ID   SC6A1_MOUSE             Reviewed;         599 AA.
AC   P31648;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Sodium- and chloride-dependent GABA transporter 1;
DE            Short=GAT-1;
DE   AltName: Full=Solute carrier family 6 member 1;
GN   Name=Slc6a1; Synonyms=Gabt1, Gat-1, Gat1;
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 [GENOMIC DNA / MRNA].
RX   PubMed=1631167; DOI=10.1073/pnas.89.14.6639;
RA   Liu Q.-R., Mandiyan S., Nelson H., Nelson N.;
RT   "A family of genes encoding neurotransmitter transporters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6639-6643(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=8420981; DOI=10.1016/s0021-9258(18)53968-5;
RA   Liu Q.-R., Lopez-Coecuera B., Mandiyan S., Nelson H., Nelson N.;
RT   "Molecular characterization of four pharmacologically distinct gamma-
RT   aminobutyric acid transporters in mouse brain.";
RL   J. Biol. Chem. 268:2106-2112(1993).
RN   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, INTERACTION WITH PALS1, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=15234345; DOI=10.1016/j.mcn.2004.03.006;
RA   McHugh E.M., Zhu W., Milgram S., Mager S.;
RT   "The GABA transporter GAT1 and the MAGUK protein Pals1: interaction, uptake
RT   modulation, and coexpression in the brain.";
RL   Mol. Cell. Neurosci. 26:406-417(2004).
RN   [5]
RP   FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=16150932; DOI=10.1124/mol.105.013870;
RA   Krause S., Schwarz W.;
RT   "Identification and selective inhibition of the channel mode of the
RT   neuronal GABA transporter 1.";
RL   Mol. Pharmacol. 68:1728-1735(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-591, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=30270321; DOI=10.1248/bpb.b18-00168;
RA   Nishimura T., Higuchi K., Yoshida Y., Sugita-Fujisawa Y., Kojima K.,
RA   Sugimoto M., Santo M., Tomi M., Nakashima E.;
RT   "Hypotaurine Is a Substrate of GABA Transporter Family Members GAT2/Slc6a13
RT   and TAUT/Slc6a6.";
RL   Biol. Pharm. Bull. 41:1523-1529(2018).
CC   -!- FUNCTION: Mediates transport of gamma-aminobutyric acid (GABA) together
CC       with sodium and chloride and is responsible for the reuptake of GABA
CC       from the synapse (PubMed:15234345, PubMed:16150932, PubMed:8420981,
CC       PubMed:30270321). The translocation of GABA, however, may also occur in
CC       the reverse direction leading to the release of GABA (By similarity).
CC       The direction and magnitude of GABA transport is a consequence of the
CC       prevailing thermodynamic conditions, determined by membrane potential
CC       and the intracellular and extracellular concentrations of Na(+), Cl(-)
CC       and GABA (By similarity). Can also mediate sodium- and chloride-
CC       dependent transport of hypotaurine but to a much lower extent as
CC       compared to GABA (PubMed:30270321). {ECO:0000250|UniProtKB:P23978,
CC       ECO:0000269|PubMed:15234345, ECO:0000269|PubMed:16150932,
CC       ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:8420981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC         aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC         Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:15234345,
CC         ECO:0000269|PubMed:16150932, ECO:0000269|PubMed:30270321,
CC         ECO:0000269|PubMed:8420981};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC         Evidence={ECO:0000305|PubMed:15234345};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70689;
CC         Evidence={ECO:0000250|UniProtKB:P23978};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC         + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC         Evidence={ECO:0000269|PubMed:30270321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC         Evidence={ECO:0000305|PubMed:30270321};
CC   -!- ACTIVITY REGULATION: Inhibited by N-[4,4-Diphenyl-3-butenyl]-nipecotic
CC       acid (SKF-89976-A), L-2,4-diamino-n-butyric acid, guvacine and
CC       nipecotic acid. {ECO:0000269|PubMed:16150932,
CC       ECO:0000269|PubMed:8420981}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=62 uM for GABA {ECO:0000269|PubMed:16150932};
CC   -!- SUBUNIT: Interacts (via PDZ domain-binding motif) with PALS1;
CC       interaction increases SLC6A1-mediated GABA uptake.
CC       {ECO:0000269|PubMed:15234345}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23978};
CC       Multi-pass membrane protein {ECO:0000255}. Presynapse
CC       {ECO:0000269|PubMed:15234345}. Note=Localized at the presynaptic
CC       terminals of interneurons. {ECO:0000269|PubMed:15234345}.
CC   -!- TISSUE SPECIFICITY: Brain. Expressed in the dentate gyrus of
CC       hippocampus, striatum and cerebellum (at protein level).
CC       {ECO:0000269|PubMed:15234345}.
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)
CC       (TC 2.A.22) family. SLC6A1 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M92377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M92378; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK042956; BAC31418.1; -; mRNA.
DR   EMBL; AK052971; BAC35226.1; -; mRNA.
DR   EMBL; AK053883; BAC35574.1; -; mRNA.
DR   CCDS; CCDS20434.1; -.
DR   PIR; F46027; F46027.
DR   RefSeq; NP_848818.1; NM_178703.4.
DR   AlphaFoldDB; P31648; -.
DR   SMR; P31648; -.
DR   BioGRID; 231239; 85.
DR   IntAct; P31648; 1.
DR   MINT; P31648; -.
DR   STRING; 10090.ENSMUSP00000032454; -.
DR   BindingDB; P31648; -.
DR   ChEMBL; CHEMBL5445; -.
DR   DrugCentral; P31648; -.
DR   GuidetoPHARMACOLOGY; 929; -.
DR   GlyCosmos; P31648; 3 sites, No reported glycans.
DR   GlyGen; P31648; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P31648; -.
DR   PhosphoSitePlus; P31648; -.
DR   SwissPalm; P31648; -.
DR   MaxQB; P31648; -.
DR   PaxDb; 10090-ENSMUSP00000032454; -.
DR   PeptideAtlas; P31648; -.
DR   ProteomicsDB; 256737; -.
DR   Antibodypedia; 1391; 315 antibodies from 33 providers.
DR   DNASU; 232333; -.
DR   Ensembl; ENSMUST00000032454.8; ENSMUSP00000032454.6; ENSMUSG00000030310.12.
DR   GeneID; 232333; -.
DR   KEGG; mmu:232333; -.
DR   UCSC; uc009dhu.2; mouse.
DR   AGR; MGI:95627; -.
DR   CTD; 6529; -.
DR   MGI; MGI:95627; Slc6a1.
DR   VEuPathDB; HostDB:ENSMUSG00000030310; -.
DR   eggNOG; KOG3660; Eukaryota.
DR   GeneTree; ENSGT00940000156027; -.
DR   HOGENOM; CLU_006855_9_5_1; -.
DR   InParanoid; P31648; -.
DR   OMA; TIWFVSR; -.
DR   OrthoDB; 3084493at2759; -.
DR   PhylomeDB; P31648; -.
DR   TreeFam; TF343812; -.
DR   Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   Reactome; R-MMU-888593; Reuptake of GABA.
DR   BioGRID-ORCS; 232333; 4 hits in 79 CRISPR screens.
DR   PRO; PR:P31648; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P31648; Protein.
DR   Bgee; ENSMUSG00000030310; Expressed in cerebellum lobe and 107 other cell types or tissues.
DR   ExpressionAtlas; P31648; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; IMP:ARUK-UCL.
DR   GO; GO:0005332; F:gamma-aminobutyric acid:sodium:chloride symporter activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015378; F:sodium:chloride symporter activity; ISO:MGI.
DR   GO; GO:0008306; P:associative learning; IMP:ARUK-UCL.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR   GO; GO:0051939; P:gamma-aminobutyric acid import; IMP:ARUK-UCL.
DR   GO; GO:0098658; P:inorganic anion import across plasma membrane; ISO:MGI.
DR   GO; GO:0007612; P:learning; ISO:MGI.
DR   GO; GO:0007613; P:memory; IMP:ARUK-UCL.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:MGI.
DR   GO; GO:0098810; P:neurotransmitter reuptake; IDA:SynGO.
DR   GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR   GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR   GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR   GO; GO:0014074; P:response to purine-containing compound; ISO:MGI.
DR   GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR   GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050808; P:synapse organization; IMP:ARUK-UCL.
DR   CDD; cd11506; SLC6sbd_GAT1; 1.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002980; Na/ntran_symport_GABA_GAT1.
DR   InterPro; IPR037272; SNS_sf.
DR   NCBIfam; NF037979; Na_transp; 1.
DR   PANTHER; PTHR11616:SF138; SODIUM- AND CHLORIDE-DEPENDENT GABA TRANSPORTER 1; 1.
DR   PANTHER; PTHR11616; SODIUM/CHLORIDE DEPENDENT TRANSPORTER; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01195; GAT1TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   SUPFAM; SSF161070; SNF-like; 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.
DR   Genevisible; P31648; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Membrane;
KW   Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW   Reference proteome; Sodium; Symport; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..599
FT                   /note="Sodium- and chloride-dependent GABA transporter 1"
FT                   /id="PRO_0000214744"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        53..73
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..80
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        81..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        124..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        212..230
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        239..256
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        292..309
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        321..342
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..374
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        375..394
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        422..440
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..456
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        457..477
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        478..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        498..517
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        518..535
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   TRANSMEM        536..554
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        555..599
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P23978"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           597..599
FT                   /note="PDZ-binding"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         61
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         62
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         66
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         295
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         327
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         392
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         395
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   BINDING         396
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         591
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        164..173
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT   CONFLICT        117..118
FT                   /note="KL -> NW (in Ref. 1; M92378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126..127
FT                   /note="GL -> AV (in Ref. 1; M92378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212..213
FT                   /note="WP -> C (in Ref. 1; M92378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285..286
FT                   /note="WL -> IF (in Ref. 1; M92378)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   599 AA;  67001 MW;  4FEF85092DC1D045 CRC64;
     MATDNSKVAD GQISTEVSEA PVASDKPKTL VVKVQKKAGD LPDRDTWKGR FDFLMSCVGY
     AIGLGNVWRF PYLCGKNGGG AFLIPYFLTL IFAGVPLFLL ECSLGQYTSI GGLGVWKLAP
     MFKGVGLAAA VLSFWLNIYY IVIISWAIYY LYNSFTTTLP WKQCDNPWNT DRCFSNYSLV
     NTTNMTSAVV EFWERNMHQM TDGLDKPGQI RWPLAITLAI AWVLVYFCIW KGVGWTGKVV
     YFSATYPYIM LIILFFRGVT LPGAKEGILF YITPNFRKLS DSEVWLDAAT QIFFSYGLGL
     GSLIALGSYN SFHNNVYRDS IIVCCINSCT SMFAGFVIFS IVGFMAHVTK RSIADVAASG
     PGLAFLAYPE AVTQLPISPL WAILFFSMLL MLGIDSQFCT VEGFITALVD EYPRLLRNRR
     ELFIAAVCIV SYLIGLSNIT QGGIYVFKLF DYYSASGMSL LFLVFFECVS ISWFYGVNRF
     YDNIQEMVGS RPCIWWKLCW SFFTPIIVAG VFLFSAVQMT PLTMGSYVFP KWGQGVGWLM
     ALSSMVLIPG YMAYMFLTLK GSLKQRLQVM IQPSEDIVRP ENGPEQPQAG SSASKEAYI
//