ID S23A2_RAT Reviewed; 647 AA.
AC Q9WTW8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Solute carrier family 23 member 2;
DE AltName: Full=Na(+)/L-ascorbic acid transporter 2;
DE AltName: Full=Sodium-dependent vitamin C transporter 2 {ECO:0000303|PubMed:10331392};
GN Name=Slc23a2; Synonyms=Svct2 {ECO:0000303|PubMed:10331392};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=10331392; DOI=10.1038/19986;
RA Tsukaguchi H., Tokui T., Mackenzie B., Berger U.V., Chen X.-Z., Wang Y.,
RA Brubaker R.F., Hediger M.A.;
RT "A family of mammalian Na+-dependent L-ascorbic acid transporters.";
RL Nature 399:70-75(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-80, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sodium/ascorbate cotransporter (PubMed:10331392). Mediates
CC electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for
CC each ascorbate (By similarity). {ECO:0000250|UniProtKB:Q9UGH3,
CC ECO:0000269|PubMed:10331392}.
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:Q9UGH3};
CC -!- SUBUNIT: Interacts with CLSTN3. {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10331392};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- TISSUE SPECIFICITY: Highly expressed in neural, neuroendocrine,
CC exocrine and endothelial tissues and in osteoblasts. Detected in
CC neurons throughout the central nervous system, in meninges and choroid
CC plexus, in the anterior pituitary, the intermediate lobe, in pancreas,
CC adrenal cortex, gastric glands, and in the inner nuclear layer of the
CC retina. {ECO:0000269|PubMed:10331392}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UGH3}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30368.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF080453; AAD30368.1; ALT_INIT; mRNA.
DR RefSeq; NP_059012.2; NM_017316.2.
DR RefSeq; XP_006235129.1; XM_006235067.3.
DR RefSeq; XP_006235130.1; XM_006235068.3.
DR AlphaFoldDB; Q9WTW8; -.
DR SMR; Q9WTW8; -.
DR STRING; 10116.ENSRNOP00000028885; -.
DR GlyCosmos; Q9WTW8; 2 sites, No reported glycans.
DR GlyGen; Q9WTW8; 2 sites.
DR iPTMnet; Q9WTW8; -.
DR PhosphoSitePlus; Q9WTW8; -.
DR SwissPalm; Q9WTW8; -.
DR PaxDb; 10116-ENSRNOP00000028885; -.
DR Ensembl; ENSRNOT00000028885.5; ENSRNOP00000028885.2; ENSRNOG00000021262.6.
DR Ensembl; ENSRNOT00055009470; ENSRNOP00055007285; ENSRNOG00055005858.
DR Ensembl; ENSRNOT00060003211; ENSRNOP00060002189; ENSRNOG00060002051.
DR Ensembl; ENSRNOT00065022743; ENSRNOP00065017639; ENSRNOG00065013821.
DR GeneID; 50622; -.
DR KEGG; rno:50622; -.
DR UCSC; RGD:619876; rat.
DR AGR; RGD:619876; -.
DR CTD; 9962; -.
DR RGD; 619876; Slc23a2.
DR eggNOG; KOG1292; Eukaryota.
DR GeneTree; ENSGT00950000182953; -.
DR HOGENOM; CLU_017959_5_4_1; -.
DR InParanoid; Q9WTW8; -.
DR OMA; NVSAYCR; -.
DR OrthoDB; 911690at2759; -.
DR PhylomeDB; Q9WTW8; -.
DR TreeFam; TF313272; -.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR PRO; PR:Q9WTW8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021262; Expressed in stomach and 19 other cell types or tissues.
DR Genevisible; Q9WTW8; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IDA:RGD.
DR GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IMP:RGD.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR006042; Xan_ur_permease.
DR PANTHER; PTHR11119:SF33; SOLUTE CARRIER FAMILY 23 MEMBER 2; 1.
DR PANTHER; PTHR11119; XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..647
FT /note="Solute carrier family 23 member 2"
FT /id="PRO_0000165980"
FT TOPO_DOM 8..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 286..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..544
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPR4"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 647 AA; 70070 MW; 623AF185769F135E CRC64;
MMGVGKNTSK SVEVGGSTEG KYEEEAKRPD FFTLPVVING GATSSGEQDN EDTELMAIYT
TENGIAEKSS LAETLDSTGS LDPQRSDMIY TIEDVPPWYL CIFLGLQHYL TCFSGTIAVP
FLLADAMCVG DDQWATSQLI GTIFFCVGIT TLLQTTFGCR LPLFQASAFA FLAPARAILS
LDKWKCNTTE ITVANGTAEL LEHIWHPRIQ EIQGAIIMSS LIEVVIGLLG LPGALLRYIG
PLTITPTVAL IGLSGFQAAG ERAGKHWGIA MLTIFLVLLF SQYARNVKFP LPIYKSKKGW
TAYKLQLFKM FPIILAILVS WLLCFIFTVT DVFPSNSTDY GYYARTDARK GVLLVAPWFK
VPYPFQWGMP TVSAAGVIGM LSAVVASIIE SIGDYYACAR LSCAPPPPIH AINRGIFVEG
LSCVLDGVFG TGNGSTSSSP NIGVLGITKV GSRRVIQYGA ALMLGLGMIG KFSALFASLP
DPVLGALFCT LFGMITAVGL SNLQFIDLNS SRNLFVLGFS IFFGLVLPSY LRQNPLVTGI
TGIDQVLNVL LTTAMFVGGC VAFILDNTIP GTPEERGIKK WKKGVSKGNK SLDGMESYNL
PFGMNIIKKY RCFSYLPISP TFAGYTWKGF GKSENRRSSD KDSQATV
//
