GENTAUR Molecular Products.

 S23A1_HUMAN             Reviewed;         598 AA.
 Q9UHI7; O95191; Q8WWB6; Q9UGH4; Q9UI39;
 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
 18-MAY-2010, sequence version 3.
 20-JUN-2018, entry version 156.
 RecName: Full=Solute carrier family 23 member 1;
 AltName: Full=Na(+)/L-ascorbic acid transporter 1;
 AltName: Full=Sodium-dependent vitamin C transporter 1;
          Short=hSVCT1;
 AltName: Full=Yolk sac permease-like molecule 3;
 Name=SLC23A1; Synonyms=SVCT1, YSPL3;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-421.
 TISSUE=Fetal liver, and Kidney;
 PubMed=9804989; DOI=10.1016/S0167-4781(98)00151-1;
 Faaland C.A., Race J.E., Ricken G., Warner F.J., Williams W.J.,
 Holtzman E.J.;
 "Molecular characterization of two novel transporters from human and
 mouse kidney and from LLC-PK1 cells reveals a novel conserved family
 that is homologous to bacterial and Aspergillus nucleobase
 transporters.";
 Biochim. Biophys. Acta 1442:353-360(1998).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ALA-421.
 TISSUE=Intestinal epithelium;
 PubMed=10556483; DOI=10.1016/S0005-2736(99)00182-0;
 Wang H., Dutta B., Huang W., Devoe L.D., Leibach F.H., Ganapathy V.,
 Prasad P.D.;
 "Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary
 structure, functional characteristics and evidence for a non-
 functional splice variant.";
 Biochim. Biophys. Acta 1461:1-9(1999).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-421.
 TISSUE=Kidney;
 PubMed=10556521; DOI=10.1016/S0014-5793(99)01393-9;
 Daruwala R.C., Song J., Koh W.S., Rumsey S.C., Levine M.;
 "Cloning and functional characterization of the human sodium-dependent
 vitamin C transporters hSVCT1 and hSVCT2.";
 FEBS Lett. 460:480-484(1999).
 [4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-421.
 TISSUE=Kidney;
 PubMed=10631088; DOI=10.1006/bbrc.1999.1929;
 Wang Y., Mackenzie B., Tsukaguchi H., Weremowicz S., Morton C.C.,
 Hediger M.A.;
 "Human vitamin C (L-ascorbic acid) transporter SVCT1.";
 Biochem. Biophys. Res. Commun. 267:488-494(2000).
 [5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-421.
 PubMed=11584081;
 Erichsen H.C., Eck P., Levine M., Chanock S.;
 "Characterization of the genomic structure of the human vitamin C
 transporter SVCT1 (SLC23A2).";
 J. Nutr. 131:2623-2627(2001).
 [6]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-421.
 TISSUE=Liver cancer;
 PubMed=11396616; DOI=10.1080/09687680110033774;
 Liang W.J., Johnson D., Jarvis S.M.;
 "Vitamin C transport systems of mammalian cells.";
 Mol. Membr. Biol. 18:87-95(2001).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15372022; DOI=10.1038/nature02919;
 Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
 Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
 She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
 Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
 Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
 Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
 Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
 Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
 Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
 Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
 Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
 Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
 Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
 Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
 "The DNA sequence and comparative analysis of human chromosome 5.";
 Nature 431:268-274(2004).
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
 ALA-421.
 TISSUE=Colon, and Kidney;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [9]
 GLYCOSYLATION AT ASN-138 AND ASN-144, SUBCELLULAR LOCATION, AND
 TOPOLOGY.
 PubMed=19379732; DOI=10.1016/j.yexcr.2009.04.007;
 Velho A.M., Jarvis S.M.;
 "Topological studies of hSVCT1, the human sodium-dependent vitamin C
 transporter and the influence of N-glycosylation on its intracellular
 targeting.";
 Exp. Cell Res. 315:2312-2321(2009).
 -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic
     uptake of vitamin C, with a stoichiometry of 2 Na(+) for each
     ascorbate.
 -!- INTERACTION:
     Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-1759386, EBI-10173507;
     O43865:AHCYL1; NbExp=3; IntAct=EBI-1759386, EBI-2371423;
     Q15323:KRT31; NbExp=3; IntAct=EBI-1759386, EBI-948001;
     P60370:KRTAP10-5; NbExp=3; IntAct=EBI-1759386, EBI-10172150;
     P60409:KRTAP10-7; NbExp=3; IntAct=EBI-1759386, EBI-10172290;
     P60410:KRTAP10-8; NbExp=3; IntAct=EBI-1759386, EBI-10171774;
     P60411:KRTAP10-9; NbExp=3; IntAct=EBI-1759386, EBI-10172052;
     Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-1759386, EBI-10172511;
     Q5JR59:MTUS2; NbExp=3; IntAct=EBI-1759386, EBI-742948;
     P16333:NCK1; NbExp=2; IntAct=EBI-1759386, EBI-389883;
     Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-1759386, EBI-945833;
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19379732};
     Multi-pass membrane protein {ECO:0000269|PubMed:19379732}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
       Comment=Experimental confirmation may be lacking for some
       isoforms.;
     Name=1;
       IsoId=Q9UHI7-1; Sequence=Displayed;
     Name=2;
       IsoId=Q9UHI7-2; Sequence=VSP_006814;
       Note=Inactive.;
     Name=3;
       IsoId=Q9UHI7-3; Sequence=VSP_006813;
 -!- TISSUE SPECIFICITY: Highly expressed in adult small intestine,
     kidney, thymus, ovary, colon, prostate and liver, and in fetal
     kidney, liver and thymus.
 -!- PTM: Phosphorylated. {ECO:0000305}.
 -!- MISCELLANEOUS: Treatment with the protein kinase C stimulator PMA
     results in a 10-fold decrease in ascorbate accumulation in
     transfected cells.
 -!- SIMILARITY: Belongs to the xanthine/uracil permease family.
     Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily.
     {ECO:0000305}.
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 EMBL; AF058317; AAC78804.1; -; mRNA.
 EMBL; AF170911; AAF24759.1; -; mRNA.
 EMBL; AJ269477; CAB58119.1; -; mRNA.
 EMBL; AF098277; AAF22490.1; -; mRNA.
 EMBL; AF375875; AAK97398.1; -; Genomic_DNA.
 EMBL; AJ250807; CAC15384.1; -; mRNA.
 EMBL; AC135457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC019225; AAH19225.1; -; mRNA.
 EMBL; BC050261; AAH50261.1; -; mRNA.
 CCDS; CCDS4212.1; -. [Q9UHI7-1]
 CCDS; CCDS4213.1; -. [Q9UHI7-2]
 PIR; JC7182; JC7182.
 RefSeq; NP_005838.3; NM_005847.4.
 RefSeq; NP_689898.2; NM_152685.3.
 UniGene; Hs.643467; -.
 ProteinModelPortal; Q9UHI7; -.
 BioGrid; 115288; 12.
 IntAct; Q9UHI7; 24.
 STRING; 9606.ENSP00000302851; -.
 DrugBank; DB00126; Vitamin C.
 GuidetoPHARMACOLOGY; 1041; -.
 TCDB; 2.A.40.6.5; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
 iPTMnet; Q9UHI7; -.
 PhosphoSitePlus; Q9UHI7; -.
 BioMuta; SLC23A1; -.
 DMDM; 296452969; -.
 PaxDb; Q9UHI7; -.
 PeptideAtlas; Q9UHI7; -.
 PRIDE; Q9UHI7; -.
 ProteomicsDB; 84358; -.
 ProteomicsDB; 84359; -. [Q9UHI7-2]
 ProteomicsDB; 84360; -. [Q9UHI7-3]
 Ensembl; ENST00000348729; ENSP00000302701; ENSG00000170482.
 Ensembl; ENST00000353963; ENSP00000302851; ENSG00000170482.
 GeneID; 9963; -.
 KEGG; hsa:9963; -.
 UCSC; uc003leg.4; human. [Q9UHI7-1]
 CTD; 9963; -.
 DisGeNET; 9963; -.
 EuPathDB; HostDB:ENSG00000170482.16; -.
 GeneCards; SLC23A1; -.
 HGNC; HGNC:10974; SLC23A1.
 HPA; HPA047612; -.
 MIM; 603790; gene.
 neXtProt; NX_Q9UHI7; -.
 PharmGKB; PA35850; -.
 eggNOG; KOG1292; Eukaryota.
 eggNOG; COG2233; LUCA.
 HOGENOM; HOG000038201; -.
 HOVERGEN; HBG056256; -.
 InParanoid; Q9UHI7; -.
 KO; K14611; -.
 OrthoDB; EOG091G063Y; -.
 PhylomeDB; Q9UHI7; -.
 TreeFam; TF313272; -.
 Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
 GeneWiki; SLC23A1; -.
 GenomeRNAi; 9963; -.
 PRO; PR:Q9UHI7; -.
 Proteomes; UP000005640; Chromosome 5.
 Bgee; ENSG00000170482; -.
 CleanEx; HS_SLC23A1; -.
 ExpressionAtlas; Q9UHI7; baseline and differential.
 Genevisible; Q9UHI7; HS.
 GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
 GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
 GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
 GO; GO:0043229; C:intracellular organelle; IDA:UniProtKB.
 GO; GO:0016020; C:membrane; TAS:ProtInc.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IMP:UniProtKB.
 GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IDA:UniProtKB.
 GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
 GO; GO:0015205; F:nucleobase transmembrane transporter activity; TAS:ProtInc.
 GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB.
 GO; GO:0070890; F:sodium-dependent L-ascorbate transmembrane transporter activity; IDA:UniProtKB.
 GO; GO:0007420; P:brain development; ISS:UniProtKB.
 GO; GO:0070837; P:dehydroascorbic acid transport; IMP:UniProtKB.
 GO; GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.
 GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
 GO; GO:0030324; P:lung development; IEA:Ensembl.
 GO; GO:0015851; P:nucleobase transport; TAS:ProtInc.
 GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
 GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
 GO; GO:0070904; P:transepithelial L-ascorbic acid transport; IDA:UniProtKB.
 InterPro; IPR029954; SLC23A1.
 InterPro; IPR006043; Xant/urac/vitC.
 PANTHER; PTHR11119:SF21; PTHR11119:SF21; 1.
 Pfam; PF00860; Xan_ur_permease; 1.
 1: Evidence at protein level;
 Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
 Ion transport; Membrane; Phosphoprotein; Polymorphism;
 Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
 Transmembrane helix; Transport.
 CHAIN         1    598       Solute carrier family 23 member 1.
                              /FTId=PRO_0000165975.
 TOPO_DOM      1     52       Cytoplasmic. {ECO:0000255}.
 TRANSMEM     53     73       Helical. {ECO:0000255}.
 TOPO_DOM     74     81       Extracellular. {ECO:0000255}.
 TRANSMEM     82    102       Helical. {ECO:0000255}.
 TOPO_DOM    103    103       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    104    124       Helical. {ECO:0000255}.
 TOPO_DOM    125    159       Extracellular. {ECO:0000255}.
 TRANSMEM    160    180       Helical. {ECO:0000255}.
 TOPO_DOM    181    207       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    208    225       Helical. {ECO:0000255}.
 TOPO_DOM    226    229       Extracellular. {ECO:0000255}.
 INTRAMEM    230    243       Helical. {ECO:0000255}.
 TOPO_DOM    244    250       Extracellular. {ECO:0000255}.
 TRANSMEM    251    271       Helical. {ECO:0000255}.
 TOPO_DOM    272    312       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    313    333       Helical. {ECO:0000255}.
 TOPO_DOM    334    358       Extracellular. {ECO:0000255}.
 TRANSMEM    359    379       Helical. {ECO:0000255}.
 TOPO_DOM    380    402       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    403    423       Helical. {ECO:0000255}.
 TOPO_DOM    424    426       Extracellular. {ECO:0000255}.
 TRANSMEM    427    447       Helical. {ECO:0000255}.
 TOPO_DOM    448    457       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    458    478       Helical. {ECO:0000255}.
 TOPO_DOM    479    490       Extracellular. {ECO:0000255}.
 TRANSMEM    491    511       Helical. {ECO:0000255}.
 TOPO_DOM    512    598       Cytoplasmic. {ECO:0000255}.
 MOD_RES     591    591       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q9Z2J0}.
 MOD_RES     593    593       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9Z2J0}.
 MOD_RES     596    596       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q9Z2J0}.
 CARBOHYD    138    138       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19379732}.
 CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:19379732}.
 VAR_SEQ      92    430       Missing (in isoform 3).
                              {ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_006813.
 VAR_SEQ     156    156       V -> VGLHV (in isoform 2).
                              {ECO:0000303|PubMed:10556483,
                              ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_006814.
 VARIANT     218    218       I -> V (in dbSNP:rs34521685).
                              /FTId=VAR_053451.
 VARIANT     258    258       M -> V (in dbSNP:rs35817838).
                              /FTId=VAR_053452.
 VARIANT     264    264       V -> M (in dbSNP:rs33972313).
                              /FTId=VAR_053453.
 VARIANT     421    421       S -> A (in dbSNP:rs6596474).
                              {ECO:0000269|PubMed:10556483,
                              ECO:0000269|PubMed:10556521,
                              ECO:0000269|PubMed:10631088,
                              ECO:0000269|PubMed:11396616,
                              ECO:0000269|PubMed:11584081,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:9804989}.
                              /FTId=VAR_062111.
 CONFLICT     11     11       T -> A (in Ref. 2; AAF24759).
                              {ECO:0000305}.
 CONFLICT     52     57       YLTCFS -> IHDCLR (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT     75     80       DQHMVS -> SQTLHC (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    139    139       W -> S (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    153    153       I -> N (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    155    155       E -> D (in Ref. 2; AAF22490).
                              {ECO:0000305}.
 CONFLICT    182    183       YI -> SL (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    207    207       A -> P (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    269    269       Y -> I (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    275    275       D -> E (in Ref. 2; AAF22490).
                              {ECO:0000305}.
 CONFLICT    284    284       Y -> I (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    434    434       T -> S (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    451    452       DM -> AL (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 CONFLICT    476    477       ES -> SP (in Ref. 2; AAF22490).
                              {ECO:0000305}.
 CONFLICT    548    548       I -> F (in Ref. 1; AAC78804).
                              {ECO:0000305}.
 SEQUENCE   598 AA;  64831 MW;  1191B2B43CE76FD6 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
 SSLPDPILGG MFCTLFGMIT AVGLSNLQFV DMNSSRNLFV LGFSMFFGLT LPNYLESNPG
 AINTGILEVD QILIVLLTTE MFVGGCLAFI LDNTVPGSPE ERGLIQWKAG AHANSDMSSS
 LKSYDFPIGM GIVKRITFLK YIPICPVFKG FSSSSKDQIA IPEDTPENTE TASVCTKV

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