NTDO_CAEEL
ID NTDO_CAEEL Reviewed; 615 AA.
AC Q03614; Q9XTK0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sodium-dependent dopamine transporter;
DE Short=DA transporter;
DE Short=DAT;
GN Name=dat-1 {ECO:0000312|WormBase:T23G5.5};
GN ORFNames=T23G5.5 {ECO:0000312|WormBase:T23G5.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9765501;
RA Jayanthi L.D., Apparsundaram S., Malone M.D., Ward E., Miller D.M.,
RA Eppler M., Blakely R.D.;
RT "The Caenorhabditis elegans gene T23G5.5 encodes an antidepressant- and
RT cocaine-sensitive dopamine transporter.";
RL Mol. Pharmacol. 54:601-609(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP ROLE IN SWIMMING-INDUCED PARALYSIS.
RX PubMed=20410438; DOI=10.1124/mol.109.062703;
RA Carvelli L., Matthies D.S., Galli A.;
RT "Molecular mechanisms of amphetamine actions in Caenorhabditis elegans.";
RL Mol. Pharmacol. 78:151-156(2010).
RN [5]
RP FUNCTION.
RX PubMed=29346382; DOI=10.1371/journal.pgen.1007125;
RA Offenburger S.L., Ho X.Y., Tachie-Menson T., Coakley S., Hilliard M.A.,
RA Gartner A.;
RT "6-OHDA-induced dopaminergic neurodegeneration in Caenorhabditis elegans is
RT promoted by the engulfment pathway and inhibited by the transthyretin-
RT related protein TTR-33.";
RL PLoS Genet. 14:E1007125-E1007125(2018).
CC -!- FUNCTION: Dopamine transporter (PubMed:9765501, PubMed:29346382).
CC Terminates the action of dopamine by its high affinity sodium-dependent
CC reuptake into presynaptic terminals. {ECO:0000269|PubMed:29346382,
CC ECO:0000269|PubMed:9765501}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9765501};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}.
CC -!- MISCELLANEOUS: This protein is the target of psychomotor stimulants
CC such as amphetamines or cocaine. Plays a role in promoting amphetamine-
CC induced loss of motility in water, termed swimming-induced paralysis
CC (PubMed:20410438). {ECO:0000269|PubMed:20410438}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. {ECO:0000305}.
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DR EMBL; AF079899; AAC83661.1; -; mRNA.
DR EMBL; BX284603; CAA79575.2; -; Genomic_DNA.
DR EMBL; Z19156; CAA79575.2; JOINED; Genomic_DNA.
DR PIR; D88551; D88551.
DR PIR; S28306; S28306.
DR PIR; T43330; T43330.
DR RefSeq; NP_499043.1; NM_066642.5.
DR AlphaFoldDB; Q03614; -.
DR SMR; Q03614; -.
DR BioGRID; 41503; 1.
DR DIP; DIP-46293N; -.
DR IntAct; Q03614; 1.
DR STRING; 6239.T23G5.5; -.
DR TCDB; 2.A.22.1.4; the neurotransmitter:sodium symporter (nss) family.
DR PaxDb; Q03614; -.
DR EnsemblMetazoa; T23G5.5.1; T23G5.5.1; WBGene00000934.
DR GeneID; 176304; -.
DR KEGG; cel:CELE_T23G5.5; -.
DR UCSC; T23G5.5; c. elegans.
DR CTD; 176304; -.
DR WormBase; T23G5.5; CE25124; WBGene00000934; dat-1.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000173306; -.
DR HOGENOM; CLU_006855_9_0_1; -.
DR InParanoid; Q03614; -.
DR OMA; IMGHFAF; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q03614; -.
DR Reactome; R-CEL-379401; Dopamine clearance from the synaptic cleft.
DR Reactome; R-CEL-442660; Na+/Cl- dependent neurotransmitter transporters.
DR PRO; PR:Q03614; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000934; Expressed in larva and 3 other tissues.
DR GO; GO:0030673; C:axolemma; IDA:WormBase.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:WormBase.
DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IMP:WormBase.
DR GO; GO:0005254; F:chloride channel activity; IDA:WormBase.
DR GO; GO:0005330; F:dopamine:sodium symporter activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015837; P:amine transport; IMP:WormBase.
DR GO; GO:0071419; P:cellular response to amphetamine; IMP:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:WormBase.
DR GO; GO:0090494; P:dopamine uptake; IDA:WormBase.
DR GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IDA:WormBase.
DR GO; GO:1905803; P:negative regulation of cellular response to manganese ion; IGI:UniProtKB.
DR GO; GO:1905847; P:negative regulation of cellular response to oxidopamine; IMP:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0015874; P:norepinephrine transport; IBA:GO_Central.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Neurotransmitter transport; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Sodium-dependent dopamine transporter"
FT /id="PRO_0000214815"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 47..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 73..76
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 77..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 101..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 121..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 152..229
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 230..250
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 251..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 254..278
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 279..302
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 303..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 329..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 335..358
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 359..398
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 399..424
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 425..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 440..460
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 461
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 462..488
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 489..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 519..541
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 542..544
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 545..565
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 566..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 57
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 58
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 62
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 314
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 346
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 411
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 414
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 415
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..170
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
SQ SEQUENCE 615 AA; 69266 MW; 0DA2876EB3AC8049 CRC64;
MQLVPTDDPD EKIGRTSNGM QNATLPIDGP VNTEPKDPAR EQWSGKLDFL LSVVGFAVDL
GNIWRFPYLC FKNGGGVFLI PYSIMVLLTG VPLFYMELCL GQYYRKGAIT TWGRICPLFK
GIGYCVILTA FYVDFFYNVI LAWGLHYLYT SFSFNLPWAS CNNSYNSPAC YEPHWSEDGT
AMCRSANQSV SAEKISAAEE YFYKGFLGLH EANAPNSHVI RSVTDLGNVR WDIALSLFVV
YLICYFSMWK GIHTSGKVVW FTALFPYVVL GILFIRGVTL PGWQNGIEYY LRPNFEMLKR
PSVWQDAATQ VFFSLGPGFG VLMAYSSYND FHNNVYVDAL FTSFINCATS FLSGFVIFSV
LGYMSCKSGK PIEAVAQEGP GLVFVVYPEA LSTMPYAPFW SVLFFLMLMT LGLDSSFGGS
EAIITGLSDE FPILKKNREV FVGCLFAFYM VIGIAMCTEG GILIMEWLII YGTTWGLLIA
VFCEAMVIAY IYGLRQFVHD VKEMMGFRPG NYWKFCWSCA APFILLSMIT SNFINYQALT
YQDYTYPTAA NVIGIIFALS GASFIPLVGI YKFVNARGNT ISEKWQRVTM PYRKRPNQTE
YIPIPTTQPH SDIML
