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Q9Z2J0 (S23A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1
Alternative name(s):
Na(+)/L-ascorbic acid transporter 1
Sodium-dependent vitamin C transporter 1
Yolk sac permease-like molecule 3
Gene names
Name:Slc23a1
Synonyms:Svct1, Yspl3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length605 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 By similarity.

Subcellular location

Cell membrane By similarity; Multi-pass membrane protein.

Sequence similarities

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

Ontologies

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

Inferred from direct assay PubMed 15333707PubMed 18668520. Source: UniProtKB

brain development

Inferred from mutant phenotype PubMed 11984597. Source: UniProtKB

dehydroascorbic acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

lung development

Inferred from mutant phenotype PubMed 11984597. Source: UniProtKB

response to toxic substance

Inferred from sequence or structural similarity. Source: UniProtKB

sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

transepithelial L-ascorbic acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

vitamin transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

basal plasma membrane

Inferred from direct assay PubMed 18668520. Source: UniProtKB

brush border

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 18668520. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular organelle

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionL-ascorbate:sodium symporter activity

Inferred from electronic annotation. Source: Ensembl

L-ascorbic acid transporter activity

Inferred from direct assay PubMed 15333707PubMed 18668520. Source: UniProtKB

dehydroascorbic acid transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

sodium ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

sodium-dependent L-ascorbate transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Solute carrier family 23 member 1
PRO_0000165976

Regions

Topological domain1 – 5959Cytoplasmic Potential
Transmembrane60 – 8021Helical; Potential
Topological domain81 – 888Extracellular Potential
Transmembrane89 – 10921Helical; Potential
Topological domain1101Cytoplasmic Potential
Transmembrane111 – 13121Helical; Potential
Topological domain132 – 16635Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 21427Cytoplasmic Potential
Transmembrane215 – 23218Helical; Potential
Topological domain233 – 2364Extracellular Potential
Intramembrane237 – 25014Helical; Potential
Topological domain251 – 2577Extracellular Potential
Transmembrane258 – 27821Helical; Potential
Topological domain279 – 31941Cytoplasmic Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 36525Extracellular Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 40923Cytoplasmic Potential
Transmembrane410 – 43021Helical; Potential
Topological domain431 – 4333Extracellular Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 46410Cytoplasmic Potential
Transmembrane465 – 48521Helical; Potential
Topological domain486 – 49712Extracellular Potential
Transmembrane498 – 51821Helical; Potential
Topological domain519 – 60587Cytoplasmic Potential

Amino acid modifications

Modified residue6031Phosphothreonine Ref.4
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2051S → Y in AAC78805. Ref.1
Sequence conflict2231C → R in BAC39457. Ref.2
Sequence conflict540 – 5412AN → PH in BAC39457. Ref.2
Sequence conflict5791S → F in BAC39457. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z2J0 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: A3F64CB42DA1CFF5

FASTA60565,554
        10         20         30         40         50         60 
MKTPEDPGSP KQHEVVDSAG TSTRDRQAPL PTEPKFDMLY KIEDVPPWYL CILLGFQHYL 

        70         80         90        100        110        120 
TCFSGTIAVP FLLAEALCVG RDQHMVSQLI GTIFTCVGIT TLIQTTVGIR LPLFQASAFA 

       130        140        150        160        170        180 
FLVPAKSILA LERWKCPSEE EIYGNWSMPL NTSHIWHPRI REVQGAIMVS SMVEVVIGLM 

       190        200        210        220        230        240 
GLPGALLSYI GPLTVTPTVS LIGLSVFQAA GDRAGSHWGI SACSILLIVL FSQYLRNLTF 

       250        260        270        280        290        300 
LLPVYRWGKG LTLFRVQIFK MFPIVLAIMT VWLLCYVLTL TDVLPADPTV YGFQARTDAR 

       310        320        330        340        350        360 
GDIMAISPWI RIPYPCQWGL PTVTVAAVLG MFSATLAGII ESIGDYYACA RLAGAPPPPV 

       370        380        390        400        410        420 
HAINRGIFTE GICCIIAGLL GTGNGSTSSS PNIGVLGITK VGSRRVVQYG AGIMLILGAI 

       430        440        450        460        470        480 
GKFTALFASL PDPILGGMFC TLFGMITAVG LSNLQFVDMN SSRNLFVLGF SMFFGLTLPN 

       490        500        510        520        530        540 
YLDSNPGAIN TGIPEVDQIL TVLLTTEMFV GGCLAFILDN TVPGSPEERG LIQWKAGAHA 

       550        560        570        580        590        600 
NSETSASLKS YDFPFGMGMV KRTTFFRYIP ICPVFRGFSK KTQNQPPVLE DTPDNIETGS 


VCTKV 

« 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].
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"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].
Tissue: Kidney.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF058318 mRNA. Translation: AAC78805.1.
AK085499 mRNA. Translation: BAC39457.1.
AK143959 mRNA. Translation: BAE25631.1.
AK165439 mRNA. Translation: BAE38187.1.
BC013528 mRNA. Translation: AAH13528.1.
RefSeqNP_035527.3. NM_011397.4.
UniGeneMm.22702.

3D structure databases

ProteinModelPortalQ9Z2J0.
SMRQ9Z2J0. Positions 42-477.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9Z2J0.

Proteomic databases

PaxDbQ9Z2J0.
PRIDEQ9Z2J0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025212; ENSMUSP00000025212; ENSMUSG00000024354.
GeneID20522.
KEGGmmu:20522.
UCSCuc008eml.2. mouse.

Organism-specific databases

CTD9963.
MGIMGI:1341903. Slc23a1.

Phylogenomic databases

eggNOGCOG2233.
GeneTreeENSGT00390000015686.
HOGENOMHOG000038201.
HOVERGENHBG056256.
InParanoidQ9Z2J0.
KOK14611.
OMALDRWKCP.
OrthoDBEOG7R56RZ.
PhylomeDBQ9Z2J0.
TreeFamTF313272.

Gene expression databases

ArrayExpressQ9Z2J0.
BgeeQ9Z2J0.
GenevestigatorQ9Z2J0.

Family and domain databases

InterProIPR006043. Xant/urac/vitC.
[Graphical view]
PANTHERPTHR11119. PTHR11119. 1 hit.
PfamPF00860. Xan_ur_permease. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC23A1. mouse.
NextBio298751.
PROQ9Z2J0.
SOURCESearch...

Entry information

Entry nameS23A1_MOUSE
AccessionPrimary (citable) accession number: Q9Z2J0
Secondary accession number(s): Q3TNA2, Q8C3M2, Q91WR7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot