SC6A4_MOUSE
ID SC6A4_MOUSE Reviewed; 630 AA.
AC Q60857; O35241; Q5NCR6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sodium-dependent serotonin transporter {ECO:0000305};
DE Short=SERT {ECO:0000303|PubMed:29038237};
DE AltName: Full=5HT transporter;
DE Short=5HTT;
DE AltName: Full=Solute carrier family 6 member 4;
GN Name=Slc6a4 {ECO:0000312|MGI:MGI:96285};
GN Synonyms=Htt, Sert {ECO:0000303|PubMed:29038237};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9037532; DOI=10.1016/s0169-328x(96)00172-6;
RA Chang A.S., Chang S.M., Starnes D.M., Schroeter S., Bauman A.L.,
RA Blakely R.D.;
RT "Cloning and expression of the mouse serotonin transporter.";
RL Brain Res. Mol. Brain Res. 43:185-192(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9073170; DOI=10.1016/s0169-328x(96)00234-3;
RA Bengel D., Heils A., Petri S., Seemann M., Glatz K., Andrews A.,
RA Murphy D.L., Lesch K.P.;
RT "Gene structure and 5'-flanking regulatory region of the murine serotonin
RT transporter.";
RL Brain Res. Mol. Brain Res. 44:286-292(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC STRAIN=BALB/cJ;
RA Saito N., Sakai N., Kobayashi S., Fujimoto M., Morikawa O., Ikegaki N.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-630.
RX PubMed=8507984; DOI=10.1007/bf00417438;
RA Gregor P., Patel A., Shimada S., Lin C.L., Rochelle J.M., Kitayama S.,
RA Seldin M.F., Uhl G.R.;
RT "Murine serotonin transporter: sequence and localization to chromosome
RT 11.";
RL Mamm. Genome 4:283-284(1993).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9547354; DOI=10.1124/mol.53.4.649;
RA Bengel D., Murphy D.L., Andrews A.M., Wichems C.H., Feltner D., Heils A.,
RA Mossner R., Westphal H., Lesch K.P.;
RT "Altered brain serotonin homeostasis and locomotor insensitivity to 3, 4-
RT methylenedioxymethamphetamine ('Ecstasy') in serotonin transporter-
RT deficient mice.";
RL Mol. Pharmacol. 53:649-655(1998).
RN [7]
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 [8]
RP INTERACTION WITH NOS1; SEC23A; SEC24C AND PATJ.
RX PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT "Physical interaction between the serotonin transporter and neuronal nitric
RT oxide synthase underlies reciprocal modulation of their activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=20676059; DOI=10.1038/emboj.2010.172;
RA Garcia-Frigola C., Herrera E.;
RT "Zic2 regulates the expression of Sert to modulate eye-specific refinement
RT at the visual targets.";
RL EMBO J. 29:3170-3183(2010).
RN [10]
RP INDUCTION.
RX PubMed=22572884; DOI=10.1124/mol.112.079079;
RA Ushijima K., Koyanagi S., Sato Y., Ogata T., Matsunaga N., Fujimura A.,
RA Ohdo S.;
RT "Role of activating transcription factor-4 in 24-hour rhythm of serotonin
RT transporter expression in the mouse midbrain.";
RL Mol. Pharmacol. 82:264-270(2012).
RN [11]
RP INTERACTION WITH ITGB3, AND SUBCELLULAR LOCATION.
RX PubMed=29038237; DOI=10.1523/jneurosci.1482-17.2017;
RA Dohn M.R., Kooker C.G., Bastarache L., Jessen T., Rinaldi C., Varney S.,
RA Mazalouskas M.D., Pan H., Oliver K.H., Velez Edwards D.R., Sutcliffe J.S.,
RA Denny J.C., Carneiro A.M.D.;
RT "The Gain-of-Function Integrin beta3 Pro33 Variant Alters the Serotonin
RT System in the Mouse Brain.";
RL J. Neurosci. 37:11271-11284(2017).
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:9037532}.
CC -!- SUBUNIT: Monomer or homooligomer (By similarity). Interacts (via C-
CC terminus) with SCAMP2; the interaction is direct and retains
CC transporter molecules intracellularly. Interacts with filamentous actin
CC and STX1A (By similarity). 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 (PubMed:17452640). Interacts with TGFB1I1
CC (PubMed:16803896). Interacts with ITGAV:ITGB3 (PubMed:29038237).
CC {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:P31652,
CC ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:17452640,
CC ECO:0000269|PubMed:29038237}.
CC -!- INTERACTION:
CC Q60857; Q9Z0J4: Nos1; NbExp=4; IntAct=EBI-15633326, EBI-397596;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9037532};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}.
CC Endomembrane system {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane
CC protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse {ECO:0000269|PubMed:29038237}. Cell junction,
CC focal adhesion {ECO:0000269|PubMed:29038237}. Note=Could be part of
CC recycling endosomes. Density of transporter molecules on the plasma
CC membrane is itself regulated by STX1A. Density of transporter molecules
CC on the plasma membrane is also regulated by serotonin (By similarity).
CC Density of transporter molecules seems to be modulated by ITGAV:ITGB3
CC (PubMed:29038237). {ECO:0000250|UniProtKB:P31645,
CC ECO:0000250|UniProtKB:P31652, ECO:0000269|PubMed:29038237}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the uncrossed ipsilateral retinal
CC ganglion cells (iRGCs) of the peripheral ventrotemporal (VT) region
CC segment in the retina at 16.5 dpc. {ECO:0000269|PubMed:20676059}.
CC -!- INDUCTION: Expressed in a circadian manner in the midbrain with a
CC higher level expression seen during the dark phase (at protein level).
CC {ECO:0000269|PubMed:22572884}.
CC -!- PTM: Phosphorylation at Thr-276 increases 5-HT uptake and is required
CC for cGMP-mediated SERT regulation. {ECO:0000250|UniProtKB:P31645}.
CC -!- DISRUPTION PHENOTYPE: Loss of serotonin uptake.
CC {ECO:0000269|PubMed:9547354}.
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 -!- SEQUENCE CAUTION:
CC Sequence=X66119; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF013604; AAB67172.1; -; mRNA.
DR EMBL; Y08870; CAA70092.1; -; Genomic_DNA.
DR EMBL; Y08871; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08872; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08873; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08874; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08875; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08876; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08877; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08878; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08879; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; Y08880; CAA70092.1; JOINED; Genomic_DNA.
DR EMBL; AL603842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U26452; AAA84750.1; -; Genomic_DNA.
DR EMBL; X66119; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25074.1; -.
DR RefSeq; NP_034614.2; NM_010484.2.
DR RefSeq; XP_006532362.1; XM_006532299.2.
DR RefSeq; XP_006532363.1; XM_006532300.2.
DR RefSeq; XP_006532364.1; XM_006532301.3.
DR AlphaFoldDB; Q60857; -.
DR SMR; Q60857; -.
DR BioGRID; 200481; 420.
DR DIP; DIP-60923N; -.
DR IntAct; Q60857; 5.
DR STRING; 10090.ENSMUSP00000021195; -.
DR BindingDB; Q60857; -.
DR ChEMBL; CHEMBL4642; -.
DR DrugCentral; Q60857; -.
DR GlyGen; Q60857; 2 sites.
DR PhosphoSitePlus; Q60857; -.
DR MaxQB; Q60857; -.
DR PaxDb; Q60857; -.
DR PRIDE; Q60857; -.
DR ProteomicsDB; 255473; -.
DR Antibodypedia; 26840; 346 antibodies from 36 providers.
DR DNASU; 15567; -.
DR Ensembl; ENSMUST00000021195; ENSMUSP00000021195; ENSMUSG00000020838.
DR Ensembl; ENSMUST00000108402; ENSMUSP00000104039; ENSMUSG00000020838.
DR GeneID; 15567; -.
DR KEGG; mmu:15567; -.
DR UCSC; uc007kgf.2; mouse.
DR CTD; 6532; -.
DR MGI; MGI:96285; Slc6a4.
DR VEuPathDB; HostDB:ENSMUSG00000020838; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000157855; -.
DR HOGENOM; CLU_006855_9_0_1; -.
DR InParanoid; Q60857; -.
DR OMA; SFICIPA; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q60857; -.
DR TreeFam; TF343812; -.
DR Reactome; R-MMU-380615; Serotonin clearance from the synaptic cleft.
DR BioGRID-ORCS; 15567; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q60857; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60857; protein.
DR Bgee; ENSMUSG00000020838; Expressed in central gray substance of midbrain and 107 other tissues.
DR ExpressionAtlas; Q60857; baseline and differential.
DR Genevisible; Q60857; MM.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0099154; C:serotonergic synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0019811; F:cocaine binding; ISO:MGI.
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; IMP:ARUK-UCL.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:UniProtKB.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
DR GO; GO:0071321; P:cellular response to cGMP; ISO:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; ISO:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0015844; P:monoamine transport; ISO:MGI.
DR GO; GO:0021941; P:negative regulation of cerebellar granule cell precursor proliferation; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:BHF-UCL.
DR GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; ISO:MGI.
DR GO; GO:0098810; P:neurotransmitter reuptake; IMP:SynGO.
DR GO; GO:0006836; P:neurotransmitter transport; IMP:ARUK-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0014064; P:positive regulation of serotonin secretion; ISO:MGI.
DR GO; GO:0090067; P:regulation of thalamus size; ISS: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; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006837; P:serotonin transport; IMP:UniProtKB.
DR GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB.
DR GO; GO:0035176; P:social behavior; IGI:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042713; P:sperm ejaculation; ISO:MGI.
DR GO; GO:0042310; P:vasoconstriction; ISO:MGI.
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_0000214759"
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 1..63
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 45..63
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:0000250|UniProtKB:P31645"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 200..209
FT /evidence="ECO:0000250|UniProtKB:P31645"
FT CONFLICT 39
FT /note="G -> E (in Ref. 1; AAB67172, 2; CAA70092 and 4;
FT AAA84750)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="K -> R (in Ref. 1; AAB67172 and 2; CAA70092)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="P -> Q (in Ref. 2; CAA70092)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="A -> R (in Ref. 2; CAA70092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 70048 MW; 2B6ABD26E3288CD0 CRC64;
METTPLNSQK VLSECKDKED CQENGVLQKG VPTPADKAGP GQISNGYSAV PSTSAGDEAP
HSTPAATTTL VAEIHQGERE TWGKKMDFLL SVIGYAVDLG NIWRFPYICY QNGGGAFLLP
YTIMAIFGGI PLFYMELALG QYHRNGCISI WKKICPIFKG IGYAICIIAF YIASYYNTII
AWALYYLISS FTDQLPWTSC KNSWNTGNCT NYFAQDNITW TLHSTSPAEE FYLRHVLQIH
QSKGLQDLGT ISWQLALCIM LIFTIIYFSI WKGVKTSGKV VWVTATFPYI VLSVLLVRGA
TLPGAWRGVV FYLKPNWQKL LETGVWVDAA AQIFFSLGPG FGVLLAFASY NKFNNNCYQD
ALVTSVVNCM TSFVSGFVIF TVLGYMAEMR NEDVSEVAKD AGPSLLFITY AEAIANMPAS
TFFAIIFFLM LITLGLDSTF AGLEGVITAV LDEFPHIWAK RREWFVLIVV ITCILGSLLT
LTSGGAYVVT LLEEYATGPA VLTVALIEAV VVSWFYGITQ FCSDVKEMLG FSPGWFWRIC
WVAISPLFLL FIICSFLMSP PQLRLFQYNY PHWSIILGYC IGTSSVICIP IYIIYRLIST
PGTLKERIIK SITPETPTEI PCGDIRMNAV
