Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9UGH3 (S23A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 23 member 2
Alternative name(s):
Na(+)/L-ascorbic acid transporter 2
Nucleobase transporter-like 1 protein
Sodium-dependent vitamin C transporter 2
Short name=hSVCT2
Yolk sac permease-like molecule 2
Gene names
Name:SLC23A2
Synonyms:KIAA0238, NBTL1, SLC23A1, SVCT2, YSPL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na+ for each ascorbate.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated Probable.

Sequence similarities

Belongs to the xanthine/uracil permease family. Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily. [View classification]

Sequence caution

The sequence BAA13244.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Symport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandSodium
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid metabolic process

Non-traceable author statement Ref.3. Source: UniProtKB

molecular hydrogen transport

Non-traceable author statement Ref.2. Source: UniProtKB

nucleobase-containing compound metabolic process

Traceable author statement Ref.1. Source: ProtInc

response to oxidative stress

Inferred from electronic annotation. Source: Compara

transepithelial L-ascorbic acid transport

Inferred from direct assay PubMed 18417304. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 18417304. Source: UniProtKB

basal plasma membrane

Inferred from electronic annotation. Source: Compara

basolateral plasma membrane

Inferred from direct assay PubMed 15993839PubMed 18247577PubMed 18417304PubMed 19216494. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: Compara

integral to plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionL-ascorbate:sodium symporter activity

Inferred from electronic annotation. Source: Compara

nucleobase transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

sodium-dependent L-ascorbate transmembrane transporter activity

Inferred from direct assay PubMed 10631088PubMed 15993839. Source: UniProtKB

sodium-dependent multivitamin transmembrane transporter activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650Solute carrier family 23 member 2
PRO_0000165978

Regions

Transmembrane103 – 12321Helical; Potential
Transmembrane140 – 16021Helical; Potential
Transmembrane162 – 18221Helical; Potential
Transmembrane219 – 23921Helical; Potential
Transmembrane242 – 26221Helical; Potential
Transmembrane267 – 28721Helical; Potential
Transmembrane313 – 33321Helical; Potential
Transmembrane372 – 39221Helical; Potential
Transmembrane462 – 48221Helical; Potential
Transmembrane486 – 50621Helical; Potential
Transmembrane514 – 53421Helical; Potential
Transmembrane548 – 56821Helical; Potential

Amino acid modifications

Modified residue781Phosphoserine By similarity
Modified residue791Phosphothreonine By similarity
Modified residue811Phosphoserine Ref.11
Modified residue6491Phosphothreonine By similarity
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict301P → R in AAD11783. Ref.4
Sequence conflict1411I → T in AAD11783. Ref.4
Sequence conflict1671A → T in AAC78806. Ref.1
Sequence conflict1821L → S in AAD11783. Ref.4
Sequence conflict2151I → V in AAD11783. Ref.4
Sequence conflict3141F → L in CAC83100. Ref.5
Sequence conflict418 – 4247GIFVEGL → YVPEKTS Ref.10

Sequences

Sequence LengthMass (Da)Tools
Q9UGH3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 28C9E190D9528D39

FASTA65070,337
        10         20         30         40         50         60 
MMGIGKNTTS KSMEAGSSTE GKYEDEAKHP AFFTLPVVIN GGATSSGEQD NEDTELMAIY 

        70         80         90        100        110        120 
TTENGIAEKS SLAETLDSTG SLDPQRSDMI YTIEDVPPWY LCIFLGLQHY LTCFSGTIAV 

       130        140        150        160        170        180 
PFLLADAMCV GYDQWATSQL IGTIFFCVGI TTLLQTTFGC RLPLFQASAF AFLAPARAIL 

       190        200        210        220        230        240 
SLDKWKCNTT DVSVANGTAE LLHTEHIWYP RIREIQGAII MSSLIEVVIG LLGLPGALLK 

       250        260        270        280        290        300 
YIGPLTITPT VALIGLSGFQ AAGERAGKHW GIAMLTIFLV LLFSQYARNV KFPLPIYKSK 

       310        320        330        340        350        360 
KGWTAYKLQL FKMFPIILAI LVSWLLCFIF TVTDVFPPDS TKYGFYARTD ARQGVLLVAP 

       370        380        390        400        410        420 
WFKVPYPFQW GLPTVSAAGV IGMLSAVVAS IIESIGDYYA CARLSCAPPP PIHAINRGIF 

       430        440        450        460        470        480 
VEGLSCVLDG IFGTGNGSTS SSPNIGVLGI TKVGSRRVIQ CGAALMLALG MIGKFSALFA 

       490        500        510        520        530        540 
SLPDPVLGAL FCTLFGMITA VGLSNLQFID LNSSRNLFVL GFSIFFGLVL PSYLRQNPLV 

       550        560        570        580        590        600 
TGITGIDQVL NVLLTTAMFV GGCVAFILDN TIPGTPEERG IRKWKKGVGK GNKSLDGMES 

       610        620        630        640        650 
YNLPFGMNII KKYRCFSYLP ISPTFVGYTW KGLRKSDNSR SSDEDSQATG 

« Hide

References

« Hide 'large scale' references
[1]"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."
Faaland C.A., Race J.E., Ricken G., Warner F.J., Williams W.J., Holtzman E.J.
Biochim. Biophys. Acta 1442:353-360(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Human placental sodium-dependent vitamin C transporter (SVCT2): molecular cloning and transport function."
Rajan D.P., Huang W., Dutta B., Devoe L.D., Leibach F.H., Ganapathy V., Prasad P.D.
Biochem. Biophys. Res. Commun. 262:762-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Choriocarcinoma.
[3]"Cloning and functional characterization of the human sodium-dependent vitamin C transporters hSVCT1 and hSVCT2."
Daruwala R.C., Song J., Koh W.S., Rumsey S.C., Levine M.
FEBS Lett. 460:480-484(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[4]"A human nucleobase transporter-like cDNA (SLC23A1): member of a transporter family conserved from bacteria to mammals."
Hogue D.L., Ling V.
Genomics 59:18-23(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[5]"Vitamin C transport systems of mammalian cells."
Liang W.J., Johnson D., Jarvis S.M.
Mol. Membr. Biol. 18:87-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[6]"SVCT2 in ciliated human tracheal epithelial cultures."
Schwarzer C., Borcanski G., Widdicombe J., Fischer H., Illek B.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Trachea.
[7]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[9]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-424.
Tissue: Skin.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF058319 mRNA. Translation: AAC78806.1.
AJ269478 mRNA. Translation: CAB58120.1.
AF164142 mRNA. Translation: AAF80493.1.
AF092511 mRNA. Translation: AAD11783.1.
AJ292318 mRNA. Translation: CAC83100.1.
AY380556 mRNA. Translation: AAQ79775.1.
D87075 mRNA. Translation: BAA13244.2. Different initiation.
AL389886 Genomic DNA. Translation: CAC16126.1.
BC013112 mRNA. Translation: AAH13112.1.
IPIIPI00295774.
PIRJC7095.
RefSeqNP_005107.4. NM_005116.5.
NP_976072.1. NM_203327.1.
UniGeneHs.516866.

3D structure databases

ProteinModelPortalQ9UGH3.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UGH3. 1 interaction.

Protein family/group databases

TCDB2.A.40.6.2. nucleobase:cation symporter-2 (NCS2) family.

PTM databases

PhosphoSiteQ9UGH3.

Polymorphism databases

DMDM24212469.

Proteomic databases

PaxDbQ9UGH3.
PRIDEQ9UGH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338244; ENSP00000344322; ENSG00000089057.
ENST00000379333; ENSP00000368637; ENSG00000089057.
GeneID9962.
KEGGhsa:9962.
UCSCuc002wlg.1. human.

Organism-specific databases

CTD9962.
GeneCardsGC20M004781.
HGNCHGNC:10973. SLC23A2.
HPAHPA052825.
MIM603791. gene.
neXtProtNX_Q9UGH3.
PharmGKBPA35849.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2233.
HOVERGENHBG056256.
InParanoidQ9UGH3.
KOK14611.
OMALEKWKCN.
OrthoDBEOG4JHCF8.
PhylomeDBQ9UGH3.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9UGH3.
BgeeQ9UGH3.
CleanExHS_SLC23A1.
HS_SLC23A2.
GenevestigatorQ9UGH3.
GermOnlineENSG00000089057. Homo sapiens.

Family and domain databases

InterProIPR006042. Xan_ur_permease.
IPR006043. Xant/urac/vitC.
[Graphical view]
PANTHERPTHR11119. PTHR11119. 1 hit.
PfamPF00860. Xan_ur_permease. 1 hit.
[Graphical view]
PROSITEPS01116. XANTH_URACIL_PERMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL3271.
ChiTaRSSLC23A2. human.
GenomeRNAi9962.
NextBio37592.
SOURCESearch...

Entry information

Entry nameS23A2_HUMAN
AccessionPrimary (citable) accession number: Q9UGH3
Secondary accession number(s): Q8WWR4 expand/collapse secondary AC list , Q92512, Q96D54, Q9UNU1, Q9UP85
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families