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

 SC6A4_HUMAN             Reviewed;         630 AA.
P31645; Q5EE02;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
22-NOV-2017, entry version 174.
RecName: Full=Sodium-dependent serotonin transporter;
Short=SERT {ECO:0000250|UniProtKB:P31652};
AltName: Full=5HT transporter;
Short=5HTT;
AltName: Full=Solute carrier family 6 member 4;
Name=SLC6A4; Synonyms=HTT, SERT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8452685; DOI=10.1007/BF01244919;
Lesch K.P., Wolozin B.L., Estler H.C., Murphy D.L., Riederer P.;
"Isolation of a cDNA encoding the human brain serotonin transporter.";
J. Neural Transm. 91:67-73(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7681602; DOI=10.1073/pnas.90.6.2542;
Ramamoorthy S., Bauman A.L., Moore K.R., Han H., Yang-Feng T.,
Chang A.S., Ganapathy V., Blakely R.D.;
"Antidepressant- and cocaine-sensitive human serotonin transporter:
molecular cloning, expression, and chromosomal localization.";
Proc. Natl. Acad. Sci. U.S.A. 90:2542-2546(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Platelet;
PubMed=7684072; DOI=10.1111/j.1471-4159.1993.tb03522.x;
Lesch K.P., Wolozin B.L., Murphy D.L., Reiderer P.;
"Primary structure of the human platelet serotonin uptake site:
identity with the brain serotonin transporter.";
J. Neurochem. 60:2319-2322(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16601320;
Iceta R., Mesonero J.E., Aramayona J.J., Alcalde A.I.;
"Molecular characterization and intracellular regulation of the human
serotonin transporter in Caco-2 cells.";
J. Physiol. Pharmacol. 57:119-130(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
TISSUE=Placenta;
Bradley C.C., Blakely R.D.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-317 (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
INTERACTION WITH TGFB1I1.
PubMed=16803896; DOI=10.1074/jbc.M603877200;
Carneiro A.M.D., Blakely R.D.;
"Serotonin-, protein kinase C-, and Hic-5-associated redistribution of
the platelet serotonin transporter.";
J. Biol. Chem. 281:24769-24780(2006).
[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]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17506858; DOI=10.1111/j.1471-4159.2007.04542.x;
Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L.,
Kilic F.;
"Plasma serotonin levels and the platelet serotonin transporter.";
J. Neurochem. 102:206-215(2007).
[12]
PHOSPHORYLATION AT THR-276, AND VARIANT VAL-425.
PubMed=17913921; DOI=10.1523/JNEUROSCI.0034-07.2007;
Zhang Y.W., Gesmonde J., Ramamoorthy S., Rudnick G.;
"Serotonin transporter phosphorylation by cGMP-dependent protein
kinase is altered by a mutation associated with obsessive compulsive
disorder.";
J. Neurosci. 27:10878-10886(2007).
[13]
FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, AND INDUCTION
BY SEROTONIN.
PubMed=18227069; DOI=10.1074/jbc.M706367200;
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R.,
Lupashin V.V., van der Sluijs P., Kilic F.;
"Serotonin transamidates Rab4 and facilitates its binding to the C
terminus of serotonin transporter.";
J. Biol. Chem. 283:9388-9398(2008).
[14]
FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY
SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, AND
PHOSPHORYLATION AT SER-611; THR-613 AND THR-616.
PubMed=19270731; DOI=10.1371/journal.pone.0004730;
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S.,
Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D.,
Kilic F.;
"The cellular distribution of serotonin transporter is impeded on
serotonin-altered vimentin network.";
PLoS ONE 4:E4730-E4730(2009).
[15]
PHOSPHORYLATION AT TYR-47 AND TYR-142.
PubMed=21992875; DOI=10.1124/mol.111.073171;
Annamalai B., Mannangatti P., Arapulisamy O., Shippenberg T.S.,
Jayanthi L.D., Ramamoorthy S.;
"Tyrosine phosphorylation of the human serotonin transporter: a role
in the transporter stability and function.";
Mol. Pharmacol. 81:73-85(2012).
[16]
X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 76-618 IN COMPLEXES WITH
SODIUM IONS AND THE ANTIDEPRESSANTS CITALOPRAM AND PAROXETINE,
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-208 AND
ASN-217, AND DISULFIDE BONDS.
PubMed=27049939; DOI=10.1038/nature17629;
Coleman J.A., Green E.M., Gouaux E.;
"X-ray structures and mechanism of the human serotonin transporter.";
Nature 532:334-339(2016).
[17]
VARIANTS ALA-56 AND ASN-605.
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]
VARIANT VAL-425.
PubMed=14593431; DOI=10.1038/sj.mp.4001365;
Ozaki N., Goldman D., Kaye W.H., Plotnicov K., Greenberg B.D.,
Lappalainen J., Rudnick G., Murphy D.L.;
"Serotonin transporter missense mutation associated with a complex
neuropsychiatric phenotype.";
Mol. Psychiatry 8:933-936(2003).
[20]
CHARACTERIZATION OF VARIANT VAL-425.
PubMed=12869649; DOI=10.1124/mol.64.2.440;
Kilic F., Murphy D.L., Rudnick G.;
"A human serotonin transporter mutation causes constitutive activation
of transport activity.";
Mol. Pharmacol. 64:440-446(2003).
[21]
POLYMORPHISM IN THE PROMOTER REGION.
PubMed=12869766; DOI=10.1126/science.1083968;
Caspi A., Sugden K., Moffitt T.E., Taylor A., Craig I.W.,
Harrington H., McClay J., Mill J., Martin J., Braithwaite A.,
Poulton R.;
"Influence of life stress on depression: moderation by a polymorphism
in the 5-HTT gene.";
Science 301:386-389(2003).
[22]
INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
PubMed=15635638; DOI=10.1002/ajmg.b.30132;
Feinn R., Nellissery M., Kranzler H.R.;
"Meta-analysis of the association of a functional serotonin
transporter promoter polymorphism with alcohol dependence.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 133:79-84(2005).
-!- 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:17506858, ECO:0000269|PubMed:18227069,
ECO:0000269|PubMed:19270731, ECO:0000269|PubMed:27049939}.
-!- SUBUNIT: Monomer or homooligomer (By similarity). Interacts with
TGFB1I1. Interacts (via sialylated form) with MYH9. 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. Interacts with
filamentous actin and STX1A (By similarity). Interacts (via C-
terminus) with VIM. Interacts (via C-terminus) with SCAMP2; the
interaction is direct and retains transporter molecules
intracellularly. Interacts with RAB4 (GTP-bound form); the
interaction retains transporter molecules intracellularly.
{ECO:0000250, ECO:0000269|PubMed:16803896,
ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:18227069,
ECO:0000269|PubMed:19270731}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16870614,
ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:18227069,
ECO:0000269|PubMed:19270731, ECO:0000269|PubMed:27049939}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6,
ECO:0000269|PubMed:27049939}. Endomembrane system
{ECO:0000269|PubMed:16870614}; Multi-pass membrane protein
{ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16870614,
ECO:0000269|PubMed:18227069}; Multi-pass membrane protein
{ECO:0000255}. Note=Could be part of recycling endosomes
(PubMed:18227069, PubMed:16870614). Density of transporter
molecules on the plasma membrane is itself regulated by STX1A (By
similarity). Density of transporter molecules on the plasma
membrane is also regulated by serotonin (PubMed:17506858)
(PubMed:18227069). {ECO:0000250|UniProtKB:P31652,
ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:17506858,
ECO:0000269|PubMed:18227069}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31645-1; Sequence=Displayed;
Name=2;
IsoId=P31645-2; Sequence=VSP_046553;
-!- TISSUE SPECIFICITY: Expressed in platelets (at protein level).
{ECO:0000269|PubMed:17506858}.
-!- INDUCTION: Down-regulated when plasma serotonin is elevated.
{ECO:0000269|PubMed:18227069, ECO:0000269|PubMed:19270731}.
-!- PTM: Glycosylated; modification with sialylated N-glycans is a
requirement for transporters to associate with each other and to
function as homooligomeric forms. {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is
required for cGMP-mediated SERT regulation. Phosphorylation upon
PKC stimulation modifies the SERT distribution and density in the
membrane, and diminishes the uptake capacity.
{ECO:0000269|PubMed:17913921, ECO:0000269|PubMed:19270731,
ECO:0000269|PubMed:21992875}.
-!- POLYMORPHISM: A polymorphism in the promoter region (5-HTT gene-
linked polymorphic region, 5-HTTLPR) is located approximately 1 kb
upstream of the transcription initiation site and is composed of
16 repeat elements. The polymorphism consists of a 44-bp insertion
or deletion involving repeat elements 6 to 8. The short allele is
associated with lower transcriptional efficiency of the promoter
compared with the long allele. Over half of the Caucasian
population has a short allele. Individuals with one or two copies
of the short allele exhibit more depressive symptoms, diagnosable
depression and suicidality in relation to stressful life events
than individuals homozygous for the long allele.
{ECO:0000269|PubMed:12869766}.
-!- POLYMORPHISM: The polymorphism Val-425 seems to be linked to a
susceptibility to obsessive-compulsive disorder (OCD)
[MIM:164230]. {ECO:0000269|PubMed:12869649,
ECO:0000269|PubMed:14593431, ECO:0000269|PubMed:17913921}.
-!- POLYMORPHISM: Genetic variations in SLC6A4 determine the genetic
susceptibility to alcoholism [MIM:103780].
{ECO:0000269|PubMed:15635638}.
-!- 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}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=SLC6A4";
-!- WEB RESOURCE: Name=Wikipedia; Note=Serotonin transporter entry;
URL="https://en.wikipedia.org/wiki/Serotonin_transporter";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Love, love, love...
-Issue 123 of November 2010;
URL="https://web.expasy.org/spotlight/back_issues/123";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/slc6a4/";
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EMBL; X70697; CAA50029.1; -; mRNA.
EMBL; L05568; AAA35492.1; -; mRNA.
EMBL; AY902473; AAW80933.1; -; mRNA.
EMBL; EU099989; ABV02581.1; -; Genomic_DNA.
EMBL; BC069484; AAH69484.1; -; mRNA.
EMBL; U79746; AAB93475.1; -; Genomic_DNA.
EMBL; AK308014; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS11256.1; -. [P31645-1]
PIR; A47398; A47398.
RefSeq; NP_001036.1; NM_001045.5. [P31645-1]
UniGene; Hs.134662; -.
UniGene; Hs.29792; -.
PDB; 5I6X; X-ray; 3.14 A; A=76-618.
PDB; 5I6Z; X-ray; 4.53 A; A=76-618.
PDB; 5I71; X-ray; 3.15 A; A=76-618.
PDB; 5I73; X-ray; 3.24 A; A=76-618.
PDB; 5I74; X-ray; 3.40 A; A=76-618.
PDB; 5I75; X-ray; 3.49 A; A=76-618.
PDBsum; 5I6X; -.
PDBsum; 5I6Z; -.
PDBsum; 5I71; -.
PDBsum; 5I73; -.
PDBsum; 5I74; -.
PDBsum; 5I75; -.
ProteinModelPortal; P31645; -.
SMR; P31645; -.
BioGrid; 112423; 5.
IntAct; P31645; 2.
MINT; MINT-577123; -.
STRING; 9606.ENSP00000261707; -.
BindingDB; P31645; -.
ChEMBL; CHEMBL228; -.
DrugBank; DB01472; 4-Methoxyamphetamine.
DrugBank; DB04836; Amineptine.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00543; Amoxapine.
DrugBank; DB00182; Amphetamine.
DrugBank; DB00289; Atomoxetine.
DrugBank; DB04889; Bicifadine.
DrugBank; DB09016; Butriptyline.
DrugBank; DB01114; Chlorphenamine.
DrugBank; DB00215; Citalopram.
DrugBank; DB01242; Clomipramine.
DrugBank; DB00907; Cocaine.
DrugBank; DB05688; CRx-119.
DrugBank; DB01151; Desipramine.
DrugBank; DB06700; Desvenlafaxine.
DrugBank; DB01191; Dexfenfluramine.
DrugBank; DB06701; Dexmethylphenidate.
DrugBank; DB00514; Dextromethorphan.
DrugBank; DB00988; Dopamine.
DrugBank; DB01142; Doxepin.
DrugBank; DB00476; Duloxetine.
DrugBank; DB01363; Ephedra.
DrugBank; DB01175; Escitalopram.
DrugBank; DB00574; Fenfluramine.
DrugBank; DB00472; Fluoxetine.
DrugBank; DB00176; Fluvoxamine.
DrugBank; DB00458; Imipramine.
DrugBank; DB08918; Levomilnacipran.
DrugBank; DB00408; Loxapine.
DrugBank; DB00579; Mazindol.
DrugBank; DB01577; Methamphetamine.
DrugBank; DB09543; Methyl salicylate.
DrugBank; DB00422; Methylphenidate.
DrugBank; DB06148; Mianserin.
DrugBank; DB04896; Milnacipran.
DrugBank; DB00805; Minaprine.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01442; MMDA.
DrugBank; DB01149; Nefazodone.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB05422; OPC-14523.
DrugBank; DB00715; Paroxetine.
DrugBank; DB00454; Pethidine.
DrugBank; DB00191; Phentermine.
DrugBank; DB00344; Protriptyline.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB01104; Sertraline.
DrugBank; DB01105; Sibutramine.
DrugBank; DB06204; Tapentadol.
DrugBank; DB01079; Tegaserod.
DrugBank; DB00193; Tramadol.
DrugBank; DB00656; Trazodone.
DrugBank; DB00726; Trimipramine.
DrugBank; DB00285; Venlafaxine.
DrugBank; DB00661; Verapamil.
DrugBank; DB06684; Vilazodone.
DrugBank; DB09068; Vortioxetine.
DrugBank; DB04832; Zimelidine.
GuidetoPHARMACOLOGY; 928; -.
TCDB; 2.A.22.1.1; the neurotransmitter:sodium symporter (nss) family.
iPTMnet; P31645; -.
PhosphoSitePlus; P31645; -.
DMDM; 400630; -.
PaxDb; P31645; -.
PeptideAtlas; P31645; -.
PRIDE; P31645; -.
Ensembl; ENST00000261707; ENSP00000261707; ENSG00000108576. [P31645-1]
Ensembl; ENST00000401766; ENSP00000385822; ENSG00000108576. [P31645-1]
GeneID; 6532; -.
KEGG; hsa:6532; -.
UCSC; uc002hey.6; human. [P31645-1]
CTD; 6532; -.
DisGeNET; 6532; -.
EuPathDB; HostDB:ENSG00000108576.9; -.
GeneCards; SLC6A4; -.
HGNC; HGNC:11050; SLC6A4.
HPA; HPA054723; -.
HPA; HPA074728; -.
MalaCards; SLC6A4; -.
MIM; 103780; phenotype.
MIM; 164230; phenotype.
MIM; 182138; gene.
neXtProt; NX_P31645; -.
OpenTargets; ENSG00000108576; -.
PharmGKB; PA312; -.
eggNOG; KOG3659; Eukaryota.
eggNOG; COG0733; LUCA.
GeneTree; ENSGT00760000118857; -.
HOGENOM; HOG000116406; -.
HOVERGEN; HBG071421; -.
InParanoid; P31645; -.
KO; K05037; -.
OMA; NMPAATF; -.
OrthoDB; EOG091G08PX; -.
PhylomeDB; P31645; -.
TreeFam; TF343812; -.
Reactome; R-HSA-380615; Serotonin clearance from the synaptic cleft.
SIGNOR; P31645; -.
GeneWiki; Serotonin_transporter; -.
GenomeRNAi; 6532; -.
PRO; PR:P31645; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108576; -.
CleanEx; HS_HTT; -.
CleanEx; HS_SLC6A4; -.
ExpressionAtlas; P31645; baseline and differential.
Genevisible; P31645; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0019811; F:cocaine binding; IEA:Ensembl.
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:0017022; F:myosin binding; IEA:Ensembl.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
GO; GO:0015222; F:serotonin transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005335; F:serotonin:sodium symporter activity; IDA:UniProtKB.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
GO; GO:0071321; P:cellular response to cGMP; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IBA:GO_Central.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0015844; P:monoamine transport; IDA:MGI.
GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0046621; P:negative regulation of organ growth; ISS:BHF-UCL.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:Reactome.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0014064; P:positive regulation of serotonin secretion; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
GO; GO:0006837; P:serotonin transport; IDA:UniProtKB.
GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0042713; P:sperm ejaculation; IEA:Ensembl.
GO; GO:0021794; P:thalamus development; IMP:UniProtKB.
GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endosome; Glycoprotein; Membrane; Metal-binding;
Neurotransmitter transport; Phosphoprotein; Polymorphism;
Reference proteome; Sodium; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 630 Sodium-dependent serotonin transporter.
/FTId=PRO_0000214757.
TOPO_DOM 1 87 Cytoplasmic. {ECO:0000305}.
TRANSMEM 88 112 Helical; Name=1.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 113 115 Extracellular. {ECO:0000305}.
TRANSMEM 116 135 Helical; Name=2.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 136 160 Cytoplasmic. {ECO:0000305}.
TRANSMEM 161 186 Helical; Name=3.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 187 252 Extracellular. {ECO:0000305}.
TRANSMEM 253 271 Helical; Name=4.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 272 277 Cytoplasmic. {ECO:0000305}.
TRANSMEM 278 297 Helical; Name=5.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 298 324 Extracellular. {ECO:0000305}.
TRANSMEM 325 347 Helical; Name=6.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 348 360 Cytoplasmic. {ECO:0000305}.
TRANSMEM 361 380 Helical; Name=7.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 381 421 Extracellular. {ECO:0000305}.
TRANSMEM 422 443 Helical; Name=8.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 444 463 Cytoplasmic. {ECO:0000305}.
TRANSMEM 464 483 Helical; Name=9.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 484 494 Extracellular. {ECO:0000305}.
TRANSMEM 495 516 Helical; Name=10.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 517 538 Cytoplasmic. {ECO:0000305}.
TRANSMEM 539 558 Helical; Name=11.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 559 574 Extracellular. {ECO:0000305}.
TRANSMEM 575 595 Helical; Name=12.
{ECO:0000269|PubMed:27049939}.
TOPO_DOM 596 630 Cytoplasmic. {ECO:0000305}.
REGION 611 630 Required for serotonin uptake activity.
{ECO:0000269|PubMed:19270731}.
REGION 616 624 Interaction with RAB4A.
METAL 94 94 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 96 96 Sodium 2; via carbonyl oxygen.
{ECO:0000305|PubMed:27049939}.
METAL 97 97 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q7K4Y6}.
METAL 101 101 Sodium 2. {ECO:0000305|PubMed:27049939}.
METAL 336 336 Sodium 2. {ECO:0000305|PubMed:27049939}.
METAL 368 368 Sodium 2. {ECO:0000305|PubMed:27049939}.
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:0000269|PubMed:21992875}.
MOD_RES 142 142 Phosphotyrosine.
{ECO:0000269|PubMed:21992875}.
MOD_RES 276 276 Phosphothreonine; by PKG.
{ECO:0000269|PubMed:17913921}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000269|PubMed:19270731}.
MOD_RES 613 613 Phosphothreonine.
{ECO:0000269|PubMed:19270731}.
MOD_RES 616 616 Phosphothreonine.
{ECO:0000269|PubMed:19270731}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27049939}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27049939}.
DISULFID 200 209 {ECO:0000244|PDB:5I6X,
ECO:0000244|PDB:5I6Z,
ECO:0000244|PDB:5I71,
ECO:0000244|PDB:5I73,
ECO:0000244|PDB:5I74,
ECO:0000244|PDB:5I75}.
VAR_SEQ 1 1 M -> MSQSRRVNPDDRELGGDLQIQAPRDQLGSLADGHQC
HLLTSRM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046553.
VARIANT 56 56 G -> A (in dbSNP:rs6355).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014181.
VARIANT 201 201 K -> N (in dbSNP:rs2228673).
/FTId=VAR_029158.
VARIANT 425 425 I -> L (in dbSNP:rs28914832).
/FTId=VAR_036788.
VARIANT 425 425 I -> V (polymorphism linked with
susceptibility to obsessive-compulsive
disorder; increased serotonin transport
capacity; dbSNP:rs28914832).
{ECO:0000269|PubMed:12869649,
ECO:0000269|PubMed:14593431,
ECO:0000269|PubMed:17913921}.
/FTId=VAR_026751.
VARIANT 465 465 F -> L (in dbSNP:rs28914833).
/FTId=VAR_036789.
VARIANT 550 550 L -> V (in dbSNP:rs28914834).
/FTId=VAR_036790.
VARIANT 605 605 K -> N (in dbSNP:rs6352).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014182.
MUTAGEN 611 611 S->A: Loss of 10 % of serotonin uptake
activity. Loss of 5 % of serotonin uptake
activity; when associated with A-613 and
A-616. {ECO:0000269|PubMed:19270731}.
MUTAGEN 611 611 S->D: Loss of 61 % of serotonin uptake
activity. Loss of 95 % of serotonin
uptake activity and lack of association
between VIM and the plasma membrane; when
associated with D-613 and D-616.
{ECO:0000269|PubMed:19270731}.
MUTAGEN 613 613 T->A: Loss of 26 % of serotonin uptake
activity. Loss of 5 % of serotonin uptake
activity; when associated with A-611 and
A-616. {ECO:0000269|PubMed:19270731}.
MUTAGEN 613 613 T->D: Loss of 26 % of serotonin uptake
activity. Loss of 95 % of serotonin
uptake activity and lack of association
between VIM and the plasma membrane; when
associated with D-611 and D-616.
{ECO:0000269|PubMed:19270731}.
MUTAGEN 616 616 T->A: No change. Loss of 5 % of serotonin
uptake activity; when associated with A-
611 and A-613.
{ECO:0000269|PubMed:19270731}.
MUTAGEN 616 616 T->D: No change. Loss of 95 % of
serotonin uptake activity and lack of
association between VIM and the plasma
membrane; when associated with D-611 and
D-613. {ECO:0000269|PubMed:19270731}.
HELIX 85 96 {ECO:0000244|PDB:5I6X}.
HELIX 99 111 {ECO:0000244|PDB:5I6X}.
HELIX 114 117 {ECO:0000244|PDB:5I6X}.
HELIX 118 127 {ECO:0000244|PDB:5I6X}.
HELIX 129 143 {ECO:0000244|PDB:5I6X}.
HELIX 149 152 {ECO:0000244|PDB:5I6X}.
HELIX 156 159 {ECO:0000244|PDB:5I6X}.
HELIX 160 173 {ECO:0000244|PDB:5I6X}.
HELIX 176 188 {ECO:0000244|PDB:5I6X}.
HELIX 189 191 {ECO:0000244|PDB:5I74}.
STRAND 192 194 {ECO:0000244|PDB:5I6X}.
TURN 196 198 {ECO:0000244|PDB:5I6X}.
STRAND 202 204 {ECO:0000244|PDB:5I6X}.
STRAND 207 209 {ECO:0000244|PDB:5I6X}.
STRAND 212 214 {ECO:0000244|PDB:5I6X}.
HELIX 227 234 {ECO:0000244|PDB:5I6X}.
TURN 235 237 {ECO:0000244|PDB:5I74}.
HELIX 239 241 {ECO:0000244|PDB:5I6X}.
STRAND 244 247 {ECO:0000244|PDB:5I6X}.
HELIX 253 270 {ECO:0000244|PDB:5I6X}.
HELIX 274 284 {ECO:0000244|PDB:5I6X}.
HELIX 287 300 {ECO:0000244|PDB:5I6X}.
TURN 303 305 {ECO:0000244|PDB:5I6X}.
HELIX 306 313 {ECO:0000244|PDB:5I6X}.
HELIX 317 321 {ECO:0000244|PDB:5I6X}.
HELIX 323 337 {ECO:0000244|PDB:5I6X}.
STRAND 340 342 {ECO:0000244|PDB:5I71}.
HELIX 343 349 {ECO:0000244|PDB:5I6X}.
STRAND 353 355 {ECO:0000244|PDB:5I6X}.
HELIX 358 389 {ECO:0000244|PDB:5I6X}.
HELIX 396 398 {ECO:0000244|PDB:5I6X}.
HELIX 403 407 {ECO:0000244|PDB:5I6X}.
HELIX 409 415 {ECO:0000244|PDB:5I6X}.
HELIX 420 453 {ECO:0000244|PDB:5I6X}.
HELIX 462 477 {ECO:0000244|PDB:5I6X}.
TURN 478 480 {ECO:0000244|PDB:5I6X}.
HELIX 485 494 {ECO:0000244|PDB:5I6X}.
HELIX 497 513 {ECO:0000244|PDB:5I6X}.
TURN 514 517 {ECO:0000244|PDB:5I6X}.
HELIX 518 528 {ECO:0000244|PDB:5I6X}.
STRAND 529 531 {ECO:0000244|PDB:5I73}.
HELIX 535 542 {ECO:0000244|PDB:5I6X}.
HELIX 544 558 {ECO:0000244|PDB:5I6X}.
HELIX 574 583 {ECO:0000244|PDB:5I6X}.
TURN 584 587 {ECO:0000244|PDB:5I6X}.
HELIX 588 599 {ECO:0000244|PDB:5I6X}.
HELIX 604 612 {ECO:0000244|PDB:5I6X}.
SEQUENCE 630 AA; 70325 MW; 0EB535B0A579BDA2 CRC64;
METTPLNSQK QLSACEDGED CQENGVLQKV VPTPGDKVES GQISNGYSAV PSPGAGDDTR
HSIPATTTTL VAELHQGERE TWGKKVDFLL SVIGYAVDLG NVWRFPYICY QNGGGAFLLP
YTIMAIFGGI PLFYMELALG QYHRNGCISI WRKICPIFKG IGYAICIIAF YIASYYNTIM
AWALYYLISS FTDQLPWTSC KNSWNTGNCT NYFSEDNITW TLHSTSPAEE FYTRHVLQIH
RSKGLQDLGG ISWQLALCIM LIFTVIYFSI WKGVKTSGKV VWVTATFPYI ILSVLLVRGA
TLPGAWRGVL FYLKPNWQKL LETGVWIDAA AQIFFSLGPG FGVLLAFASY NKFNNNCYQD
ALVTSVVNCM TSFVSGFVIF TVLGYMAEMR NEDVSEVAKD AGPSLLFITY AEAIANMPAS
TFFAIIFFLM LITLGLDSTF AGLEGVITAV LDEFPHVWAK RRERFVLAVV ITCFFGSLVT
LTFGGAYVVK LLEEYATGPA VLTVALIEAV AVSWFYGITQ FCRDVKEMLG FSPGWFWRIC
WVAISPLFLL FIICSFLMSP PQLRLFQYNY PYWSIILGYC IGTSSFICIP TYIAYRLIIT
PGTFKERIIK SITPETPTEI PCGDIRLNAV


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