ID   S23A1_HUMAN             Reviewed;         598 AA.
AC   Q9UHI7; O95191; Q8WWB6; Q9UGH4; Q9UI39;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 4.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Solute carrier family 23 member 1 {ECO:0000305};
DE   AltName: Full=Na(+)/L-ascorbic acid transporter 1;
DE   AltName: Full=Sodium-dependent vitamin C transporter 1 {ECO:0000303|PubMed:10556483};
DE            Short=hSVCT1 {ECO:0000303|PubMed:10556483};
DE   AltName: Full=Yolk sac permease-like molecule 3 {ECO:0000303|PubMed:9804989};
GN   Name=SLC23A1 {ECO:0000312|HGNC:HGNC:10974};
GN   Synonyms=SVCT1 {ECO:0000303|PubMed:10556483}, YSPL3
GN   {ECO:0000303|PubMed:9804989};
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=Fetal liver, and Kidney;
RX   PubMed=9804989; DOI=10.1016/s0167-4781(98)00151-1;
RA   Faaland C.A., Race J.E., Ricken G., Warner F.J., Williams W.J.,
RA   Holtzman E.J.;
RT   "Molecular characterization of two novel transporters from human and mouse
RT   kidney and from LLC-PK1 cells reveals a novel conserved family that is
RT   homologous to bacterial and Aspergillus nucleobase transporters.";
RL   Biochim. Biophys. Acta 1442:353-360(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TRANSPORTER
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RC   TISSUE=Intestinal epithelium;
RX   PubMed=10556483; DOI=10.1016/s0005-2736(99)00182-0;
RA   Wang H., Dutta B., Huang W., Devoe L.D., Leibach F.H., Ganapathy V.,
RA   Prasad P.D.;
RT   "Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary structure,
RT   functional characteristics and evidence for a non-functional splice
RT   variant.";
RL   Biochim. Biophys. Acta 1461:1-9(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PHOSPHORYLATION.
RC   TISSUE=Kidney;
RX   PubMed=10556521; DOI=10.1016/s0014-5793(99)01393-9;
RA   Daruwala R.C., Song J., Koh W.S., Rumsey S.C., Levine M.;
RT   "Cloning and functional characterization of the human sodium-dependent
RT   vitamin C transporters hSVCT1 and hSVCT2.";
RL   FEBS Lett. 460:480-484(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Kidney;
RX   PubMed=10631088; DOI=10.1006/bbrc.1999.1929;
RA   Wang Y., Mackenzie B., Tsukaguchi H., Weremowicz S., Morton C.C.,
RA   Hediger M.A.;
RT   "Human vitamin C (L-ascorbic acid) transporter SVCT1.";
RL   Biochem. Biophys. Res. Commun. 267:488-494(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=11584081; DOI=10.1093/jn/131.10.2623;
RA   Erichsen H.C., Eck P., Levine M., Chanock S.;
RT   "Characterization of the genomic structure of the human vitamin C
RT   transporter SVCT1 (SLC23A2).";
RL   J. Nutr. 131:2623-2627(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver cancer;
RX   PubMed=11396616; DOI=10.1080/09687680110033774;
RA   Liang W.J., Johnson D., Jarvis S.M.;
RT   "Vitamin C transport systems of mammalian cells.";
RL   Mol. Membr. Biol. 18:87-95(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Colon, and Kidney;
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   [9]
RP   GLYCOSYLATION AT ASN-138 AND ASN-144, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=19379732; DOI=10.1016/j.yexcr.2009.04.007;
RA   Velho A.M., Jarvis S.M.;
RT   "Topological studies of hSVCT1, the human sodium-dependent vitamin C
RT   transporter and the influence of N-glycosylation on its intracellular
RT   targeting.";
RL   Exp. Cell Res. 315:2312-2321(2009).
RN   [10]
RP   FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=36749388; DOI=10.1007/s00424-023-02792-1;
RA   Toyoda Y., Miyata H., Uchida N., Morimoto K., Shigesawa R., Kassai H.,
RA   Nakao K., Tomioka N.H., Matsuo H., Ichida K., Hosoyamada M., Aiba A.,
RA   Suzuki H., Takada T.;
RT   "Vitamin C transporter SVCT1 serves a physiological role as a urate
RT   importer: functional analyses and in vivo investigations.";
RL   Pflugers Arch. 475:489-504(2023).
CC   -!- FUNCTION: Sodium:ascorbate cotransporter. Mediates electrogenic uptake
CC       of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate
CC       (PubMed:10556483, PubMed:10556521, PubMed:10631088, PubMed:36749388).
CC       Has retained some ancestral activity toward nucleobases such as urate,
CC       an oxidized purine. Low-affinity high-capacity sodium:urate
CC       cotransporter, may regulate serum urate levels by serving as a renal
CC       urate re-absorber (PubMed:36749388). {ECO:0000269|PubMed:10556483,
CC       ECO:0000269|PubMed:10556521, ECO:0000269|PubMed:10631088,
CC       ECO:0000269|PubMed:36749388}.
CC   -!- FUNCTION: [Isoform 2]: Inactive transporter.
CC       {ECO:0000269|PubMed:10556483}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC         Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:10556483,
CC         ECO:0000269|PubMed:10556521, ECO:0000269|PubMed:10631088,
CC         ECO:0000269|PubMed:36749388};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69884;
CC         Evidence={ECO:0000305|PubMed:10556483, ECO:0000305|PubMed:10556521,
CC         ECO:0000305|PubMed:10631088, ECO:0000305|PubMed:36749388};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Na(+)(out) + urate(out) = 2 Na(+)(in) + urate(in);
CC         Xref=Rhea:RHEA:76339, ChEBI:CHEBI:17775, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:36749388};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76340;
CC         Evidence={ECO:0000305|PubMed:36749388};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1511 uM for urate {ECO:0000269|PubMed:36749388};
CC         KM=252 uM for L-ascorbate {ECO:0000269|PubMed:10556521};
CC         Vmax=265.3 pmol/min/mg enzyme toward urate
CC         {ECO:0000269|PubMed:36749388};
CC         Note=Transports urate at physiological and alkaline pH with similar
CC         efficiency. {ECO:0000269|PubMed:36749388};
CC   -!- INTERACTION:
CC       Q9UHI7; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1759386, EBI-10173507;
CC       Q9UHI7; O43865: AHCYL1; NbExp=3; IntAct=EBI-1759386, EBI-2371423;
CC       Q9UHI7; Q9UBQ7: GRHPR; NbExp=6; IntAct=EBI-1759386, EBI-372445;
CC       Q9UHI7; Q15323: KRT31; NbExp=3; IntAct=EBI-1759386, EBI-948001;
CC       Q9UHI7; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-1759386, EBI-10172150;
CC       Q9UHI7; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1759386, EBI-10172290;
CC       Q9UHI7; P60410: KRTAP10-8; NbExp=4; IntAct=EBI-1759386, EBI-10171774;
CC       Q9UHI7; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1759386, EBI-10172052;
CC       Q9UHI7; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-1759386, EBI-10172511;
CC       Q9UHI7; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1759386, EBI-742948;
CC       Q9UHI7; P16333: NCK1; NbExp=2; IntAct=EBI-1759386, EBI-389883;
CC       Q9UHI7; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-1759386, EBI-945833;
CC       Q9UHI7-3; O43865: AHCYL1; NbExp=3; IntAct=EBI-11998660, EBI-2371423;
CC       Q9UHI7-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11998660, EBI-3867333;
CC       Q9UHI7-3; O95967: EFEMP2; NbExp=3; IntAct=EBI-11998660, EBI-743414;
CC       Q9UHI7-3; P49639: HOXA1; NbExp=3; IntAct=EBI-11998660, EBI-740785;
CC       Q9UHI7-3; Q15323: KRT31; NbExp=3; IntAct=EBI-11998660, EBI-948001;
CC       Q9UHI7-3; O76011: KRT34; NbExp=3; IntAct=EBI-11998660, EBI-1047093;
CC       Q9UHI7-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-11998660, EBI-10171697;
CC       Q9UHI7-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11998660, EBI-11959885;
CC       Q9UHI7-3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11998660, EBI-11749135;
CC       Q9UHI7-3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11998660, EBI-10171774;
CC       Q9UHI7-3; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11998660, EBI-11953334;
CC       Q9UHI7-3; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-11998660, EBI-10302392;
CC       Q9UHI7-3; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11998660, EBI-1043191;
CC       Q9UHI7-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11998660, EBI-16439278;
CC       Q9UHI7-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11998660, EBI-22310682;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10631088,
CC       ECO:0000269|PubMed:19379732, ECO:0000269|PubMed:36749388}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:19379732}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q9UHI7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UHI7-2; Sequence=VSP_006814;
CC       Name=3;
CC         IsoId=Q9UHI7-3; Sequence=VSP_006813;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult small intestine, kidney,
CC       thymus, ovary, colon, prostate and liver, and in fetal kidney, liver
CC       and thymus. {ECO:0000269|PubMed:10556483}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10556521}.
CC   -!- MISCELLANEOUS: Treatment with the protein kinase C stimulator PMA
CC       results in a 10-fold decrease in ascorbate accumulation in transfected
CC       cells. {ECO:0000269|PubMed:10556521}.
CC   -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2)
CC       (TC 2.A.40) family. {ECO:0000305}.
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DR   EMBL; AF058317; AAC78804.1; -; mRNA.
DR   EMBL; AF170911; AAF24759.1; -; mRNA.
DR   EMBL; AJ269477; CAB58119.1; -; mRNA.
DR   EMBL; AF098277; AAF22490.1; -; mRNA.
DR   EMBL; AF375875; AAK97398.1; -; Genomic_DNA.
DR   EMBL; AJ250807; CAC15384.1; -; mRNA.
DR   EMBL; AC135457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF458016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019225; AAH19225.1; -; mRNA.
DR   EMBL; BC050261; AAH50261.1; -; mRNA.
DR   CCDS; CCDS4212.1; -. [Q9UHI7-1]
DR   CCDS; CCDS4213.1; -. [Q9UHI7-2]
DR   PIR; JC7182; JC7182.
DR   RefSeq; NP_005838.3; NM_005847.4. [Q9UHI7-1]
DR   RefSeq; NP_689898.2; NM_152685.3. [Q9UHI7-2]
DR   AlphaFoldDB; Q9UHI7; -.
DR   SMR; Q9UHI7; -.
DR   BioGRID; 115288; 25.
DR   IntAct; Q9UHI7; 28.
DR   STRING; 9606.ENSP00000302851; -.
DR   ChEMBL; CHEMBL5209632; -.
DR   DrugBank; DB00126; Ascorbic acid.
DR   DrugCentral; Q9UHI7; -.
DR   GuidetoPHARMACOLOGY; 1041; -.
DR   TCDB; 2.A.40.6.5; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR   GlyCosmos; Q9UHI7; 2 sites, No reported glycans.
DR   GlyGen; Q9UHI7; 3 sites.
DR   iPTMnet; Q9UHI7; -.
DR   PhosphoSitePlus; Q9UHI7; -.
DR   BioMuta; SLC23A1; -.
DR   DMDM; 296452969; -.
DR   jPOST; Q9UHI7; -.
DR   MassIVE; Q9UHI7; -.
DR   PaxDb; 9606-ENSP00000302851; -.
DR   PeptideAtlas; Q9UHI7; -.
DR   ProteomicsDB; 84358; -. [Q9UHI7-1]
DR   ProteomicsDB; 84359; -. [Q9UHI7-2]
DR   ProteomicsDB; 84360; -. [Q9UHI7-3]
DR   Antibodypedia; 26736; 125 antibodies from 17 providers.
DR   DNASU; 9963; -.
DR   Ensembl; ENST00000348729.8; ENSP00000302701.4; ENSG00000170482.17. [Q9UHI7-1]
DR   Ensembl; ENST00000353963.7; ENSP00000302851.5; ENSG00000170482.17. [Q9UHI7-2]
DR   GeneID; 9963; -.
DR   KEGG; hsa:9963; -.
DR   MANE-Select; ENST00000348729.8; ENSP00000302701.4; NM_005847.5; NP_005838.3.
DR   UCSC; uc003leg.4; human. [Q9UHI7-1]
DR   AGR; HGNC:10974; -.
DR   CTD; 9963; -.
DR   DisGeNET; 9963; -.
DR   GeneCards; SLC23A1; -.
DR   HGNC; HGNC:10974; SLC23A1.
DR   HPA; ENSG00000170482; Group enriched (fallopian tube, intestine, kidney, liver).
DR   MIM; 603790; gene.
DR   neXtProt; NX_Q9UHI7; -.
DR   OpenTargets; ENSG00000170482; -.
DR   PharmGKB; PA35850; -.
DR   VEuPathDB; HostDB:ENSG00000170482; -.
DR   eggNOG; KOG1292; Eukaryota.
DR   GeneTree; ENSGT00950000182953; -.
DR   HOGENOM; CLU_017959_5_4_1; -.
DR   InParanoid; Q9UHI7; -.
DR   OMA; AHANSEM; -.
DR   OrthoDB; 911690at2759; -.
DR   PhylomeDB; Q9UHI7; -.
DR   TreeFam; TF313272; -.
DR   PathwayCommons; Q9UHI7; -.
DR   Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR   SignaLink; Q9UHI7; -.
DR   BioGRID-ORCS; 9963; 15 hits in 1143 CRISPR screens.
DR   ChiTaRS; SLC23A1; human.
DR   GeneWiki; SLC23A1; -.
DR   GenomeRNAi; 9963; -.
DR   Pharos; Q9UHI7; Tchem.
DR   PRO; PR:Q9UHI7; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UHI7; Protein.
DR   Bgee; ENSG00000170482; Expressed in ileal mucosa and 112 other cell types or tissues.
DR   ExpressionAtlas; Q9UHI7; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043229; C:intracellular organelle; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015143; F:urate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0070837; P:dehydroascorbic acid transport; IMP:UniProtKB.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
DR   GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0015851; P:nucleobase transport; TAS:ProtInc.
DR   GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR   InterPro; IPR006043; NCS2.
DR   PANTHER; PTHR11119:SF21; SOLUTE CARRIER FAMILY 23 MEMBER 1; 1.
DR   PANTHER; PTHR11119; XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER; 1.
DR   Pfam; PF00860; Xan_ur_permease; 1.
DR   Genevisible; Q9UHI7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..598
FT                   /note="Solute carrier family 23 member 1"
FT                   /id="PRO_0000165975"
FT   TOPO_DOM        1..52
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:19379732"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..159
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        230..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..358
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..426
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        479..490
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        512..598
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:19379732"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         591
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT   MOD_RES         596
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2J0"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19379732"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19379732"
FT   VAR_SEQ         92..430
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006813"
FT   VAR_SEQ         156
FT                   /note="V -> VGLHV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10556483,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_006814"
FT   VARIANT         218
FT                   /note="I -> V (in dbSNP:rs34521685)"
FT                   /id="VAR_053451"
FT   VARIANT         258
FT                   /note="M -> V (in dbSNP:rs35817838)"
FT                   /id="VAR_053452"
FT   VARIANT         264
FT                   /note="V -> M (in dbSNP:rs33972313)"
FT                   /id="VAR_053453"
FT   VARIANT         421
FT                   /note="A -> S (in dbSNP:rs6596474)"
FT                   /id="VAR_062111"
FT   CONFLICT        11
FT                   /note="T -> A (in Ref. 2; AAF24759)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..57
FT                   /note="YLTCFS -> IHDCLR (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..80
FT                   /note="DQHMVS -> SQTLHC (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="W -> S (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="I -> N (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="E -> D (in Ref. 2; AAF22490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182..183
FT                   /note="YI -> SL (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="A -> P (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="Y -> I (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="D -> E (in Ref. 2; AAF22490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="Y -> I (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        434
FT                   /note="T -> S (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451..452
FT                   /note="DM -> AL (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476..477
FT                   /note="ES -> SP (in Ref. 2; AAF22490)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        548
FT                   /note="I -> F (in Ref. 1; AAC78804)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   598 AA;  64815 MW;  939C52B9D1157029 CRC64;
     MRAQEDLEGR TQHETTRDPS TPLPTEPKFD MLYKIEDVPP WYLCILLGFQ HYLTCFSGTI
     AVPFLLAEAL CVGHDQHMVS QLIGTIFTCV GITTLIQTTV GIRLPLFQAS AFAFLVPAKA
     ILALERWKCP PEEEIYGNWS LPLNTSHIWH PRIREVQGAI MVSSVVEVVI GLLGLPGALL
     NYIGPLTVTP TVSLIGLSVF QAAGDRAGSH WGISACSILL IILFSQYLRN LTFLLPVYRW
     GKGLTLLRIQ IFKMFPIMLA IMTVWLLCYV LTLTDVLPTD PKAYGFQART DARGDIMAIA
     PWIRIPYPCQ WGLPTVTAAA VLGMFSATLA GIIESIGDYY ACARLAGAPP PPVHAINRGI
     FTEGICCIIA GLLGTGNGST SSSPNIGVLG ITKVGSRRVV QYGAAIMLVL GTIGKFTALF
     ASLPDPILGG MFCTLFGMIT AVGLSNLQFV DMNSSRNLFV LGFSMFFGLT LPNYLESNPG
     AINTGILEVD QILIVLLTTE MFVGGCLAFI LDNTVPGSPE ERGLIQWKAG AHANSDMSSS
     LKSYDFPIGM GIVKRITFLK YIPICPVFKG FSSSSKDQIA IPEDTPENTE TASVCTKV
//