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Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4)

 SC6A4_RAT               Reviewed;         630 AA.
P31652; P23976;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Sodium-dependent serotonin transporter;
Short=SERT {ECO:0000303|PubMed:16870614};
AltName: Full=5HT transporter;
Short=5HTT;
AltName: Full=Solute carrier family 6 member 4;
Name=Slc6a4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
PubMed=1765155; DOI=10.1016/0014-5793(91)81418-8;
Mayser W., Betz H., Schloss P.;
"Isolation of cDNAs encoding a novel member of the neurotransmitter
transporter gene family.";
FEBS Lett. 295:203-206(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Brain stem;
PubMed=1944572; DOI=10.1038/354066a0;
Blakely R.D., Berson H.E., Fremeau R.T. Jr., Caron M.G., Peek M.M.,
Prince H.K., Bardley C.C.;
"Cloning and expression of a functional serotonin transporter from rat
brain.";
Nature 354:66-70(1991).
[3]
SEQUENCE REVISION.
Blakely R.D.;
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1948036; DOI=10.1126/science.1948036;
Hoffman B.J., Mezey E., Brownstein M.J.;
"Cloning of a serotonin transporter affected by antidepressants.";
Science 254:579-580(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fawn hooded;
Gonzalez A.M., Smith A.P.L., Emery C.J., Higenbottam T.W.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[6]
MUTAGENESIS OF CYS-109 AND ILE-172, FUNCTION, SUBCELLULAR LOCATION,
AND SUBUNIT.
PubMed=10716733; DOI=10.1073/pnas.97.7.3106;
Kilic F., Rudnick G.;
"Oligomerization of serotonin transporter and its functional
consequences.";
Proc. Natl. Acad. Sci. U.S.A. 97:3106-3111(2000).
[7]
INTERACTION WITH STX1A, AND SUBCELLULAR LOCATION.
PubMed=11709063; DOI=10.1042/0300-5127:0290722;
Haase J., Killian A.M., Magnani F., Williams C.;
"Regulation of the serotonin transporter by interacting proteins.";
Biochem. Soc. Trans. 29:722-728(2001).
[8]
GLYCOSYLATION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-208
AND ASN-217, SUBUNIT, AND INTERACTION WITH MYH9.
PubMed=12944413; DOI=10.1074/jbc.M306360200;
Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C.,
Bene A., Kilic F.;
"Glycosyl modification facilitates homo- and hetero-oligomerization of
the serotonin transporter. A specific role for sialic acid residues.";
J. Biol. Chem. 278:43991-44000(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FILAMENTOUS
ACTIN.
PubMed=15627510; DOI=10.1016/j.neuint.2004.08.008;
Mochizuki H., Amano T., Seki T., Matsubayashi H., Mitsuhata C.,
Morita K., Kitayama S., Dohi T., Mishima H.K., Sakai N.;
"Role of C-terminal region in the functional regulation of rat
serotonin transporter (SERT).";
Neurochem. Int. 46:93-105(2005).
[10]
INTERACTION WITH SCAMP2, AND SUBCELLULAR LOCATION.
PubMed=16870614; DOI=10.1074/jbc.M602848200;
Mueller H.K., Wiborg O., Haase J.;
"Subcellular redistribution of the serotonin transporter by secretory
carrier membrane protein 2.";
J. Biol. Chem. 281:28901-28909(2006).
[11]
PHOSPHORYLATION AT THR-276.
PubMed=17310063; DOI=10.1074/jbc.M611353200;
Ramamoorthy S., Samuvel D.J., Buck E.R., Rudnick G., Jayanthi L.D.;
"Phosphorylation of threonine residue 276 is required for acute
regulation of serotonin transporter by cyclic GMP.";
J. Biol. Chem. 282:11639-11647(2007).
-!- FUNCTION: Serotonin transporter whose primary function in the
central nervous system involves the regulation of serotonergic
signaling via transport of serotonin molecules from the synaptic
cleft back into the pre-synaptic terminal for re-utilization.
Plays a key role in mediating regulation of the availability of
serotonin to other receptors of serotonergic systems. Terminates
the action of serotonin and recycles it in a sodium-dependent
manner. {ECO:0000269|PubMed:10716733, ECO:0000269|PubMed:12944413,
ECO:0000269|PubMed:15627510, ECO:0000269|PubMed:1944572,
ECO:0000269|PubMed:1948036}.
-!- SUBUNIT: Monomer or homooligomer. Interacts with TGFB1I1.
Interacts (via C-terminus) with VIM. Interacts with RAB4 (GTP-
bound form); the interaction retains transporter molecules
intracellularly. Interacts with SEC23A, SEC24C and PATJ. Interacts
with NOS1; the interaction may diminish the cell surface
localization of SERT in the brain and, correspondingly, reduce
serotonin reuptake (By similarity). Interacts (via C-terminus)
with SCAMP2; the interaction is direct and retains transporter
molecules intracellularly. Interacts with filamentous actin and
STX1A. Interacts (via sialylated form) with MYH9. {ECO:0000250,
ECO:0000269|PubMed:10716733, ECO:0000269|PubMed:11709063,
ECO:0000269|PubMed:12944413, ECO:0000269|PubMed:15627510,
ECO:0000269|PubMed:16870614}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11709063,
ECO:0000269|PubMed:12944413, ECO:0000269|PubMed:15627510,
ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:1944572,
ECO:0000269|PubMed:1948036}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q7K4Y6}. Endomembrane system
{ECO:0000269|PubMed:16870614}; Multi-pass membrane protein
{ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16870614};
Multi-pass membrane protein {ECO:0000255}. Note=Could be part of
recycling endosomes (PubMed:16870614). Density of transporter
molecules on the plasma membrane is itself regulated by STX1A
(PubMed:11709063). Density of transporter molecules on the plasma
membrane is also regulated by serotonin (By similarity).
{ECO:0000250|UniProtKB:P31645, ECO:0000269|PubMed:11709063,
ECO:0000269|PubMed:16870614}.
-!- PTM: Glycosylated; modification with sialylated N-glycans is a
requirement for transporters to associate with each other and to
function as homooligomeric forms. {ECO:0000269|PubMed:12944413}.
-!- PTM: Phosphorylation upon PKC stimulation modifies the SERT
distribution and density in the membrane, and diminishes the
uptake capacity (By similarity). Phosphorylation at Thr-276
increases 5-HT uptake and is required for cGMP-mediated SERT
regulation. {ECO:0000250, ECO:0000269|PubMed:17310063}.
-!- 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. SLC6A4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X63995; CAA45401.1; -; mRNA.
EMBL; X63253; CAA44913.1; -; mRNA.
EMBL; M79450; AAA42186.1; -; mRNA.
EMBL; Y11024; CAA71909.1; -; mRNA.
PIR; S19585; S19585.
PIR; S30604; S30604.
RefSeq; NP_037166.2; NM_013034.4.
RefSeq; XP_008766172.1; XM_008767950.2.
RefSeq; XP_017452530.1; XM_017597041.1.
RefSeq; XP_017452531.1; XM_017597042.1.
RefSeq; XP_017452532.1; XM_017597043.1.
UniGene; Rn.1663; -.
ProteinModelPortal; P31652; -.
SMR; P31652; -.
IntAct; P31652; 1.
STRING; 10116.ENSRNOP00000004717; -.
BindingDB; P31652; -.
ChEMBL; CHEMBL313; -.
GuidetoPHARMACOLOGY; 928; -.
iPTMnet; P31652; -.
SwissPalm; P31652; -.
PaxDb; P31652; -.
Ensembl; ENSRNOT00000004717; ENSRNOP00000004717; ENSRNOG00000003476.
GeneID; 25553; -.
KEGG; rno:25553; -.
CTD; 6532; -.
RGD; 3714; Slc6a4.
eggNOG; KOG3659; Eukaryota.
eggNOG; COG0733; LUCA.
GeneTree; ENSGT00760000118857; -.
HOGENOM; HOG000116406; -.
HOVERGEN; HBG071421; -.
InParanoid; P31652; -.
KO; K05037; -.
OMA; NMPAATF; -.
OrthoDB; EOG091G08PX; -.
PhylomeDB; P31652; -.
TreeFam; TF343812; -.
Reactome; R-RNO-380615; Serotonin clearance from the synaptic cleft.
PRO; PR:P31652; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000003476; -.
Genevisible; P31652; RN.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0019811; F:cocaine binding; IMP:RGD.
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; ISO:RGD.
GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
GO; GO:0050998; F:nitric-oxide synthase binding; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; IMP:RGD.
GO; GO:0017137; F:Rab GTPase binding; ISO:RGD.
GO; GO:0015222; F:serotonin transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005335; F:serotonin:sodium symporter activity; ISS:UniProtKB.
GO; GO:0017075; F:syntaxin-1 binding; IPI:UniProtKB.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
GO; GO:0071321; P:cellular response to cGMP; IDA:RGD.
GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0007623; P:circadian rhythm; IMP:RGD.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IBA:GO_Central.
GO; GO:0007626; P:locomotory behavior; NAS:RGD.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0015844; P:monoamine transport; ISO:RGD.
GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; IMP:RGD.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
GO; GO:0046621; P:negative regulation of organ growth; ISO:RGD.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IMP:RGD.
GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0014064; P:positive regulation of serotonin secretion; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; ISO:RGD.
GO; GO:0006837; P:serotonin transport; IDA:UniProtKB.
GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB.
GO; GO:0035176; P:social behavior; ISO:RGD.
GO; GO:0042713; P:sperm ejaculation; IMP:RGD.
GO; GO:0021794; P:thalamus development; ISO:RGD.
GO; GO:0042310; P:vasoconstriction; IMP:RGD.
InterPro; IPR000175; Na/ntran_symport.
InterPro; IPR013086; Na/ntran_symport_serotonin_N.
InterPro; IPR037272; SNS_sf.
PANTHER; PTHR11616; PTHR11616; 1.
Pfam; PF03491; 5HT_transport_N; 1.
Pfam; PF00209; SNF; 1.
PRINTS; PR01203; 5HTTRANSPORT.
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; Disulfide bond; Endosome;
Glycoprotein; Membrane; Metal-binding; Neurotransmitter transport;
Phosphoprotein; Reference proteome; Sodium; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 630 Sodium-dependent serotonin transporter.
/FTId=PRO_0000214760.
TOPO_DOM 1 87 Cytoplasmic. {ECO:0000305}.
TRANSMEM 88 112 Helical; Name=1.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 113 115 Extracellular. {ECO:0000305}.
TRANSMEM 116 135 Helical; Name=2.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 136 160 Cytoplasmic. {ECO:0000305}.
TRANSMEM 161 186 Helical; Name=3.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 187 252 Extracellular. {ECO:0000305}.
TRANSMEM 253 271 Helical; Name=4.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 272 277 Cytoplasmic. {ECO:0000305}.
TRANSMEM 278 297 Helical; Name=5.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 298 324 Extracellular. {ECO:0000305}.
TRANSMEM 325 347 Helical; Name=6.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 348 360 Cytoplasmic. {ECO:0000305}.
TRANSMEM 361 380 Helical; Name=7.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 381 421 Extracellular. {ECO:0000305}.
TRANSMEM 422 443 Helical; Name=8.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 444 463 Cytoplasmic. {ECO:0000305}.
TRANSMEM 464 483 Helical; Name=9.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 484 494 Extracellular. {ECO:0000305}.
TRANSMEM 495 516 Helical; Name=10.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 517 538 Cytoplasmic. {ECO:0000305}.
TRANSMEM 539 558 Helical; Name=11.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 559 574 Extracellular. {ECO:0000305}.
TRANSMEM 575 595 Helical; Name=12.
{ECO:0000250|UniProtKB:P31645}.
TOPO_DOM 596 630 Cytoplasmic. {ECO:0000305}.
REGION 611 630 Required for serotonin uptake activity.
{ECO:0000250|UniProtKB:P31645}.
REGION 616 624 Interaction with RAB4A. {ECO:0000250}.
METAL 94 94 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 96 96 Sodium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 97 97 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 101 101 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 336 336 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 368 368 Sodium 2. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 434 434 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 437 437 Sodium 1. {ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 438 438 Sodium 1. {ECO:0000250|UniProtKB:Q7K4Y6}.
MOD_RES 47 47 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31645}.
MOD_RES 142 142 Phosphotyrosine.
{ECO:0000250|UniProtKB:P31645}.
MOD_RES 276 276 Phosphothreonine.
{ECO:0000269|PubMed:17310063}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000250|UniProtKB:P31645,
ECO:0000255}.
MOD_RES 613 613 Phosphothreonine.
{ECO:0000250|UniProtKB:P31645,
ECO:0000255}.
MOD_RES 616 616 Phosphothreonine.
{ECO:0000250|UniProtKB:P31645,
ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:12944413}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:12944413}.
DISULFID 200 209 {ECO:0000250|UniProtKB:P31645}.
MUTAGEN 109 109 C->A: Cocaine is effective at blocking
transport. {ECO:0000269|PubMed:10716733}.
MUTAGEN 172 172 I->C: Cocaine is effective at blocking
transport. {ECO:0000269|PubMed:10716733}.
MUTAGEN 208 208 N->Q: No change in transport function.
Important decrease of transport function
and serotonin uptake function; when
associated with Q-217.
{ECO:0000269|PubMed:12944413}.
MUTAGEN 217 217 N->Q: No change in transport function.
Important decrease of transport function
and serotonin uptake function; when
associated with Q-208.
{ECO:0000269|PubMed:12944413}.
CONFLICT 415 415 A -> G (in Ref. 4; AAA42186).
{ECO:0000305}.
CONFLICT 533 536 PGWF -> GMV (in Ref. 4; AAA42186).
{ECO:0000305}.
CONFLICT 621 630 PCGDIRMNAV -> RVGHPHECCVTHPGRGHLFPATSLSSE
KPTGLLL (in Ref. 4; AAA42186).
{ECO:0000305}.
SEQUENCE 630 AA; 70172 MW; 44DA7C5888C403EE CRC64;
METTPLNSQK VLSECKDRED CQENGVLQKG VPTTADRAEP SQISNGYSAV PSTSAGDEAS
HSIPAATTTL VAEIRQGERE TWGKKMDFLL SVIGYAVDLG NIWRFPYICY QNGGGAFLLP
YTIMAIFGGI PLFYMELALG QYHRNGCISI WRKICPIFKG IGYAICIIAF YIASYYNTII
AWALYYLISS LTDRLPWTSC TNSWNTGNCT NYFAQDNITW TLHSTSPAEE FYLRHVLQIH
QSKGLQDLGT ISWQLTLCIV LIFTVIYFSI WKGVKTSGKV VWVTATFPYI VLSVLLVRGA
TLPGAWRGVV FYLKPNWQKL LETGVWVDAA AQIFFSLGPG FGVLLAFASY NKFNNNCYQD
ALVTSVVNCM TSFVSGFVIF TVLGYMAEMR NEDVSEVAKD AGPSLLFITY AEAIANMPAS
TFFAIIFFLM LITLGLDSTF AGLEGVITAV LDEFPHIWAK RREWFVLIVV ITCVLGSLLT
LTSGGAYVVT LLEEYATGPA VLTVALIEAV AVSWFYGITQ FCSDVKEMLG FSPGWFWRIC
WVAISPLFLL FIICSFLMSP PQLRLFQYNY PHWSIVLGYC IGMSSVICIP TYIIYRLIST
PGTLKERIIK SITPETPTEI PCGDIRMNAV


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Genprice Inc, Invoices and accounting
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