SC6A4_RAT
ID SC6A4_RAT Reviewed; 630 AA.
AC P31652; P23976;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sodium-dependent serotonin transporter;
DE Short=SERT {ECO:0000303|PubMed:16870614};
DE AltName: Full=5HT transporter;
DE Short=5HTT;
DE AltName: Full=Solute carrier family 6 member 4;
GN Name=Slc6a4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=1765155; DOI=10.1016/0014-5793(91)81418-8;
RA Mayser W., Betz H., Schloss P.;
RT "Isolation of cDNAs encoding a novel member of the neurotransmitter
RT transporter gene family.";
RL FEBS Lett. 295:203-206(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain stem;
RX PubMed=1944572; DOI=10.1038/354066a0;
RA Blakely R.D., Berson H.E., Fremeau R.T. Jr., Caron M.G., Peek M.M.,
RA Prince H.K., Bardley C.C.;
RT "Cloning and expression of a functional serotonin transporter from rat
RT brain.";
RL Nature 354:66-70(1991).
RN [3]
RP SEQUENCE REVISION.
RA Blakely R.D.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1948036; DOI=10.1126/science.1948036;
RA Hoffman B.J., Mezey E., Brownstein M.J.;
RT "Cloning of a serotonin transporter affected by antidepressants.";
RL Science 254:579-580(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fawn hooded;
RA Gonzalez A.M., Smith A.P.L., Emery C.J., Higenbottam T.W.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP MUTAGENESIS OF CYS-109 AND ILE-172, FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=10716733; DOI=10.1073/pnas.97.7.3106;
RA Kilic F., Rudnick G.;
RT "Oligomerization of serotonin transporter and its functional
RT consequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3106-3111(2000).
RN [7]
RP INTERACTION WITH STX1A, AND SUBCELLULAR LOCATION.
RX PubMed=11709063; DOI=10.1042/0300-5127:0290722;
RA Haase J., Killian A.M., Magnani F., Williams C.;
RT "Regulation of the serotonin transporter by interacting proteins.";
RL Biochem. Soc. Trans. 29:722-728(2001).
RN [8]
RP RETRACTED PAPER.
RX PubMed=12944413; DOI=10.1074/jbc.m306360200;
RA Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C., Bene A.,
RA Kilic F.;
RT "Glycosyl modification facilitates homo- and hetero-oligomerization of the
RT serotonin transporter. A specific role for sialic acid residues.";
RL J. Biol. Chem. 278:43991-44000(2003).
RN [9]
RP RETRACTION NOTICE OF PUBMED:12944413.
RX PubMed=31201245; DOI=10.1074/jbc.w119.009466;
RA Ozaslan D., Wang S., Ahmed B.A., Kocabas A.M., McCastlain J.C., Bene A.,
RA Kilic F.;
RT "Withdrawal: Glycosyl modification facilitates homo- and hetero-
RT oligomerization of the serotonin transporter: a specific role for sialic
RT acid residues.";
RL J. Biol. Chem. 294:9657-9657(2019).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FILAMENTOUS ACTIN.
RX PubMed=15627510; DOI=10.1016/j.neuint.2004.08.008;
RA Mochizuki H., Amano T., Seki T., Matsubayashi H., Mitsuhata C., Morita K.,
RA Kitayama S., Dohi T., Mishima H.K., Sakai N.;
RT "Role of C-terminal region in the functional regulation of rat serotonin
RT transporter (SERT).";
RL Neurochem. Int. 46:93-105(2005).
RN [11]
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 [12]
RP PHOSPHORYLATION AT THR-276.
RX PubMed=17310063; DOI=10.1074/jbc.m611353200;
RA Ramamoorthy S., Samuvel D.J., Buck E.R., Rudnick G., Jayanthi L.D.;
RT "Phosphorylation of threonine residue 276 is required for acute regulation
RT of serotonin transporter by cyclic GMP.";
RL J. Biol. Chem. 282:11639-11647(2007).
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:10716733,
CC ECO:0000269|PubMed:15627510, ECO:0000269|PubMed:1944572,
CC ECO:0000269|PubMed:1948036}.
CC -!- SUBUNIT: Monomer or homooligomer (PubMed:10716733). Interacts with
CC TGFB1I1. Interacts with SEC23A, SEC24C and PATJ. Interacts with NOS1;
CC the interaction may diminish the cell surface localization of SERT in
CC the brain and, correspondingly, reduce serotonin reuptake (By
CC similarity). Interacts (via C-terminus) with SCAMP2; the interaction is
CC direct and retains transporter molecules intracellularly
CC (PubMed:16870614). Interacts with filamentous actin and STX1A
CC (PubMed:11709063). Interacts with ITGAV:ITGB3 (By similarity).
CC {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:Q60857,
CC ECO:0000269|PubMed:10716733, ECO:0000269|PubMed:11709063,
CC ECO:0000269|PubMed:16870614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11709063,
CC ECO:0000269|PubMed:15627510, ECO:0000269|PubMed:16870614,
CC ECO:0000269|PubMed:1944572, ECO:0000269|PubMed:1948036}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}. 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 (PubMed:11709063). Density
CC of transporter molecules on the plasma membrane is also regulated by
CC serotonin (By similarity). Density of transporter molecules seems to be
CC modulated by ITGAV:ITGB3 (By similarity).
CC {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:Q60857,
CC ECO:0000269|PubMed:11709063, ECO:0000269|PubMed:16870614}.
CC -!- PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required
CC for cGMP-mediated SERT regulation. {ECO:0000269|PubMed:17310063}.
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: Reported to be glycosylated with sialylated N-glycans and in
CC its sialylated form to interact with MYH9 (PubMed:12944413). However,
CC this publication was retracted due to image duplication in the figures.
CC {ECO:0000269|PubMed:12944413, ECO:0000305|PubMed:31201245}.
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DR EMBL; X63995; CAA45401.1; -; mRNA.
DR EMBL; X63253; CAA44913.1; -; mRNA.
DR EMBL; M79450; AAA42186.1; -; mRNA.
DR EMBL; Y11024; CAA71909.1; -; mRNA.
DR PIR; S19585; S19585.
DR PIR; S30604; S30604.
DR RefSeq; NP_037166.2; NM_013034.4.
DR RefSeq; XP_008766172.1; XM_008767950.2.
DR RefSeq; XP_017452530.1; XM_017597041.1.
DR RefSeq; XP_017452531.1; XM_017597042.1.
DR RefSeq; XP_017452532.1; XM_017597043.1.
DR AlphaFoldDB; P31652; -.
DR SMR; P31652; -.
DR BioGRID; 247584; 2.
DR IntAct; P31652; 1.
DR STRING; 10116.ENSRNOP00000004717; -.
DR BindingDB; P31652; -.
DR ChEMBL; CHEMBL313; -.
DR DrugCentral; P31652; -.
DR GuidetoPHARMACOLOGY; 928; -.
DR GlyGen; P31652; 2 sites.
DR iPTMnet; P31652; -.
DR SwissPalm; P31652; -.
DR PaxDb; P31652; -.
DR Ensembl; ENSRNOT00000004717; ENSRNOP00000004717; ENSRNOG00000003476.
DR GeneID; 25553; -.
DR KEGG; rno:25553; -.
DR CTD; 6532; -.
DR RGD; 3714; Slc6a4.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000157855; -.
DR HOGENOM; CLU_006855_9_0_1; -.
DR InParanoid; P31652; -.
DR OMA; SFICIPA; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; P31652; -.
DR TreeFam; TF343812; -.
DR Reactome; R-RNO-380615; Serotonin clearance from the synaptic cleft.
DR PRO; PR:P31652; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003476; Expressed in duodenum and 16 other tissues.
DR Genevisible; P31652; RN.
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; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0099154; C:serotonergic synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0019811; F:cocaine binding; IMP:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:RGD.
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; IPI:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0071321; P:cellular response to cGMP; IDA:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IMP:RGD.
DR GO; GO:0007626; P:locomotory behavior; NAS:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0015844; P:monoamine transport; ISO:RGD.
DR GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; IMP:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0046621; P:negative regulation of organ growth; ISO:RGD.
DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IMP:RGD.
DR GO; GO:0098810; P:neurotransmitter reuptake; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0014064; P:positive regulation of serotonin secretion; IMP:RGD.
DR GO; GO:0090067; P:regulation of thalamus size; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0006837; P:serotonin transport; IDA:UniProtKB.
DR GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042713; P:sperm ejaculation; IMP:RGD.
DR GO; GO:0042310; P:vasoconstriction; IMP:RGD.
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 Cell junction; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW Membrane; Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Sodium; Symport; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..630
FT /note="Sodium-dependent serotonin transporter"
FT /id="PRO_0000214760"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..112
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 113..115
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..135
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 136..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..186
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 187..252
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..271
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 272..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 298..324
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..347
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 348..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..380
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 381..421
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..443
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 444..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..483
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 484..494
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..516
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 517..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 539..558
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 559..574
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 575..595
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT TOPO_DOM 596..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 23..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..624
FT /note="Interaction with RAB4A"
FT /evidence="ECO:0000250"
FT COMPBIAS 35..60
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:0000250|UniProtKB:Q7K4Y6"
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:0000250|UniProtKB:Q7K4Y6"
FT BINDING 336
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 368
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
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:0000250|UniProtKB:P31645"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17310063"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT DISULFID 200..209
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT MUTAGEN 109
FT /note="C->A: Cocaine is effective at blocking transport."
FT /evidence="ECO:0000269|PubMed:10716733"
FT MUTAGEN 172
FT /note="I->C: Cocaine is effective at blocking transport."
FT /evidence="ECO:0000269|PubMed:10716733"
FT CONFLICT 415
FT /note="A -> G (in Ref. 4; AAA42186)"
FT /evidence="ECO:0000305"
FT CONFLICT 533..536
FT /note="PGWF -> GMV (in Ref. 4; AAA42186)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..630
FT /note="PCGDIRMNAV -> RVGHPHECCVTHPGRGHLFPATSLSSEKPTGLLL (in
FT Ref. 4; AAA42186)"
FT /evidence="ECO:0000305"
SQ 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
