SC6A4_HUMAN
ID SC6A4_HUMAN Reviewed; 630 AA.
AC P31645; Q5EE02;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Sodium-dependent serotonin transporter;
DE Short=SERT {ECO:0000250|UniProtKB:P31652};
DE AltName: Full=5HT transporter;
DE Short=5HTT;
DE AltName: Full=Solute carrier family 6 member 4;
GN Name=SLC6A4; Synonyms=HTT, SERT;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8452685; DOI=10.1007/bf01244919;
RA Lesch K.P., Wolozin B.L., Estler H.C., Murphy D.L., Riederer P.;
RT "Isolation of a cDNA encoding the human brain serotonin transporter.";
RL J. Neural Transm. 91:67-73(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7681602; DOI=10.1073/pnas.90.6.2542;
RA Ramamoorthy S., Bauman A.L., Moore K.R., Han H., Yang-Feng T., Chang A.S.,
RA Ganapathy V., Blakely R.D.;
RT "Antidepressant- and cocaine-sensitive human serotonin transporter:
RT molecular cloning, expression, and chromosomal localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2542-2546(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=7684072; DOI=10.1111/j.1471-4159.1993.tb03522.x;
RA Lesch K.P., Wolozin B.L., Murphy D.L., Reiderer P.;
RT "Primary structure of the human platelet serotonin uptake site: identity
RT with the brain serotonin transporter.";
RL J. Neurochem. 60:2319-2322(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16601320;
RA Iceta R., Mesonero J.E., Aramayona J.J., Alcalde A.I.;
RT "Molecular characterization and intracellular regulation of the human
RT serotonin transporter in Caco-2 cells.";
RL J. Physiol. Pharmacol. 57:119-130(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC TISSUE=Placenta;
RA Bradley C.C., Blakely R.D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-317 (ISOFORM 2).
RC TISSUE=Lung;
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 [9]
RP INTERACTION WITH TGFB1I1.
RX PubMed=16803896; DOI=10.1074/jbc.m603877200;
RA Carneiro A.M.D., Blakely R.D.;
RT "Serotonin-, protein kinase C-, and Hic-5-associated redistribution of the
RT platelet serotonin transporter.";
RL J. Biol. Chem. 281:24769-24780(2006).
RN [10]
RP INTERACTION WITH SCAMP2, AND SUBCELLULAR LOCATION.
RX PubMed=16870614; DOI=10.1074/jbc.m602848200;
RA Mueller H.K., Wiborg O., Haase J.;
RT "Subcellular redistribution of the serotonin transporter by secretory
RT carrier membrane protein 2.";
RL J. Biol. Chem. 281:28901-28909(2006).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17506858; DOI=10.1111/j.1471-4159.2007.04542.x;
RA Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L.,
RA Kilic F.;
RT "Plasma serotonin levels and the platelet serotonin transporter.";
RL J. Neurochem. 102:206-215(2007).
RN [12]
RP PHOSPHORYLATION AT THR-276, AND VARIANT VAL-425.
RX PubMed=17913921; DOI=10.1523/jneurosci.0034-07.2007;
RA Zhang Y.W., Gesmonde J., Ramamoorthy S., Rudnick G.;
RT "Serotonin transporter phosphorylation by cGMP-dependent protein kinase is
RT altered by a mutation associated with obsessive compulsive disorder.";
RL J. Neurosci. 27:10878-10886(2007).
RN [13]
RP RETRACTED PAPER.
RX PubMed=18227069; DOI=10.1074/jbc.m706367200;
RA Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V.,
RA van der Sluijs P., Kilic F.;
RT "Serotonin transamidates Rab4 and facilitates its binding to the C terminus
RT of serotonin transporter.";
RL J. Biol. Chem. 283:9388-9398(2008).
RN [14]
RP RETRACTION NOTICE OF PUBMED:18227069.
RX PubMed=31201246; DOI=10.1074/jbc.w119.009467;
RA Ahmed B.A., Jeffus B.C., Bukhari S.I.A., Harney J.T., Unal R.,
RA Lupashin V.V., van der Sluijs P., Kilic F.;
RL J. Biol. Chem. 294:9658-9658(2019).
RN [15]
RP RETRACTED PAPER.
RX PubMed=19270731; DOI=10.1371/journal.pone.0004730;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E.,
RA Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.;
RT "The cellular distribution of serotonin transporter is impeded on
RT serotonin-altered vimentin network.";
RL PLoS ONE 4:E4730-E4730(2009).
RN [16]
RP RETRACTION NOTICE OF PUBMED:19270731.
RX PubMed=30707744; DOI=10.1371/journal.pone.0211966;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E.,
RA Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.;
RT "Retraction: The Cellular Distribution of Serotonin Transporter Is Impeded
RT on Serotonin-Altered Vimentin Network.";
RL PLoS ONE 14:e0211966-e0211966(2019).
RN [17]
RP PHOSPHORYLATION AT TYR-47 AND TYR-142.
RX PubMed=21992875; DOI=10.1124/mol.111.073171;
RA Annamalai B., Mannangatti P., Arapulisamy O., Shippenberg T.S.,
RA Jayanthi L.D., Ramamoorthy S.;
RT "Tyrosine phosphorylation of the human serotonin transporter: a role in the
RT transporter stability and function.";
RL Mol. Pharmacol. 81:73-85(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 76-618 IN COMPLEXES WITH SODIUM
RP IONS AND THE ANTIDEPRESSANTS CITALOPRAM AND PAROXETINE, FUNCTION,
RP SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-208 AND ASN-217, AND
RP DISULFIDE BONDS.
RX PubMed=27049939; DOI=10.1038/nature17629;
RA Coleman J.A., Green E.M., Gouaux E.;
RT "X-ray structures and mechanism of the human serotonin transporter.";
RL Nature 532:334-339(2016).
RN [19]
RP VARIANTS ALA-56 AND ASN-605.
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 [20]
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).
RN [21]
RP VARIANT VAL-425.
RX PubMed=14593431; DOI=10.1038/sj.mp.4001365;
RA Ozaki N., Goldman D., Kaye W.H., Plotnicov K., Greenberg B.D.,
RA Lappalainen J., Rudnick G., Murphy D.L.;
RT "Serotonin transporter missense mutation associated with a complex
RT neuropsychiatric phenotype.";
RL Mol. Psychiatry 8:933-936(2003).
RN [22]
RP CHARACTERIZATION OF VARIANT VAL-425.
RX PubMed=12869649; DOI=10.1124/mol.64.2.440;
RA Kilic F., Murphy D.L., Rudnick G.;
RT "A human serotonin transporter mutation causes constitutive activation of
RT transport activity.";
RL Mol. Pharmacol. 64:440-446(2003).
RN [23]
RP POLYMORPHISM IN THE PROMOTER REGION.
RX PubMed=12869766; DOI=10.1126/science.1083968;
RA Caspi A., Sugden K., Moffitt T.E., Taylor A., Craig I.W., Harrington H.,
RA McClay J., Mill J., Martin J., Braithwaite A., Poulton R.;
RT "Influence of life stress on depression: moderation by a polymorphism in
RT the 5-HTT gene.";
RL Science 301:386-389(2003).
RN [24]
RP POLYMORPHISM IN THE PROMOTER REGION, AND INVOLVEMENT IN SUSCEPTIBILITY TO
RP ANXIETY.
RX PubMed=15108187; DOI=10.1002/ajmg.b.20158;
RA Sen S., Burmeister M., Ghosh D.;
RT "Meta-analysis of the association between a serotonin transporter promoter
RT polymorphism (5-HTTLPR) and anxiety-related personality traits.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 127B:85-89(2004).
RN [25]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
RX PubMed=15635638; DOI=10.1002/ajmg.b.30132;
RA Feinn R., Nellissery M., Kranzler H.R.;
RT "Meta-analysis of the association of a functional serotonin transporter
RT promoter polymorphism with alcohol dependence.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 133:79-84(2005).
CC -!- FUNCTION: Serotonin transporter whose primary function in the central
CC nervous system involves the regulation of serotonergic signaling via
CC transport of serotonin molecules from the synaptic cleft back into the
CC pre-synaptic terminal for re-utilization. Plays a key role in mediating
CC regulation of the availability of serotonin to other receptors of
CC serotonergic systems. Terminates the action of serotonin and recycles
CC it in a sodium-dependent manner. {ECO:0000269|PubMed:17506858,
CC ECO:0000269|PubMed:27049939}.
CC -!- SUBUNIT: Monomer or homooligomer (By similarity). Interacts with
CC TGFB1I1 (PubMed:16803896). Interacts with SEC23A, SEC24C and PATJ.
CC Interacts with NOS1; the interaction may diminish the cell surface
CC localization of SERT in the brain and, correspondingly, reduce
CC serotonin reuptake. Interacts with filamentous actin and STX1A (By
CC similarity). Interacts (via C-terminus) with SCAMP2; the interaction is
CC direct and retains transporter molecules intracellularly
CC (PubMed:16870614). Interacts with ITGAV:ITGB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q60857, ECO:0000269|PubMed:16803896,
CC ECO:0000269|PubMed:16870614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16870614,
CC ECO:0000269|PubMed:17506858, ECO:0000269|PubMed:27049939}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q7K4Y6,
CC ECO:0000269|PubMed:27049939}. Endomembrane system
CC {ECO:0000269|PubMed:16870614}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:16870614}; Multi-
CC pass membrane protein {ECO:0000255}. Synapse
CC {ECO:0000250|UniProtKB:Q60857}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q60857}. Note=Could be part of recycling
CC endosomes (PubMed:16870614). Density of transporter molecules on the
CC plasma membrane is itself regulated by STX1A (By similarity). Density
CC of transporter molecules on the plasma membrane is also regulated by
CC serotonin (PubMed:17506858). Density of transporter molecules seems to
CC be modulated by ITGAV:ITGB3 (By similarity).
CC {ECO:0000250|UniProtKB:P31652, ECO:0000250|UniProtKB:Q60857,
CC ECO:0000269|PubMed:16870614, ECO:0000269|PubMed:17506858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31645-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31645-2; Sequence=VSP_046553;
CC -!- TISSUE SPECIFICITY: Expressed in platelets (at protein level).
CC {ECO:0000269|PubMed:17506858}.
CC -!- PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required
CC for cGMP-mediated SERT regulation. {ECO:0000269|PubMed:17913921,
CC ECO:0000269|PubMed:21992875}.
CC -!- POLYMORPHISM: A polymorphism in the promoter region (5-HTT gene-linked
CC polymorphic region, 5-HTTLPR) is located approximately 1 kb upstream of
CC the transcription initiation site and is composed of 16 repeat
CC elements. The polymorphism consists of a 44-bp insertion or deletion
CC involving repeat elements 6 to 8. The short allele is associated with
CC lower transcriptional efficiency of the promoter compared with the long
CC allele. Over half of the Caucasian population has a short allele.
CC Individuals with one or two copies of the short allele exhibit more
CC depressive symptoms, diagnosable depression and suicidality in relation
CC to stressful life events than individuals homozygous for the long
CC allele. {ECO:0000269|PubMed:12869766}.
CC -!- POLYMORPHISM: The 5-HTTLPR polymorphism may influence susceptibility to
CC anxiety [MIM:607834]. {ECO:0000269|PubMed:15108187}.
CC -!- POLYMORPHISM: The polymorphism Val-425 seems to be linked to a
CC susceptibility to obsessive-compulsive disorder (OCD) [MIM:164230].
CC {ECO:0000269|PubMed:12869649, ECO:0000269|PubMed:14593431,
CC ECO:0000269|PubMed:17913921}.
CC -!- POLYMORPHISM: Genetic variations in SLC6A4 determine the genetic
CC susceptibility to alcoholism [MIM:103780].
CC {ECO:0000269|PubMed:15635638}.
CC -!- MISCELLANEOUS: This protein is the target of psychomotor stimulants
CC such as amphetamines or cocaine.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A4 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was reported to interact with VIM, however the paper was
CC retracted as some results and conclusions are not reliable.
CC {ECO:0000269|PubMed:19270731, ECO:0000305|PubMed:30707744}.
CC -!- CAUTION: Was reported to interact with RAB4 and to be induced by
CC serotonin, however the paper was retracted as some results and
CC conclusions are not reliable. {ECO:0000269|PubMed:18227069,
CC ECO:0000305|PubMed:31201246}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Serotonin transporter entry;
CC URL="https://en.wikipedia.org/wiki/Serotonin_transporter";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Love, love, love... -Issue
CC 123 of November 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/123";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/slc6a4/";
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DR EMBL; X70697; CAA50029.1; -; mRNA.
DR EMBL; L05568; AAA35492.1; -; mRNA.
DR EMBL; AY902473; AAW80933.1; -; mRNA.
DR EMBL; EU099989; ABV02581.1; -; Genomic_DNA.
DR EMBL; BC069484; AAH69484.1; -; mRNA.
DR EMBL; U79746; AAB93475.1; -; Genomic_DNA.
DR EMBL; AK308014; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11256.1; -. [P31645-1]
DR PIR; A47398; A47398.
DR RefSeq; NP_001036.1; NM_001045.5. [P31645-1]
DR PDB; 5I6X; X-ray; 3.14 A; A=76-618.
DR PDB; 5I6Z; X-ray; 4.53 A; A=76-618.
DR PDB; 5I71; X-ray; 3.15 A; A=76-618.
DR PDB; 5I73; X-ray; 3.24 A; A=76-618.
DR PDB; 5I74; X-ray; 3.40 A; A=76-618.
DR PDB; 5I75; X-ray; 3.49 A; A=76-618.
DR PDB; 6AWN; X-ray; 3.62 A; A=76-618.
DR PDB; 6AWO; X-ray; 3.53 A; A=76-618.
DR PDB; 6AWP; X-ray; 3.80 A; A=76-618.
DR PDB; 6AWQ; X-ray; 4.05 A; A=76-618.
DR PDB; 6DZV; EM; 4.20 A; A=79-615.
DR PDB; 6DZW; EM; 4.30 A; A=79-615.
DR PDB; 6DZY; EM; 4.10 A; A=79-615.
DR PDB; 6DZZ; EM; 3.60 A; A=78-617.
DR PDB; 6VRH; EM; 3.30 A; A=1-630.
DR PDB; 6VRK; EM; 4.10 A; A=1-630.
DR PDB; 6VRL; EM; 3.80 A; A=1-630.
DR PDB; 6W2B; X-ray; 4.70 A; A=76-618.
DR PDB; 6W2C; X-ray; 6.30 A; A=76-618.
DR PDB; 7LI6; EM; 3.50 A; A=79-617.
DR PDB; 7LI7; EM; 4.10 A; A=79-615.
DR PDB; 7LI8; EM; 3.90 A; A=79-617.
DR PDB; 7LI9; EM; 3.90 A; A=79-617.
DR PDB; 7LIA; EM; 3.30 A; A=79-617.
DR PDB; 7LWD; EM; 3.65 A; A=77-617.
DR PDB; 7MGW; EM; 3.50 A; A=79-615.
DR PDBsum; 5I6X; -.
DR PDBsum; 5I6Z; -.
DR PDBsum; 5I71; -.
DR PDBsum; 5I73; -.
DR PDBsum; 5I74; -.
DR PDBsum; 5I75; -.
DR PDBsum; 6AWN; -.
DR PDBsum; 6AWO; -.
DR PDBsum; 6AWP; -.
DR PDBsum; 6AWQ; -.
DR PDBsum; 6DZV; -.
DR PDBsum; 6DZW; -.
DR PDBsum; 6DZY; -.
DR PDBsum; 6DZZ; -.
DR PDBsum; 6VRH; -.
DR PDBsum; 6VRK; -.
DR PDBsum; 6VRL; -.
DR PDBsum; 6W2B; -.
DR PDBsum; 6W2C; -.
DR PDBsum; 7LI6; -.
DR PDBsum; 7LI7; -.
DR PDBsum; 7LI8; -.
DR PDBsum; 7LI9; -.
DR PDBsum; 7LIA; -.
DR PDBsum; 7LWD; -.
DR PDBsum; 7MGW; -.
DR AlphaFoldDB; P31645; -.
DR SMR; P31645; -.
DR BioGRID; 112423; 23.
DR IntAct; P31645; 3.
DR MINT; P31645; -.
DR STRING; 9606.ENSP00000261707; -.
DR BindingDB; P31645; -.
DR ChEMBL; CHEMBL228; -.
DR DrugBank; DB01472; 4-Methoxyamphetamine.
DR DrugBank; DB04836; Amineptine.
DR DrugBank; DB05964; Amitifadine.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00182; Amphetamine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB00245; Benzatropine.
DR DrugBank; DB04889; Bicifadine.
DR DrugBank; DB09016; Butriptyline.
DR DrugBank; DB01114; Chlorpheniramine.
DR DrugBank; DB00215; Citalopram.
DR DrugBank; DB01242; Clomipramine.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB05688; CRx-119.
DR DrugBank; DB00924; Cyclobenzaprine.
DR DrugBank; DB12305; Dasotraline.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB06700; Desvenlafaxine.
DR DrugBank; DB01191; Dexfenfluramine.
DR DrugBank; DB06701; Dexmethylphenidate.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB09167; Dosulepin.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB00476; Duloxetine.
DR DrugBank; DB01363; Ephedra sinica root.
DR DrugBank; DB01175; Escitalopram.
DR DrugBank; DB09194; Etoperidone.
DR DrugBank; DB00574; Fenfluramine.
DR DrugBank; DB00472; Fluoxetine.
DR DrugBank; DB00176; Fluvoxamine.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB08918; Levomilnacipran.
DR DrugBank; DB09195; Lorpiprazole.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB06077; Lumateperone.
DR DrugBank; DB00579; Mazindol.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB01454; Midomafetamine.
DR DrugBank; DB04896; Milnacipran.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB00370; Mirtazapine.
DR DrugBank; DB01442; MMDA.
DR DrugBank; DB01149; Nefazodone.
DR DrugBank; DB09186; Nisoxetine.
DR DrugBank; DB04821; Nomifensine.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB05422; OPC-14523.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB00191; Phentermine.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00344; Protriptyline.
DR DrugBank; DB00852; Pseudoephedrine.
DR DrugBank; DB08839; Serotonin.
DR DrugBank; DB01104; Sertraline.
DR DrugBank; DB01105; Sibutramine.
DR DrugBank; DB06204; Tapentadol.
DR DrugBank; DB01079; Tegaserod.
DR DrugBank; DB06156; Tesofensine.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB00656; Trazodone.
DR DrugBank; DB00726; Trimipramine.
DR DrugBank; DB00285; Venlafaxine.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB06684; Vilazodone.
DR DrugBank; DB09068; Vortioxetine.
DR DrugBank; DB04832; Zimelidine.
DR DrugBank; DB09225; Zotepine.
DR DrugCentral; P31645; -.
DR GuidetoPHARMACOLOGY; 928; -.
DR TCDB; 2.A.22.1.1; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; P31645; 2 sites.
DR iPTMnet; P31645; -.
DR PhosphoSitePlus; P31645; -.
DR BioMuta; SLC6A4; -.
DR DMDM; 400630; -.
DR MassIVE; P31645; -.
DR PaxDb; P31645; -.
DR PeptideAtlas; P31645; -.
DR PRIDE; P31645; -.
DR ProteomicsDB; 54798; -. [P31645-1]
DR ABCD; P31645; 2 sequenced antibodies.
DR Antibodypedia; 26840; 346 antibodies from 36 providers.
DR DNASU; 6532; -.
DR Ensembl; ENST00000261707.7; ENSP00000261707.3; ENSG00000108576.10. [P31645-1]
DR Ensembl; ENST00000401766.6; ENSP00000385822.2; ENSG00000108576.10. [P31645-1]
DR Ensembl; ENST00000650711.1; ENSP00000498537.1; ENSG00000108576.10. [P31645-1]
DR GeneID; 6532; -.
DR KEGG; hsa:6532; -.
DR MANE-Select; ENST00000650711.1; ENSP00000498537.1; NM_001045.6; NP_001036.1.
DR UCSC; uc002hey.6; human. [P31645-1]
DR CTD; 6532; -.
DR DisGeNET; 6532; -.
DR GeneCards; SLC6A4; -.
DR HGNC; HGNC:11050; SLC6A4.
DR HPA; ENSG00000108576; Tissue enhanced (brain, intestine, lung).
DR MalaCards; SLC6A4; -.
DR MIM; 103780; phenotype.
DR MIM; 164230; phenotype.
DR MIM; 182138; gene.
DR MIM; 607834; phenotype.
DR neXtProt; NX_P31645; -.
DR OpenTargets; ENSG00000108576; -.
DR PharmGKB; PA312; -.
DR VEuPathDB; HostDB:ENSG00000108576; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000157855; -.
DR InParanoid; P31645; -.
DR OMA; SFICIPA; -.
DR PhylomeDB; P31645; -.
DR TreeFam; TF343812; -.
DR PathwayCommons; P31645; -.
DR Reactome; R-HSA-380615; Serotonin clearance from the synaptic cleft.
DR SignaLink; P31645; -.
DR SIGNOR; P31645; -.
DR BioGRID-ORCS; 6532; 13 hits in 1074 CRISPR screens.
DR GeneWiki; Serotonin_transporter; -.
DR GenomeRNAi; 6532; -.
DR Pharos; P31645; Tclin.
DR PRO; PR:P31645; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P31645; protein.
DR Bgee; ENSG00000108576; Expressed in right lung and 111 other tissues.
DR ExpressionAtlas; P31645; baseline and differential.
DR Genevisible; P31645; HS.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0099154; C:serotonergic synapse; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0019811; F:cocaine binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
DR GO; GO:0071321; P:cellular response to cGMP; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0015844; P:monoamine transport; IDA:MGI.
DR GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0046621; P:negative regulation of organ growth; ISS:BHF-UCL.
DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
DR GO; GO:0006836; P:neurotransmitter transport; ISS:ARUK-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0014064; P:positive regulation of serotonin secretion; IEA:Ensembl.
DR GO; GO:0090067; P:regulation of thalamus size; IMP:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042713; P:sperm ejaculation; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR013086; Na/ntran_symport_serotonin_N.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF03491; 5HT_transport_N; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR01203; 5HTTRANSPORT.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Disulfide bond; Endosome; Glycoprotein; Membrane; Metal-binding;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Sodium;
KW Symport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..630
FT /note="Sodium-dependent serotonin transporter"
FT /id="PRO_0000214757"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..112
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 113..115
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 136..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..186
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 187..252
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..271
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 272..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 298..324
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..347
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 348..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..380
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 381..421
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..443
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 444..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..483
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 484..494
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..516
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 517..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 539..558
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 559..574
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 575..595
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:27049939"
FT TOPO_DOM 596..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..624
FT /note="Interaction with RAB4A"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 96
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27049939"
FT BINDING 97
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27049939"
FT BINDING 336
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27049939"
FT BINDING 368
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27049939"
FT BINDING 434
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 437
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 438
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21992875"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21992875"
FT MOD_RES 276
FT /note="Phosphothreonine; by PKG"
FT /evidence="ECO:0000269|PubMed:17913921"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27049939"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27049939"
FT DISULFID 200..209
FT /evidence="ECO:0007744|PDB:5I6X, ECO:0007744|PDB:5I6Z,
FT ECO:0007744|PDB:5I71, ECO:0007744|PDB:5I73,
FT ECO:0007744|PDB:5I74, ECO:0007744|PDB:5I75"
FT VAR_SEQ 1
FT /note="M -> MSQSRRVNPDDRELGGDLQIQAPRDQLGSLADGHQCHLLTSRM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046553"
FT VARIANT 56
FT /note="G -> A (in dbSNP:rs6355)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014181"
FT VARIANT 201
FT /note="K -> N (in dbSNP:rs2228673)"
FT /id="VAR_029158"
FT VARIANT 425
FT /note="I -> L (in dbSNP:rs28914832)"
FT /id="VAR_036788"
FT VARIANT 425
FT /note="I -> V (linked with susceptibility to obsessive-
FT compulsive disorder; increased serotonin transport
FT capacity; dbSNP:rs28914832)"
FT /evidence="ECO:0000269|PubMed:12869649,
FT ECO:0000269|PubMed:14593431, ECO:0000269|PubMed:17913921"
FT /id="VAR_026751"
FT VARIANT 465
FT /note="F -> L (in dbSNP:rs28914833)"
FT /id="VAR_036789"
FT VARIANT 550
FT /note="L -> V (in dbSNP:rs28914834)"
FT /id="VAR_036790"
FT VARIANT 605
FT /note="K -> N (in dbSNP:rs6352)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014182"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5I74"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5I74"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 253..270
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:5I71"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 358..389
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 409..415
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6VRH"
FT HELIX 420..453
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6VRH"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:6VRH"
FT HELIX 462..477
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 497..513
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:5I6X"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:5I73"
FT HELIX 535..542
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 544..558
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:5I6X"
FT TURN 584..587
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 588..599
FT /evidence="ECO:0007829|PDB:5I6X"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:5I6X"
SQ 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
