ID DRD5_HUMAN Reviewed; 477 AA. AC P21918; B2R9S3; Q8NEQ8; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 2. DT 27-MAR-2024, entry version 230. DE RecName: Full=D(1B) dopamine receptor; DE AltName: Full=D(5) dopamine receptor; DE AltName: Full=D1beta dopamine receptor; DE AltName: Full=Dopamine D5 receptor; GN Name=DRD5; Synonyms=DRD1B, DRD1L2; 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 [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=1826762; DOI=10.1038/350614a0; RA Sunahara R.K., Guan H.-C., O'Dowd B.F., Seeman P., Laurier L.G., Ng G., RA George S.R., Torchia J., van Tol H.H.M., Niznik H.B.; RT "Cloning of the gene for a human dopamine D5 receptor with higher affinity RT for dopamine than D1."; RL Nature 350:614-619(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1833775; DOI=10.1073/pnas.88.20.9175; RA Grandy D.K., Zhang Y., Bouvier C., Zhou Q.-Y., Johnson R.A., Allen L., RA Buck K., Bunzow J.R., Salon J., Civelli O.; RT "Multiple human D5 dopamine receptor genes: a functional receptor and two RT pseudogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9175-9179(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Spleen; RX PubMed=1834671; DOI=10.1016/s0021-9258(18)54590-7; RA Weinshank R.L., Adham N., Macchi M., Olsen M.A., Branchek T.A., RA Hartig P.R.; RT "Molecular cloning and characterization of a high affinity dopamine RT receptor (D1 beta) and its pseudogene."; RL J. Biol. Chem. 266:22427-22435(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [8] RP GLYCOSYLATION AT ASN-7, AND MUTAGENESIS OF ASN-7. RX PubMed=10531415; DOI=10.1124/mol.56.5.1071; RA Karpa K.D., Lidow M.S., Pickering M.T., Levenson R., Bergson C.; RT "N-linked glycosylation is required for plasma membrane localization of D5, RT but not D1, dopamine receptors in transfected mammalian cells."; RL Mol. Pharmacol. 56:1071-1078(1999). RN [9] RP INVOLVEMENT IN BEB. RX PubMed=11781417; DOI=10.1212/wnl.58.1.124; RA Misbahuddin A., Placzek M.R., Chaudhuri K.R., Wood N.W., Bhatia K.P., RA Warner T.T.; RT "A polymorphism in the dopamine receptor DRD5 is associated with RT blepharospasm."; RL Neurology 58:124-126(2002). RN [10] RP VARIANTS VAL-269; GLN-330; ASP-351 AND CYS-453. RX PubMed=7633397; DOI=10.1093/hmg/4.4.507; RA Sobell J.L., Lind T.J., Sigurdson D.C., Zald D.H., Snitz B.E., Grove W.M., RA Heston L.L., Sommer S.S.; RT "The D5 dopamine receptor gene in schizophrenia: identification of a RT nonsense change and multiple missense changes but lack of association with RT disease."; RL Hum. Mol. Genet. 4:507-514(1995). RN [11] RP VARIANT ARG-88. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [12] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins CC which activate adenylyl cyclase. {ECO:0000269|PubMed:1834671}. CC -!- INTERACTION: CC P21918; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12139313, EBI-22310682; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Neuron-specific, localized primarily within limbic CC regions of the brain. {ECO:0000269|PubMed:1834671}. CC -!- DISEASE: Benign essential blepharospasm (BEB) [MIM:606798]: A primary CC focal dystonia affecting the orbicularis oculi muscles. Dystonia is CC defined by the presence of sustained involuntary muscle contraction, CC often leading to abnormal postures. BEB usually begins in middle age. CC Initial symptoms include eye irritation and frequent blinking, CC progressing to involuntary spasms of eyelid closure. Patients have CC normal eyes. The visual disturbance is due solely to the forced closure CC of the eyelids. In severe cases, this can lead to functional blindness. CC {ECO:0000269|PubMed:11781417}. Note=Disease susceptibility may be CC associated with variants affecting the gene represented in this entry. 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; X58454; CAA41360.1; -; Genomic_DNA. DR EMBL; M67439; AAA52329.1; -; Genomic_DNA. DR EMBL; AY136750; AAN01276.1; -; mRNA. DR EMBL; AK313897; BAG36620.1; -; mRNA. DR EMBL; CH471069; EAW92679.1; -; Genomic_DNA. DR EMBL; BC009748; AAH09748.1; -; mRNA. DR CCDS; CCDS3405.1; -. DR PIR; S15080; DYHUD5. DR RefSeq; NP_000789.1; NM_000798.4. DR PDB; 8IRV; EM; 3.10 A; R=1-477. DR PDBsum; 8IRV; -. DR AlphaFoldDB; P21918; -. DR EMDB; EMD-35687; -. DR SMR; P21918; -. DR BioGRID; 108150; 7. DR IntAct; P21918; 1. DR STRING; 9606.ENSP00000306129; -. DR BindingDB; P21918; -. DR ChEMBL; CHEMBL1850; -. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB01038; Carphenazine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB11274; Dihydro-alpha-ergocryptine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB11275; Epicriptine. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB00800; Fenoldopam. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB01235; Levodopa. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB11584; Pipradrol. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB09097; Quinagolide. DR DrugBank; DB05271; Rotigotine. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB09225; Zotepine. DR DrugBank; DB01624; Zuclopenthixol. DR DrugCentral; P21918; -. DR GuidetoPHARMACOLOGY; 218; -. DR GlyCosmos; P21918; 2 sites, No reported glycans. DR GlyGen; P21918; 2 sites. DR iPTMnet; P21918; -. DR PhosphoSitePlus; P21918; -. DR BioMuta; DRD5; -. DR DMDM; 118214; -. DR jPOST; P21918; -. DR MassIVE; P21918; -. DR PaxDb; 9606-ENSP00000306129; -. DR PeptideAtlas; P21918; -. DR Antibodypedia; 9652; 456 antibodies from 39 providers. DR DNASU; 1816; -. DR Ensembl; ENST00000304374.4; ENSP00000306129.2; ENSG00000169676.6. DR GeneID; 1816; -. DR KEGG; hsa:1816; -. DR MANE-Select; ENST00000304374.4; ENSP00000306129.2; NM_000798.5; NP_000789.1. DR UCSC; uc003gmb.5; human. DR AGR; HGNC:3026; -. DR CTD; 1816; -. DR DisGeNET; 1816; -. DR GeneCards; DRD5; -. DR HGNC; HGNC:3026; DRD5. DR HPA; ENSG00000169676; Group enriched (brain, lymphoid tissue, stomach). DR MalaCards; DRD5; -. DR MIM; 126453; gene. DR MIM; 606798; phenotype. DR neXtProt; NX_P21918; -. DR OpenTargets; ENSG00000169676; -. DR PharmGKB; PA148; -. DR VEuPathDB; HostDB:ENSG00000169676; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000157037; -. DR HOGENOM; CLU_009579_11_0_1; -. DR InParanoid; P21918; -. DR OMA; HWHRDKA; -. DR OrthoDB; 2900736at2759; -. DR PhylomeDB; P21918; -. DR TreeFam; TF325181; -. DR PathwayCommons; P21918; -. DR Reactome; R-HSA-390651; Dopamine receptors. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR SignaLink; P21918; -. DR SIGNOR; P21918; -. DR BioGRID-ORCS; 1816; 180 hits in 1152 CRISPR screens. DR GeneWiki; Dopamine_receptor_D5; -. DR GenomeRNAi; 1816; -. DR Pharos; P21918; Tchem. DR PRO; PR:P21918; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P21918; Protein. DR Bgee; ENSG00000169676; Expressed in pancreatic ductal cell and 43 other cell types or tissues. DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl. DR GO; GO:0060170; C:ciliary membrane; IDA:SYSCILIA_CCNET. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0097730; C:non-motile cilium; IDA:SYSCILIA_CCNET. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0035240; F:dopamine binding; IDA:UniProtKB. DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:UniProtKB. DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:BHF-UCL. DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0008306; P:associative learning; IEA:Ensembl. DR GO; GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL. DR GO; GO:0007268; P:chemical synaptic transmission; NAS:UniProtKB. DR GO; GO:0007212; P:dopamine receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; TAS:BHF-UCL. DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IDA:UniProtKB. DR GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; TAS:BHF-UCL. DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; NAS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0045924; P:regulation of female receptivity; IEA:Ensembl. DR GO; GO:0001992; P:regulation of systemic arterial blood pressure by vasopressin; IEA:Ensembl. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0046960; P:sensitization; IEA:Ensembl. DR GO; GO:0001963; P:synaptic transmission, dopaminergic; NAS:UniProtKB. DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000497; Dopamine_D5_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:SF136; D(1B) DOPAMINE RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00566; DOPAMINED1BR. 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. DR Genevisible; P21918; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; Dystonia; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..477 FT /note="D(1B) dopamine receptor" FT /id="PRO_0000069405" FT TOPO_DOM 1..39 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 40..66 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 67..77 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 78..104 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 105..114 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 115..136 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 137..158 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 159..180 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 181..223 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 224..246 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 247..296 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 297..320 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 321..340 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 341..360 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 361..477 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT LIPID 375 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:10531415" FT CARBOHYD 222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 113..217 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VARIANT 62 FT /note="C -> S (in dbSNP:rs2227840)" FT /id="VAR_029210" FT VARIANT 88 FT /note="L -> R (in dbSNP:rs6282)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_011837" FT VARIANT 110 FT /note="G -> E (in dbSNP:rs2227849)" FT /id="VAR_029211" FT VARIANT 207 FT /note="F -> V (in dbSNP:rs2227845)" FT /id="VAR_029212" FT VARIANT 233 FT /note="S -> N (in dbSNP:rs2227843)" FT /id="VAR_029213" FT VARIANT 238 FT /note="V -> I (in dbSNP:rs2227852)" FT /id="VAR_024254" FT VARIANT 269 FT /note="A -> V (in dbSNP:rs538877978)" FT /evidence="ECO:0000269|PubMed:7633397" FT /id="VAR_003458" FT VARIANT 286 FT /note="A -> V (in dbSNP:rs2227850)" FT /id="VAR_029215" FT VARIANT 297 FT /note="T -> P (in dbSNP:rs2227851)" FT /id="VAR_061217" FT VARIANT 330 FT /note="P -> Q (in dbSNP:rs1800762)" FT /evidence="ECO:0000269|PubMed:7633397" FT /id="VAR_003459" FT VARIANT 351 FT /note="N -> D (in dbSNP:rs1577263526)" FT /evidence="ECO:0000269|PubMed:7633397" FT /id="VAR_003460" FT VARIANT 453 FT /note="S -> C (in dbSNP:rs776114395)" FT /evidence="ECO:0000269|PubMed:7633397" FT /id="VAR_003461" FT MUTAGEN 7 FT /note="N->Q: Impairs subcellular location." FT /evidence="ECO:0000269|PubMed:10531415" FT HELIX 38..67 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 69..73 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 76..93 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 95..104 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 110..143 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 145..151 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 154..177 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 223..233 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 235..270 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 291..322 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 338..360 FT /evidence="ECO:0007829|PDB:8IRV" FT HELIX 363..373 FT /evidence="ECO:0007829|PDB:8IRV" SQ SEQUENCE 477 AA; 52951 MW; BACCB85E5A72F9CA CRC64; MLPPGSNGTA YPGQFALYQQ LAQGNAVGGS AGAPPLGPSQ VVTACLLTLL IIWTLLGNVL VCAAIVRSRH LRANMTNVFI VSLAVSDLFV ALLVMPWKAV AEVAGYWPFG AFCDVWVAFD IMCSTASILN LCVISVDRYW AISRPFRYKR KMTQRMALVM VGLAWTLSIL ISFIPVQLNW HRDQAASWGG LDLPNNLANW TPWEEDFWEP DVNAENCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQVQIRRIS SLERAAEHAQ SCRSSAACAP DTSLRASIKK ETKVLKTLSV IMGVFVCCWL PFFILNCMVP FCSGHPEGPP AGFPCVSETT FDVFVWFGWA NSSLNPVIYA FNADFQKVFA QLLGCSHFCS RTPVETVNIS NELISYNQDI VFHKEIAAAY IHMMPNAVTP GNREVDNDEE EGPFDRMFQI YQTSPDGDPV AESVWELDCE GEISLDKITP FTPNGFH //