00000538967.5; ENSP00000438215.1; ENSG00000149295.14. [P14416-3]
DR Ensembl; ENST00000542968.5; ENSP00000442172.1; ENSG00000149295.14. [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 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 neXtProt; NX_P14416; -.
DR OpenTargets; ENSG00000149295; -.
DR Orphanet; 36899; Myoclonus-dystonia syndrome.
DR PharmGKB; PA27478; -.
DR VEuPathDB; HostDB:ENSG00000149295; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155539; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P14416; -.
DR OMA; APMDPLN; -.
DR PhylomeDB; P14416; -.
DR TreeFam; TF334382; -.
DR PathwayCommons; P14416; -.
DR Reactome; R-HSA-390651; Dopamine receptors.
DR SignaLink; P14416; -.
DR SIGNOR; P14416; -.
DR BioGRID-ORCS; 1813; 13 hits in 1080 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 122 other tissues.
DR ExpressionAtlas; P14416; baseline and differential.
DR Genevisible; P14416; HS.
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:0098691; C:dopaminergic synapse; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IBA:GO_Central.
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:WormBase.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
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: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:1901363; F:heterocyclic compound binding; IEA:Ensembl.
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:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0046717; P:acid secretion; IEA:Ensembl.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0021984; P:adenohypophysis development; ISS:BHF-UCL.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
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:arachidonic acid 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:0048755; P:branching morphogenesis of a nerve; ISS:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IC:BHF-UCL.
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:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl.
DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; 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:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
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:0007194; P:negative regulation of adenylate cyclase activity; IDA:BHF-UCL.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISS:BHF-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
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:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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:0050680; P:negative regulation of epithelial cell proliferation; 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:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:BHF-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
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:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; ISS:BHF-UCL.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
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:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:BHF-UCL.
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:0040018; P:positive regulation of multicellular organism growth; 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:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
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:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
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:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
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: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 InterPro; IPR001922; Dopamine_D2_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00567; DOPAMINED2R.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="D(2) dopamine receptor"
FT /id="PRO_0000069387"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..188
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 189..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 374..395
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 396..409
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 410..431
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 432..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 211..373
FT /note="Interaction with PPP1R9B"
FT /evidence="ECO:0000250"
FT REGION 281..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 194
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
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:29466326,
FT ECO:0007744|PDB:6CM4"
FT DISULFID 399..401
FT /evidence="ECO:0000269|PubMed:29466326,
FT ECO:0007744|PDB:6CM4"
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; unknown pathological significance; the
FT mutation does not affect functional properties;
FT 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 (may be associated with a higher risk for
FT schizophrenia; 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 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 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 35..61
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6CM4"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 104..137
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 145..172
FT /evidence="ECO:0007829|PDB:7JVR"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6CM4"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 199..224
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 366..385
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:7JVR"
FT HELIX 405..426
FT /evidence="ECO:0007829|PDB:7JVR"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7JVR"
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
