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Solute carrier family 23 member 1 (Na( )/L-ascorbic acid transporter 1) (Sodium-dependent vitamin C transporter 1) (hSVCT1) (Yolk sac permease-like molecule 3)

 S23A1_HUMAN             Reviewed;         598 AA.
Q9UHI7; O95191; Q8WWB6; Q9UGH4; Q9UI39;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 157.
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; Expressed in 98 organ(s), highest expression level in right uterine tube.
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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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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