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Protein

Solute carrier family 23 member 1

Gene

Slc23a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. dehydroascorbic acid transporter activity Source: UniProtKB
  2. L-ascorbate:sodium symporter activity Source: MGI
  3. L-ascorbic acid transporter activity Source: UniProtKB
  4. sodium-dependent L-ascorbate transmembrane transporter activity Source: UniProtKB
  5. sodium ion transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. dehydroascorbic acid transport Source: UniProtKB
  3. L-ascorbic acid transport Source: UniProtKB
  4. lung development Source: UniProtKB
  5. response to toxic substance Source: UniProtKB
  6. sodium ion transmembrane transport Source: MGI
  7. sodium ion transport Source: UniProtKB
  8. transepithelial L-ascorbic acid transport Source: UniProtKB
  9. vitamin transmembrane transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiREACT_287684. Vitamin C (ascorbate) metabolism.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Slc23a1
Synonyms:Svct1, Yspl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1341903. Slc23a1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5959CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei60 – 8021HelicalSequence AnalysisAdd
BLAST
Topological domaini81 – 888ExtracellularSequence Analysis
Transmembranei89 – 10921HelicalSequence AnalysisAdd
BLAST
Topological domaini110 – 1101CytoplasmicSequence Analysis
Transmembranei111 – 13121HelicalSequence AnalysisAdd
BLAST
Topological domaini132 – 16635ExtracellularSequence AnalysisAdd
BLAST
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Topological domaini188 – 21427CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei215 – 23218HelicalSequence AnalysisAdd
BLAST
Topological domaini233 – 2364ExtracellularSequence Analysis
Intramembranei237 – 25014HelicalSequence AnalysisAdd
BLAST
Topological domaini251 – 2577ExtracellularSequence Analysis
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Topological domaini279 – 31941CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence AnalysisAdd
BLAST
Topological domaini341 – 36525ExtracellularSequence AnalysisAdd
BLAST
Transmembranei366 – 38621HelicalSequence AnalysisAdd
BLAST
Topological domaini387 – 40923CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei410 – 43021HelicalSequence AnalysisAdd
BLAST
Topological domaini431 – 4333ExtracellularSequence Analysis
Transmembranei434 – 45421HelicalSequence AnalysisAdd
BLAST
Topological domaini455 – 46410CytoplasmicSequence Analysis
Transmembranei465 – 48521HelicalSequence AnalysisAdd
BLAST
Topological domaini486 – 49712ExtracellularSequence AnalysisAdd
BLAST
Transmembranei498 – 51821HelicalSequence AnalysisAdd
BLAST
Topological domaini519 – 60587CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basal plasma membrane Source: UniProtKB
  3. brush border Source: Ensembl
  4. cytoplasm Source: UniProtKB
  5. extracellular vesicular exosome Source: MGI
  6. integral component of membrane Source: UniProtKB-KW
  7. intracellular organelle Source: UniProtKB
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Solute carrier family 23 member 1PRO_0000165976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Modified residuei603 – 6031Phosphothreonine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Z2J0.
PaxDbiQ9Z2J0.
PRIDEiQ9Z2J0.

PTM databases

PhosphoSiteiQ9Z2J0.

Expressioni

Gene expression databases

BgeeiQ9Z2J0.
ExpressionAtlasiQ9Z2J0. baseline and differential.
GenevestigatoriQ9Z2J0.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2J0.
SMRiQ9Z2J0. Positions 42-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2233.
GeneTreeiENSGT00390000015686.
HOGENOMiHOG000038201.
HOVERGENiHBG056256.
InParanoidiQ9Z2J0.
KOiK14611.
OMAiKWRCPPE.
OrthoDBiEOG7R56RZ.
PhylomeDBiQ9Z2J0.
TreeFamiTF313272.

Family and domain databases

InterProiIPR029954. SLC23A1.
IPR006043. Xant/urac/vitC.
[Graphical view]
PANTHERiPTHR11119. PTHR11119. 1 hit.
PTHR11119:SF21. PTHR11119:SF21. 1 hit.
PfamiPF00860. Xan_ur_permease. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2J0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPEDPGSP KQHEVVDSAG TSTRDRQAPL PTEPKFDMLY KIEDVPPWYL
60 70 80 90 100
CILLGFQHYL TCFSGTIAVP FLLAEALCVG RDQHMVSQLI GTIFTCVGIT
110 120 130 140 150
TLIQTTVGIR LPLFQASAFA FLVPAKSILA LERWKCPSEE EIYGNWSMPL
160 170 180 190 200
NTSHIWHPRI REVQGAIMVS SMVEVVIGLM GLPGALLSYI GPLTVTPTVS
210 220 230 240 250
LIGLSVFQAA GDRAGSHWGI SACSILLIVL FSQYLRNLTF LLPVYRWGKG
260 270 280 290 300
LTLFRVQIFK MFPIVLAIMT VWLLCYVLTL TDVLPADPTV YGFQARTDAR
310 320 330 340 350
GDIMAISPWI RIPYPCQWGL PTVTVAAVLG MFSATLAGII ESIGDYYACA
360 370 380 390 400
RLAGAPPPPV HAINRGIFTE GICCIIAGLL GTGNGSTSSS PNIGVLGITK
410 420 430 440 450
VGSRRVVQYG AGIMLILGAI GKFTALFASL PDPILGGMFC TLFGMITAVG
460 470 480 490 500
LSNLQFVDMN SSRNLFVLGF SMFFGLTLPN YLDSNPGAIN TGIPEVDQIL
510 520 530 540 550
TVLLTTEMFV GGCLAFILDN TVPGSPEERG LIQWKAGAHA NSETSASLKS
560 570 580 590 600
YDFPFGMGMV KRTTFFRYIP ICPVFRGFSK KTQNQPPVLE DTPDNIETGS

VCTKV
Length:605
Mass (Da):65,554
Last modified:October 19, 2002 - v2
Checksum:iA3F64CB42DA1CFF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051S → Y in AAC78805 (PubMed:9804989).Curated
Sequence conflicti223 – 2231C → R in BAC39457 (PubMed:16141072).Curated
Sequence conflicti540 – 5412AN → PH in BAC39457 (PubMed:16141072).Curated
Sequence conflicti579 – 5791S → F in BAC39457 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29144.1.
RefSeqiNP_035527.3. NM_011397.4.
UniGeneiMm.22702.

Genome annotation databases

EnsembliENSMUST00000025212; ENSMUSP00000025212; ENSMUSG00000024354.
GeneIDi20522.
KEGGimmu:20522.
UCSCiuc008eml.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29144.1.
RefSeqiNP_035527.3. NM_011397.4.
UniGeneiMm.22702.

3D structure databases

ProteinModelPortaliQ9Z2J0.
SMRiQ9Z2J0. Positions 42-477.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9Z2J0.

Proteomic databases

MaxQBiQ9Z2J0.
PaxDbiQ9Z2J0.
PRIDEiQ9Z2J0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025212; ENSMUSP00000025212; ENSMUSG00000024354.
GeneIDi20522.
KEGGimmu:20522.
UCSCiuc008eml.2. mouse.

Organism-specific databases

CTDi9963.
MGIiMGI:1341903. Slc23a1.

Phylogenomic databases

eggNOGiCOG2233.
GeneTreeiENSGT00390000015686.
HOGENOMiHOG000038201.
HOVERGENiHBG056256.
InParanoidiQ9Z2J0.
KOiK14611.
OMAiKWRCPPE.
OrthoDBiEOG7R56RZ.
PhylomeDBiQ9Z2J0.
TreeFamiTF313272.

Enzyme and pathway databases

ReactomeiREACT_287684. Vitamin C (ascorbate) metabolism.

Miscellaneous databases

ChiTaRSiSlc23a1. mouse.
NextBioi298751.
PROiQ9Z2J0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2J0.
ExpressionAtlasiQ9Z2J0. baseline and differential.
GenevestigatoriQ9Z2J0.

Family and domain databases

InterProiIPR029954. SLC23A1.
IPR006043. Xant/urac/vitC.
[Graphical view]
PANTHERiPTHR11119. PTHR11119. 1 hit.
PTHR11119:SF21. PTHR11119:SF21. 1 hit.
PfamiPF00860. Xan_ur_permease. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiS23A1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2J0
Secondary accession number(s): Q3TNA2, Q8C3M2, Q91WR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: April 1, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.