S23A1_MOUSE
ID S23A1_MOUSE Reviewed; 605 AA.
AC Q9Z2J0; Q3TNA2; Q8C3M2; Q91WR7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Solute carrier family 23 member 1;
DE AltName: Full=Na(+)/L-ascorbic acid transporter 1;
DE AltName: Full=Sodium-dependent vitamin C transporter 1;
DE AltName: Full=Yolk sac permease-like molecule 3;
GN Name=Slc23a1; Synonyms=Svct1, Yspl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9804989; DOI=10.1016/s0167-4781(98)00151-1;
RA Faaland C.A., Race J.E., Ricken G., Warner F.J., Williams W.J.,
RA Holtzman E.J.;
RT "Molecular characterization of two novel transporters from human and mouse
RT kidney and from LLC-PK1 cells reveals a novel conserved family that is
RT homologous to bacterial and Aspergillus nucleobase transporters.";
RL Biochim. Biophys. Acta 1442:353-360(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-600 AND THR-603, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake
CC of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
CC {ECO:0000250|UniProtKB:Q9UHI7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9UHI7};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UHI7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UHI7}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UHI7}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; AF058318; AAC78805.1; -; mRNA.
DR EMBL; AK085499; BAC39457.1; -; mRNA.
DR EMBL; AK143959; BAE25631.1; -; mRNA.
DR EMBL; AK165439; BAE38187.1; -; mRNA.
DR EMBL; BC013528; AAH13528.1; -; mRNA.
DR CCDS; CCDS29144.1; -.
DR RefSeq; NP_035527.3; NM_011397.4.
DR RefSeq; XP_017173340.1; XM_017317851.1.
DR AlphaFoldDB; Q9Z2J0; -.
DR SMR; Q9Z2J0; -.
DR STRING; 10090.ENSMUSP00000025212; -.
DR GlyGen; Q9Z2J0; 2 sites.
DR iPTMnet; Q9Z2J0; -.
DR PhosphoSitePlus; Q9Z2J0; -.
DR SwissPalm; Q9Z2J0; -.
DR jPOST; Q9Z2J0; -.
DR MaxQB; Q9Z2J0; -.
DR PaxDb; Q9Z2J0; -.
DR PRIDE; Q9Z2J0; -.
DR ProteomicsDB; 253365; -.
DR Antibodypedia; 26736; 109 antibodies from 17 providers.
DR DNASU; 20522; -.
DR Ensembl; ENSMUST00000025212; ENSMUSP00000025212; ENSMUSG00000024354.
DR GeneID; 20522; -.
DR KEGG; mmu:20522; -.
DR UCSC; uc008eml.2; mouse.
DR CTD; 9963; -.
DR MGI; MGI:1341903; Slc23a1.
DR VEuPathDB; HostDB:ENSMUSG00000024354; -.
DR eggNOG; KOG1292; Eukaryota.
DR GeneTree; ENSGT00950000182953; -.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9Z2J0; -.
DR OMA; RKSAPFF; -.
DR OrthoDB; 387031at2759; -.
DR PhylomeDB; Q9Z2J0; -.
DR TreeFam; TF313272; -.
DR Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR BioGRID-ORCS; 20522; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc23a1; mouse.
DR PRO; PR:Q9Z2J0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9Z2J0; protein.
DR Bgee; ENSMUSG00000024354; Expressed in proximal tubule and 98 other tissues.
DR ExpressionAtlas; Q9Z2J0; baseline and differential.
DR Genevisible; Q9Z2J0; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008520; F:L-ascorbate:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0070837; P:dehydroascorbic acid transport; ISS:UniProtKB.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; ISS:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR029954; SLC23A1.
DR PANTHER; PTHR11119:SF21; PTHR11119:SF21; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..605
FT /note="Solute carrier family 23 member 1"
FT /id="PRO_0000165976"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 237..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 205
FT /note="S -> Y (in Ref. 1; AAC78805)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="C -> R (in Ref. 2; BAC39457)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..541
FT /note="AN -> PH (in Ref. 2; BAC39457)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="S -> F (in Ref. 2; BAC39457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 65554 MW; A3F64CB42DA1CFF5 CRC64;
MKTPEDPGSP KQHEVVDSAG TSTRDRQAPL PTEPKFDMLY KIEDVPPWYL CILLGFQHYL
TCFSGTIAVP FLLAEALCVG RDQHMVSQLI GTIFTCVGIT TLIQTTVGIR LPLFQASAFA
FLVPAKSILA LERWKCPSEE EIYGNWSMPL NTSHIWHPRI REVQGAIMVS SMVEVVIGLM
GLPGALLSYI GPLTVTPTVS LIGLSVFQAA GDRAGSHWGI SACSILLIVL FSQYLRNLTF
LLPVYRWGKG LTLFRVQIFK MFPIVLAIMT VWLLCYVLTL TDVLPADPTV YGFQARTDAR
GDIMAISPWI RIPYPCQWGL PTVTVAAVLG MFSATLAGII ESIGDYYACA RLAGAPPPPV
HAINRGIFTE GICCIIAGLL GTGNGSTSSS PNIGVLGITK VGSRRVVQYG AGIMLILGAI
GKFTALFASL PDPILGGMFC TLFGMITAVG LSNLQFVDMN SSRNLFVLGF SMFFGLTLPN
YLDSNPGAIN TGIPEVDQIL TVLLTTEMFV GGCLAFILDN TVPGSPEERG LIQWKAGAHA
NSETSASLKS YDFPFGMGMV KRTTFFRYIP ICPVFRGFSK KTQNQPPVLE DTPDNIETGS
VCTKV
