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Sodium-dependent dopamine transporter (DA transporter) (DAT) (Solute carrier family 6 member 3)

 SC6A3_HUMAN             Reviewed;         620 AA.
Q01959; A2RUN4; Q14996;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
12-SEP-2018, entry version 192.
RecName: Full=Sodium-dependent dopamine transporter;
Short=DA transporter;
Short=DAT;
AltName: Full=Solute carrier family 6 member 3;
Name=SLC6A3; Synonyms=DAT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1359373; DOI=10.1016/0169-328X(92)90165-8;
Vandenbergh D.J., Persico A.M., Uhl G.R.;
"A human dopamine transporter cDNA predicts reduced glycosylation,
displays a novel repetitive element and provides racially-dimorphic
TaqI RFLPs.";
Brain Res. Mol. Brain Res. 15:161-166(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=1406597;
Giros B., el Mestikawy S., Godinot N., Zheng K., Han H., Yang-Feng T.,
Caron M.G.;
"Cloning, pharmacological characterization, and chromosome assignment
of the human dopamine transporter.";
Mol. Pharmacol. 42:383-390(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=8302271;
Pristupa Z.B., Wilson J.M., Hoffman B.J., Kish S.J., Niznik H.B.;
"Pharmacological heterogeneity of the cloned and native human dopamine
transporter: disassociation of [3H]WIN 35,428 and [3H]GBR 12,935
binding.";
Mol. Pharmacol. 45:125-135(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9300814; DOI=10.1016/S0378-1119(97)00131-5;
Kawarai T., Kawakami H., Yamamura Y., Nakamura S.;
"Structure and organization of the gene encoding human dopamine
transporter.";
Gene 195:11-18(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10889531; DOI=10.1038/sj.mp.4000701;
Vandenbergh D.J., Thompson M.D., Cook E.H., Bendahhou E., Nguyen T.,
Krasowski M.D., Zarrabian D., Comings D., Sellers E.M., Tyndale R.F.,
George S.R., O'Dowd B.F., Uhl G.R.;
"Human dopamine transporter gene: coding region conservation among
normal, Tourette's disorder, alcohol dependence and attention-deficit
hyperactivity disorder populations.";
Mol. Psychiatry 5:283-292(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11304827;
DOI=10.1002/1096-8628(2001)9999:9999<::AID-AJMG1161>3.0.CO;2-8;
Greenwood T.A., Alexander M., Keck P.E., McElroy S., Sadovnick A.D.,
Remick R.A., Kelsoe J.R.;
"Evidence for linkage disequilibrium between the dopamine transporter
and bipolar disorder.";
Am. J. Med. Genet. 105:145-151(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=17934207; DOI=10.1093/molbev/msm219;
Miller-Butterworth C.M., Kaplan J.R., Shaffer J., Devlin B.,
Manuck S.B., Ferrell R.E.;
"Sequence variation in the primate dopamine transporter gene and its
relationship to social dominance.";
Mol. Biol. Evol. 25:18-28(2008).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-385, AND TISSUE
SPECIFICITY.
PubMed=7637582; DOI=10.1016/0169-328X(95)00018-N;
Donovan D.M., Vandenbergh D.J., Perry M.P., Bird G.S., Ingersoll R.,
Nanthakumar E., Uhl G.R.;
"Human and mouse dopamine transporter genes: conservation of 5'-
flanking sequence elements and gene structures.";
Brain Res. Mol. Brain Res. 30:327-335(1995).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 164-255.
PubMed=1353885; DOI=10.1073/pnas.89.15.7095;
Bannon M.J., Poosch M.S., Xia Y., Goebel D.J., Cassin B., Kapatos G.;
"Dopamine transporter mRNA content in human substantia nigra decreases
precipitously with age.";
Proc. Natl. Acad. Sci. U.S.A. 89:7095-7099(1992).
[13]
INTERACTION WITH PRKCABP.
PubMed=11343649; DOI=10.1016/S0896-6273(01)00267-7;
Torres G.E., Yao W.-D., Mohn A.R., Quan H., Kim K.-M., Levey A.I.,
Staudinger J., Caron M.G.;
"Functional interaction between monoamine plasma membrane transporters
and the synaptic PDZ domain-containing protein PICK1.";
Neuron 30:121-134(2001).
[14]
INTERCHAIN DISULFIDE BOND, AND SUBUNIT.
Hastrup H., Karlin A., Javitch J.A.;
"Symmetrical homodimer of the human dopamine transporter revealed by
cross-linking Cys306 at the extracellular end of TM6.";
Abstr. - Soc. Neurosci. 27:1866-1866(2001).
[15]
INTERACTION WITH TGFB1I1.
PubMed=12177201;
Carneiro A.M.D., Ingram S.L., Beaulieu J.-M., Sweeney A., Amara S.G.,
Thomas S.M., Caron M.G., Torres G.E.;
"The multiple LIM domain-containing adaptor protein Hic-5 synaptically
colocalizes and interacts with the dopamine transporter.";
J. Neurosci. 22:7045-7054(2002).
[16]
FUNCTION AS DOPAMINE TRANSPORTER, INTERACTION WITH TOR1A, AND
SUBCELLULAR LOCATION.
PubMed=15505207; DOI=10.1073/pnas.0308088101;
Torres G.E., Sweeney A.L., Beaulieu J.M., Shashidharan P., Caron M.G.;
"Effect of torsinA on membrane proteins reveals a loss of function and
a dominant-negative phenotype of the dystonia-associated DeltaE-
torsinA mutant.";
Proc. Natl. Acad. Sci. U.S.A. 101:15650-15655(2004).
[17]
VARIANT GLN-237.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[18]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[19]
VARIANTS [LARGE SCALE ANALYSIS] SER-121 AND SER-544.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[20]
VARIANTS PKDYS GLN-368 AND LEU-395, AND CHARACTERIZATION OF VARIANTS
PKDYS GLN-368 AND LEU-395.
PubMed=19478460; DOI=10.1172/JCI39060;
Kurian M.A., Zhen J., Cheng S.Y., Li Y., Mordekar S.R., Jardine P.,
Morgan N.V., Meyer E., Tee L., Pasha S., Wassmer E., Heales S.J.,
Gissen P., Reith M.E., Maher E.R.;
"Homozygous loss-of-function mutations in the gene encoding the
dopamine transporter are associated with infantile parkinsonism-
dystonia.";
J. Clin. Invest. 119:1595-1603(2009).
[21]
VARIANT ILE-471.
PubMed=21179162; DOI=10.1038/nature09629;
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A.,
Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J.,
Peltonen L., Virkkunen M., Goldman D.;
"A population-specific HTR2B stop codon predisposes to severe
impulsivity.";
Nature 468:1061-1066(2010).
-!- FUNCTION: Amine transporter. Terminates the action of dopamine by
its high affinity sodium-dependent reuptake into presynaptic
terminals. {ECO:0000269|PubMed:1406597,
ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:8302271}.
-!- SUBUNIT: Homooligomer; disulfide-linked (Ref.14). Interacts with
PRKCABP and TGFB1I1 (PubMed:11343649, PubMed:12177201). Interacts
(via N-terminus) with SYNGR3 (via N-terminus). Interacts with
SLC18A2. Interacts with TOR1A (ATP-bound); TOR1A regulates SLC6A3
subcellular location (By similarity).
{ECO:0000250|UniProtKB:Q61327, ECO:0000269|PubMed:11343649,
ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:15505207,
ECO:0000269|Ref.14}.
-!- INTERACTION:
P14416:DRD2; NbExp=4; IntAct=EBI-6661445, EBI-2928178;
O15354:GPR37; NbExp=2; IntAct=EBI-6661445, EBI-15639515;
Q9EP80:Pick1 (xeno); NbExp=2; IntAct=EBI-6661445, EBI-77728;
Q99578:RIT2; NbExp=5; IntAct=EBI-6661445, EBI-365914;
Q5BJQ5:Rit2 (xeno); NbExp=2; IntAct=EBI-6661445, EBI-11686902;
P37840:SNCA; NbExp=3; IntAct=EBI-6661445, EBI-985879;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1406597,
ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:8302271}; Multi-
pass membrane protein {ECO:0000269|PubMed:15505207}.
-!- TISSUE SPECIFICITY: Highly expressed in substantia nigra.
{ECO:0000269|PubMed:7637582}.
-!- DISEASE: Parkinsonism-dystonia infantile (PKDYS) [MIM:613135]: A
neurodegenerative disorder characterized by infantile onset of
parkinsonism and dystonia. Other neurologic features include
global developmental delay, bradykinesia and pyramidal tract
signs. {ECO:0000269|PubMed:19478460}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: This protein is the target of psychomotor
stimulants such as amphetamines or cocaine.
-!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
(TC 2.A.22) family. SLC6A3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/slc6a3/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Dopamine transporter entry;
URL="https://en.wikipedia.org/wiki/Dopamine_transporter";
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EMBL; M95167; AAC41720.1; -; mRNA.
EMBL; S46955; AAA11754.1; -; mRNA.
EMBL; S44626; AAB23443.1; -; mRNA.
EMBL; L24178; AAA19560.1; -; mRNA.
EMBL; D88570; BAA22511.1; -; Genomic_DNA.
EMBL; AF119117; AAC50179.2; -; Genomic_DNA.
EMBL; AF321321; AAG33844.1; -; Genomic_DNA.
EMBL; AF306558; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF321320; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306559; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306560; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306561; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306562; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306563; AAG33844.1; JOINED; Genomic_DNA.
EMBL; AF306564; AAG33844.1; JOINED; Genomic_DNA.
EMBL; EF174603; ABO77644.1; -; mRNA.
EMBL; AY623110; AAT38106.1; -; Genomic_DNA.
EMBL; CH471102; EAX08159.1; -; Genomic_DNA.
EMBL; BC132977; AAI32978.1; -; mRNA.
EMBL; BC133003; AAI33004.1; -; mRNA.
EMBL; M96670; AAA35770.1; -; mRNA.
CCDS; CCDS3863.1; -.
PIR; A48980; A48980.
PIR; I57937; I57937.
PIR; I84455; I84455.
RefSeq; NP_001035.1; NM_001044.4.
UniGene; Hs.406; -.
ProteinModelPortal; Q01959; -.
SMR; Q01959; -.
BioGrid; 112422; 14.
DIP; DIP-41827N; -.
IntAct; Q01959; 8.
MINT; Q01959; -.
STRING; 9606.ENSP00000270349; -.
BindingDB; Q01959; -.
ChEMBL; CHEMBL238; -.
DrugBank; DB01472; 4-Methoxyamphetamine.
DrugBank; DB04947; Altropane.
DrugBank; DB00543; Amoxapine.
DrugBank; DB00182; Amphetamine.
DrugBank; DB06413; Armodafinil.
DrugBank; DB00289; Atomoxetine.
DrugBank; DB00245; Benzatropine.
DrugBank; DB00865; Benzphetamine.
DrugBank; DB01156; Bupropion.
DrugBank; DB01161; Chloroprocaine.
DrugBank; DB01114; Chlorphenamine.
DrugBank; DB00215; Citalopram.
DrugBank; DB00907; Cocaine.
DrugBank; DB06701; Dexmethylphenidate.
DrugBank; DB01576; Dextroamphetamine.
DrugBank; DB00937; Diethylpropion.
DrugBank; DB01146; Diphenylpyraline.
DrugBank; DB00988; Dopamine.
DrugBank; DB00476; Duloxetine.
DrugBank; DB01363; Ephedra.
DrugBank; DB01175; Escitalopram.
DrugBank; DB01463; Fencamfamine.
DrugBank; DB00458; Imipramine.
DrugBank; DB08824; Ioflupane I-123.
DrugBank; DB01255; Lisdexamfetamine.
DrugBank; DB00408; Loxapine.
DrugBank; DB00579; Mazindol.
DrugBank; DB01577; Methamphetamine.
DrugBank; DB09543; Methyl salicylate.
DrugBank; DB00422; Methylphenidate.
DrugBank; DB06148; Mianserin.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01442; MMDA.
DrugBank; DB00745; Modafinil.
DrugBank; DB01149; Nefazodone.
DrugBank; DB04821; Nomifensine.
DrugBank; DB00454; Pethidine.
DrugBank; DB00830; Phenmetrazine.
DrugBank; DB00191; Phentermine.
DrugBank; DB00721; Procaine.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB01104; Sertraline.
DrugBank; DB01105; Sibutramine.
DrugBank; DB00726; Trimipramine.
DrugBank; DB00285; Venlafaxine.
GuidetoPHARMACOLOGY; 927; -.
TCDB; 2.A.22.1.3; the neurotransmitter:sodium symporter (nss) family.
iPTMnet; Q01959; -.
PhosphoSitePlus; Q01959; -.
BioMuta; SLC6A3; -.
DMDM; 266667; -.
PaxDb; Q01959; -.
PeptideAtlas; Q01959; -.
PRIDE; Q01959; -.
ProteomicsDB; 58021; -.
Ensembl; ENST00000270349; ENSP00000270349; ENSG00000142319.
Ensembl; ENST00000621716; ENSP00000479597; ENSG00000276996.
GeneID; 6531; -.
KEGG; hsa:6531; -.
UCSC; uc003jck.4; human.
CTD; 6531; -.
DisGeNET; 6531; -.
EuPathDB; HostDB:ENSG00000142319.17; -.
GeneCards; SLC6A3; -.
HGNC; HGNC:11049; SLC6A3.
HPA; CAB016249; -.
HPA; CAB078172; -.
HPA; HPA012763; -.
HPA; HPA013602; -.
MalaCards; SLC6A3; -.
MIM; 126455; gene.
MIM; 613135; phenotype.
neXtProt; NX_Q01959; -.
OpenTargets; ENSG00000142319; -.
Orphanet; 238455; Infantile dystonia-parkinsonism.
PharmGKB; PA311; -.
eggNOG; KOG3659; Eukaryota.
eggNOG; COG0733; LUCA.
GeneTree; ENSGT00760000118857; -.
HOGENOM; HOG000116406; -.
HOVERGEN; HBG071421; -.
InParanoid; Q01959; -.
KO; K05036; -.
OMA; GMATFIF; -.
OrthoDB; EOG091G08PX; -.
PhylomeDB; Q01959; -.
TreeFam; TF343812; -.
Reactome; R-HSA-379401; Dopamine clearance from the synaptic cleft.
Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
Reactome; R-HSA-5619081; Defective SLC6A3 causes Parkinsonism-dystonia infantile (PKDYS).
Reactome; R-HSA-5660724; Defective SLC6A3 causes Parkinsonism-dystonia infantile (PKDYS).
SABIO-RK; Q01959; -.
ChiTaRS; SLC6A3; human.
GeneWiki; Dopamine_transporter; -.
GenomeRNAi; 6531; -.
PMAP-CutDB; Q01959; -.
PRO; PR:Q01959; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000142319; Expressed in 60 organ(s), highest expression level in substantia nigra.
CleanEx; HS_SLC6A3; -.
Genevisible; Q01959; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:ParkinsonsUK-UCL.
GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0035240; F:dopamine binding; IEA:Ensembl.
GO; GO:0005329; F:dopamine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005330; F:dopamine:sodium symporter activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008504; F:monoamine transmembrane transporter activity; IDA:MGI.
GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0021984; P:adenohypophysis development; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
GO; GO:0042420; P:dopamine catabolic process; IEA:Ensembl.
GO; GO:0015872; P:dopamine transport; IDA:UniProtKB.
GO; GO:0090494; P:dopamine uptake; IDA:ParkinsonsUK-UCL.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IBA:GO_Central.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0015844; P:monoamine transport; IDA:MGI.
GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:Reactome.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
InterPro; IPR000175; Na/ntran_symport.
InterPro; IPR002436; Na/ntran_symport_dopamine.
InterPro; IPR037272; SNS_sf.
PANTHER; PTHR11616; PTHR11616; 1.
Pfam; PF00209; SNF; 1.
PRINTS; PR01202; DOPTRANSPORT.
PRINTS; PR00176; NANEUSMPORT.
SUPFAM; SSF161070; SSF161070; 1.
PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disease mutation; Disulfide bond;
Dystonia; Glycoprotein; Membrane; Metal-binding; Neurodegeneration;
Neurotransmitter transport; Parkinsonism; Polymorphism;
Reference proteome; Sodium; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 620 Sodium-dependent dopamine transporter.
/FTId=PRO_0000214751.
TOPO_DOM 1 68 Cytoplasmic. {ECO:0000255}.
TRANSMEM 69 89 Helical; Name=1. {ECO:0000255}.
TRANSMEM 96 116 Helical; Name=2. {ECO:0000255}.
TRANSMEM 140 160 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 161 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 256 Helical; Name=4. {ECO:0000255}.
TRANSMEM 265 282 Helical; Name=5. {ECO:0000255}.
TRANSMEM 318 335 Helical; Name=6. {ECO:0000255}.
TRANSMEM 347 368 Helical; Name=7. {ECO:0000255}.
TRANSMEM 401 420 Helical; Name=8. {ECO:0000255}.
TRANSMEM 447 465 Helical; Name=9. {ECO:0000255}.
TRANSMEM 481 501 Helical; Name=10. {ECO:0000255}.
TRANSMEM 522 541 Helical; Name=11. {ECO:0000255}.
TRANSMEM 560 578 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 579 620 Cytoplasmic. {ECO:0000255}.
REGION 561 590 Interaction with TGFB1I1.
{ECO:0000269|PubMed:12177201}.
METAL 75 75 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 77 77 Sodium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 78 78 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 82 82 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 321 321 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 353 353 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 418 418 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 421 421 Sodium 1. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 422 422 Sodium 1. {ECO:0000250|UniProtKB:Q7K4Y6}.
SITE 105 105 Contributes to high-affinity binding to
cocaine. {ECO:0000250|UniProtKB:Q61327}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 180 189 {ECO:0000250|UniProtKB:Q7K4Y6}.
DISULFID 306 306 Interchain. {ECO:0000269|Ref.14}.
VARIANT 121 121 G -> S (in a breast cancer sample;
somatic mutation; dbSNP:rs760871529).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036158.
VARIANT 237 237 R -> Q (in dbSNP:rs6345).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014180.
VARIANT 368 368 L -> Q (in PKDYS; loss of function;
dbSNP:rs267607068).
{ECO:0000269|PubMed:19478460}.
/FTId=VAR_063771.
VARIANT 395 395 P -> L (in PKDYS; loss of function;
dbSNP:rs267607069).
{ECO:0000269|PubMed:19478460}.
/FTId=VAR_063772.
VARIANT 471 471 V -> I (in dbSNP:rs75916702).
{ECO:0000269|PubMed:21179162}.
/FTId=VAR_064580.
VARIANT 544 544 R -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036159.
CONFLICT 35 35 K -> M (in Ref. 2; AAB23443).
{ECO:0000305}.
CONFLICT 354 354 S -> C (in Ref. 2; AAB23443).
{ECO:0000305}.
SEQUENCE 620 AA; 68495 MW; CD95009B6BA93108 CRC64;
MSKSKCSVGL MSSVVAPAKE PNAVGPKEVE LILVKEQNGV QLTSSTLTNP RQSPVEAQDR
ETWGKKIDFL LSVIGFAVDL ANVWRFPYLC YKNGGGAFLV PYLLFMVIAG MPLFYMELAL
GQFNREGAAG VWKICPILKG VGFTVILISL YVGFFYNVII AWALHYLFSS FTTELPWIHC
NNSWNSPNCS DAHPGDSSGD SSGLNDTFGT TPAAEYFERG VLHLHQSHGI DDLGPPRWQL
TACLVLVIVL LYFSLWKGVK TSGKVVWITA TMPYVVLTAL LLRGVTLPGA IDGIRAYLSV
DFYRLCEASV WIDAATQVCF SLGVGFGVLI AFSSYNKFTN NCYRDAIVTT SINSLTSFSS
GFVVFSFLGY MAQKHSVPIG DVAKDGPGLI FIIYPEAIAT LPLSSAWAVV FFIMLLTLGI
DSAMGGMESV ITGLIDEFQL LHRHRELFTL FIVLATFLLS LFCVTNGGIY VFTLLDHFAA
GTSILFGVLI EAIGVAWFYG VGQFSDDIQQ MTGQRPSLYW RLCWKLVSPC FLLFVVVVSI
VTFRPPHYGA YIFPDWANAL GWVIATSSMA MVPIYAAYKF CSLPGSFREK LAYAIAPEKD
RELVDRGEVR QFTLRHWLKV


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