ID S13A3_HUMAN Reviewed; 602 AA. AC Q8WWT9; B4DIR8; E1P5U4; F6WI18; Q5JYC9; Q5JYD0; Q5JYD1; Q5TCQ2; Q8IVB1; AC Q8N8K4; Q96MM5; Q9BR25; Q9H1G1; Q9H3W4; Q9NQN5; Q9NS04; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Na(+)/dicarboxylate cotransporter 3 {ECO:0000303|PubMed:30635937}; DE Short=NaDC-3; DE Short=hNaDC3 {ECO:0000303|PubMed:10794676}; DE AltName: Full=Na(+)-coupled carboxylate transporter 3; DE Short=NaC3; DE AltName: Full=Sodium-dependent high-affinity dicarboxylate transporter 2; DE AltName: Full=Solute carrier family 13 member 3; DE Short=SLC13A3 {ECO:0000303|PubMed:30635937}; GN Name=SLC13A3; Synonyms=NADC3, SDCT2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND RP ACTIVITY REGULATION. RC TISSUE=Placenta; RX PubMed=10794676; DOI=10.1152/ajpcell.2000.278.5.c1019; RA Wang H., Fei Y.-J., Kekuda R., Yang-Feng T.L., Devoe L.D., Leibach F.H., RA Prasad P.D., Ganapathy V.; RT "Structure, function, and genomic organization of human Na(+)-dependent RT high-affinity dicarboxylate transporter."; RL Am. J. Physiol. 278:C1019-C1030(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Kidney; RA Bai X.-Y., Chen X.-M., Qiu Q.; RT "Cloning and characterization of energy metabolism-related sodium-dependent RT high-affinity dicarboxylate transporter gene from human kidney."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5). RC TISSUE=Brain, Hippocampus, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-602 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10992006; RA Huang W., Wang H., Kekuda R., Fei Y.J., Friedrich A., Wang J., Conway S.J., RA Cameron R.S., Leibach F.H., Ganapathy V.; RT "Transport of N-acetylaspartate by the Na(+)-dependent high-affinity RT dicarboxylate transporter NaDC3 and its relevance to the expression of the RT transporter in the brain."; RL J. Pharmacol. Exp. Ther. 295:392-403(2000). RN [9] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15561973; DOI=10.1152/ajprenal.00360.2004; RA Burckhardt B.C., Lorenz J., Kobbe C., Burckhardt G.; RT "Substrate specificity of the human renal sodium dicarboxylate RT cotransporter, hNaDC-3, under voltage-clamp conditions."; RL Am. J. Physiol. 288:F792-F799(2005). RN [10] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=16331647; DOI=10.1002/jcp.20553; RA Bai X., Chen X., Feng Z., Hou K., Zhang P., Fu B., Shi S.; RT "Identification of basolateral membrane targeting signal of human sodium- RT dependent dicarboxylate transporter 3."; RL J. Cell. Physiol. 206:821-830(2006). RN [11] RP SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, TRANSPORTER ACTIVITY, AND RP FUNCTION. RX PubMed=17426067; DOI=10.1096/fj.06-7652com; RA Bai X.Y., Chen X., Sun A.Q., Feng Z., Hou K., Fu B.; RT "Membrane topology structure of human high-affinity, sodium-dependent RT dicarboxylate transporter."; RL FASEB J. 21:2409-2417(2007). RN [12] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17356845; DOI=10.1007/s00109-007-0174-5; RA Stellmer F., Keyser B., Burckhardt B.C., Koepsell H., Streichert T., RA Glatzel M., Jabs S., Thiem J., Herdering W., Koeller D.M., Goodman S.I., RA Lukacs Z., Ullrich K., Burckhardt G., Braulke T., Muehlhausen C.; RT "3-Hydroxyglutaric acid is transported via the sodium-dependent RT dicarboxylate transporter NaDC3."; RL J. Mol. Med. 85:763-770(2007). RN [13] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=24247155; DOI=10.1159/000356419; RA Schorbach L., Krick W., Burckhardt G., Burckhardt B.C.; RT "Glutathione is a low-affinity substrate of the human sodium-dependent RT dicarboxylate transporter."; RL Nephron Physiol. 124:1-5(2013). RN [14] RP FUNCTION, INVOLVEMENT IN ARLIAK, VARIANTS ARLIAK ASP-254 AND SER-548, RP CHARACTERIZATION OF VARIANTS ARLIAK ASP-254 AND SER-548, BIOPHYSICOCHEMICAL RP PROPERTIES, AND TRANSPORTER ACTIVITY. RX PubMed=30635937; DOI=10.1002/ana.25412; RA Dewulf J.P., Wiame E., Dorboz I., Elmaleh-Berges M., Imbard A., RA Dumitriu D., Rak M., Bourillon A., Helaers R., Malla A., Renaldo F., RA Boespflug-Tanguy O., Vincent M.F., Benoist J.F., Wevers R.A., RA Schlessinger A., Van Schaftingen E., Nassogne M.C., Schiff M.; RT "SLC13A3 variants cause acute reversible leukoencephalopathy and alpha- RT ketoglutarate accumulation."; RL Ann. Neurol. 85:385-395(2019). CC -!- FUNCTION: High-affinity sodium-dicarboxylate cotransporter that accepts CC a range of substrates with 4-6 carbon atoms, such as the citric acid CC cycle intermediates succinate and alpha-ketoglutarate (2-oxoglutarate), CC as well as other compounds including N-acetyl-L-aspartate CC (PubMed:10794676, PubMed:10992006, PubMed:15561973, PubMed:17426067, CC PubMed:17356845, PubMed:24247155, PubMed:30635937). Transports the CC dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) CC for 1 divalent dicarboxylate, rendering the process electrogenic CC (PubMed:10794676, PubMed:10992006). Can transport citrate in a Na(+)- CC dependent manner, recognizing the divalent form of citrate rather than CC the trivalent form which is normally found in blood (PubMed:10794676). CC {ECO:0000269|PubMed:10794676, ECO:0000269|PubMed:10992006, CC ECO:0000269|PubMed:15561973, ECO:0000269|PubMed:17356845, CC ECO:0000269|PubMed:17426067, ECO:0000269|PubMed:24247155, CC ECO:0000269|PubMed:30635937}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3 Na(+)(out) + succinate(out) = 3 Na(+)(in) + succinate(in); CC Xref=Rhea:RHEA:71919, ChEBI:CHEBI:29101, ChEBI:CHEBI:30031; CC Evidence={ECO:0000269|PubMed:10794676, ECO:0000269|PubMed:10992006, CC ECO:0000269|PubMed:15561973, ECO:0000269|PubMed:17356845, CC ECO:0000269|PubMed:17426067, ECO:0000269|PubMed:24247155, CC ECO:0000269|PubMed:30635937}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate(out) + 3 Na(+)(out) = 2-oxoglutarate(in) + 3 CC Na(+)(in); Xref=Rhea:RHEA:71939, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:15561973, CC ECO:0000269|PubMed:17356845, ECO:0000269|PubMed:30635937, CC ECO:0000305|PubMed:10794676}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-L-aspartate(out) + 3 Na(+)(out) = N-acetyl-L- CC aspartate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:71947, ChEBI:CHEBI:16953, CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10992006, CC ECO:0000269|PubMed:30635937}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glutarate(out) + 3 Na(+)(out) = glutarate(in) + 3 Na(+)(in); CC Xref=Rhea:RHEA:71955, ChEBI:CHEBI:29101, ChEBI:CHEBI:30921; CC Evidence={ECO:0000269|PubMed:15561973, ECO:0000269|PubMed:17356845}; CC -!- CATALYTIC ACTIVITY: CC Reaction=fumarate(out) + 3 Na(+)(out) = fumarate(in) + 3 Na(+)(in); CC Xref=Rhea:RHEA:71931, ChEBI:CHEBI:29101, ChEBI:CHEBI:29806; CC Evidence={ECO:0000269|PubMed:15561973}; CC -!- CATALYTIC ACTIVITY: CC Reaction=malate(out) + 3 Na(+)(out) = malate(in) + 3 Na(+)(in); CC Xref=Rhea:RHEA:72295, ChEBI:CHEBI:15595, ChEBI:CHEBI:29101; CC Evidence={ECO:0000269|PubMed:15561973}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2,2-dimethylsuccinate(out) + 3 Na(+)(out) = 2,2- CC dimethylsuccinate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:72287, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:191383; CC Evidence={ECO:0000269|PubMed:15561973}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2,3-dimethylsuccinate(out) + 3 Na(+)(out) = 2,3- CC dimethylsuccinate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:72291, CC ChEBI:CHEBI:29101, ChEBI:CHEBI:191384; CC Evidence={ECO:0000269|PubMed:15561973}; CC -!- ACTIVITY REGULATION: Li(+) decreases succinate transport in the CC presence of Na(+). {ECO:0000269|PubMed:10794676}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=112 uM for succinate {ECO:0000269|PubMed:30635937}; CC KM=25 uM for succinate {ECO:0000269|PubMed:15561973, CC ECO:0000269|PubMed:17356845}; CC KM=149 uM for 2-oxoglutarate {ECO:0000269|PubMed:30635937}; CC KM=45 uM for 2-oxoglutarate {ECO:0000269|PubMed:15561973, CC ECO:0000269|PubMed:17356845}; CC KM=40 uM for glutarate {ECO:0000269|PubMed:15561973, CC ECO:0000269|PubMed:17356845}; CC KM=220 uM for N-acetyl-L-aspartate {ECO:0000269|PubMed:30635937}; CC KM=1.65 mM for glutathione {ECO:0000269|PubMed:24247155}; CC KM=0.95 mM for 3-hydroxyglutarate {ECO:0000269|PubMed:17356845}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:10992006}; CC -!- INTERACTION: CC Q8WWT9; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12938720, EBI-11343438; CC Q8WWT9; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12938720, EBI-1045797; CC Q8WWT9; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12938720, EBI-6942903; CC Q8WWT9; P00387: CYB5R3; NbExp=3; IntAct=EBI-12938720, EBI-1046040; CC Q8WWT9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12938720, EBI-781551; CC Q8WWT9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12938720, EBI-18304435; CC Q8WWT9; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12938720, EBI-11721746; CC Q8WWT9; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12938720, EBI-17490413; CC Q8WWT9; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-12938720, EBI-1056589; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16331647, CC ECO:0000269|PubMed:17426067}; Multi-pass membrane protein CC {ECO:0000269|PubMed:16331647, ECO:0000269|PubMed:17426067}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q8WWT9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWT9-2; Sequence=VSP_006123, VSP_006124; CC Name=3; CC IsoId=Q8WWT9-3; Sequence=VSP_015291, VSP_015293; CC Name=4; CC IsoId=Q8WWT9-4; Sequence=VSP_015292, VSP_015294, VSP_015295; CC Name=5; CC IsoId=Q8WWT9-5; Sequence=VSP_015292; CC Name=6; CC IsoId=Q8WWT9-6; Sequence=VSP_015291; CC -!- TISSUE SPECIFICITY: Expression is highest in kidney (PubMed:16331647). CC Detected in placenta, brain, liver and pancreas. CC {ECO:0000269|PubMed:16331647}. CC -!- DISEASE: Leukoencephalopathy, acute reversible, with increased urinary CC alpha-ketoglutarate (ARLIAK) [MIM:618384]: An autosomal recessive CC disorder characterized by acute, reversible neurological deterioration CC during febrile illness. Patients exhibit reversible leukoencephalopathy CC and increased urinary excretion of alpha-ketoglutarate. CC {ECO:0000269|PubMed:30635937}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. CC NADC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF73251.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAC09447.2; Type=Miscellaneous discrepancy; Note=erroneous CDS prediction.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF154121; AAF73251.1; ALT_FRAME; mRNA. DR EMBL; AY072810; AAL66762.1; -; mRNA. DR EMBL; AK056713; BAB71262.1; -; mRNA. DR EMBL; AK096658; BAC04834.1; -; mRNA. DR EMBL; AK295748; BAG58580.1; -; mRNA. DR EMBL; AL133520; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL034424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75725.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75726.1; -; Genomic_DNA. DR EMBL; BC035966; AAH35966.1; -; mRNA. DR EMBL; AL442082; CAC09447.2; ALT_SEQ; mRNA. DR CCDS; CCDS13400.1; -. [Q8WWT9-1] DR CCDS; CCDS42886.1; -. [Q8WWT9-6] DR CCDS; CCDS54469.1; -. [Q8WWT9-3] DR CCDS; CCDS54470.1; -. [Q8WWT9-5] DR RefSeq; NP_001011554.1; NM_001011554.2. [Q8WWT9-6] DR RefSeq; NP_001180268.1; NM_001193339.1. [Q8WWT9-5] DR RefSeq; NP_001180269.1; NM_001193340.1. [Q8WWT9-3] DR RefSeq; NP_073740.2; NM_022829.5. [Q8WWT9-1] DR AlphaFoldDB; Q8WWT9; -. DR SMR; Q8WWT9; -. DR BioGRID; 122322; 12. DR IntAct; Q8WWT9; 10. DR MINT; Q8WWT9; -. DR STRING; 9606.ENSP00000279027; -. DR BindingDB; Q8WWT9; -. DR ChEMBL; CHEMBL3712947; -. DR DrugBank; DB00139; Succinic acid. DR TCDB; 2.A.47.1.15; the divalent anion:na(+) symporter (dass) family. DR GlyCosmos; Q8WWT9; 3 sites, 1 glycan. DR GlyGen; Q8WWT9; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q8WWT9; -. DR PhosphoSitePlus; Q8WWT9; -. DR BioMuta; SLC13A3; -. DR DMDM; 23396845; -. DR EPD; Q8WWT9; -. DR jPOST; Q8WWT9; -. DR MassIVE; Q8WWT9; -. DR MaxQB; Q8WWT9; -. DR PaxDb; 9606-ENSP00000279027; -. DR PeptideAtlas; Q8WWT9; -. DR ProteomicsDB; 28114; -. DR ProteomicsDB; 4325; -. DR ProteomicsDB; 74929; -. [Q8WWT9-1] DR ProteomicsDB; 74930; -. [Q8WWT9-2] DR ProteomicsDB; 74931; -. [Q8WWT9-3] DR ProteomicsDB; 74932; -. [Q8WWT9-4] DR Antibodypedia; 13229; 137 antibodies from 24 providers. DR DNASU; 64849; -. DR Ensembl; ENST00000279027.9; ENSP00000279027.4; ENSG00000158296.14. [Q8WWT9-1] DR Ensembl; ENST00000290317.9; ENSP00000290317.5; ENSG00000158296.14. [Q8WWT9-6] DR Ensembl; ENST00000413164.6; ENSP00000415852.2; ENSG00000158296.14. [Q8WWT9-5] DR Ensembl; ENST00000472148.5; ENSP00000420177.1; ENSG00000158296.14. [Q8WWT9-3] DR Ensembl; ENST00000495082.5; ENSP00000419621.1; ENSG00000158296.14. [Q8WWT9-6] DR GeneID; 64849; -. DR KEGG; hsa:64849; -. DR MANE-Select; ENST00000279027.9; ENSP00000279027.4; NM_022829.6; NP_073740.2. DR UCSC; uc002xsf.3; human. [Q8WWT9-1] DR AGR; HGNC:14430; -. DR CTD; 64849; -. DR DisGeNET; 64849; -. DR GeneCards; SLC13A3; -. DR HGNC; HGNC:14430; SLC13A3. DR HPA; ENSG00000158296; Tissue enriched (kidney). DR MalaCards; SLC13A3; -. DR MIM; 606411; gene. DR MIM; 618384; phenotype. DR neXtProt; NX_Q8WWT9; -. DR OpenTargets; ENSG00000158296; -. DR PharmGKB; PA37881; -. DR VEuPathDB; HostDB:ENSG00000158296; -. DR eggNOG; KOG1281; Eukaryota. DR GeneTree; ENSGT01030000234550; -. DR HOGENOM; CLU_005170_9_1_1; -. DR InParanoid; Q8WWT9; -. DR OMA; WISNAAT; -. DR OrthoDB; 1359392at2759; -. DR PhylomeDB; Q8WWT9; -. DR TreeFam; TF312913; -. DR PathwayCommons; Q8WWT9; -. DR Reactome; R-HSA-433137; Sodium-coupled sulphate, di- and tri-carboxylate transporters. DR SABIO-RK; Q8WWT9; -. DR SignaLink; Q8WWT9; -. DR BioGRID-ORCS; 64849; 14 hits in 1165 CRISPR screens. DR ChiTaRS; SLC13A3; human. DR GeneWiki; SLC13A3; -. DR GenomeRNAi; 64849; -. DR Pharos; Q8WWT9; Tbio. DR PRO; PR:Q8WWT9; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q8WWT9; Protein. DR Bgee; ENSG00000158296; Expressed in nephron tubule and 159 other cell types or tissues. DR ExpressionAtlas; Q8WWT9; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015137; F:citrate transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0005310; F:dicarboxylic acid transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0015362; F:high-affinity sodium:dicarboxylate symporter activity; TAS:Reactome. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IDA:ARUK-UCL. DR GO; GO:0015141; F:succinate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015746; P:citrate transport; ISS:ARUK-UCL. DR GO; GO:0006835; P:dicarboxylic acid transport; IDA:ARUK-UCL. DR GO; GO:0034775; P:glutathione transmembrane transport; IDA:ARUK-UCL. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0071422; P:succinate transmembrane transport; IDA:ARUK-UCL. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR CDD; cd01115; SLC13_permease; 1. DR InterPro; IPR001898; SLC13A/DASS. DR PANTHER; PTHR10283; SOLUTE CARRIER FAMILY 13 MEMBER; 1. DR PANTHER; PTHR10283:SF62; SOLUTE CARRIER FAMILY 13 MEMBER 3; 1. DR Pfam; PF00939; Na_sulph_symp; 1. DR Genevisible; Q8WWT9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disease variant; Glycoprotein; KW Ion transport; Lipid transport; Membrane; Reference proteome; Sodium; KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..602 FT /note="Na(+)/dicarboxylate cotransporter 3" FT /id="PRO_0000172492" FT TOPO_DOM 1..16 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 17..37 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 38..55 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 56..76 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 77..82 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 104..137 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 138..158 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 159..229 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 230..250 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 251..278 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 279..299 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 300..336 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 337..357 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 358..372 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 373..393 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 394..422 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 423..443 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 444..461 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 462..482 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 483..505 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 506..526 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 527..546 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 547..567 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 568..602 FT /note="Extracellular" FT /evidence="ECO:0000255" FT CARBOHYD 586 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 596 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..47 FT /note="Missing (in isoform 3 and isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015291" FT VAR_SEQ 181..297 FT /note="AAVRRNGLHTVPTEMQFLASTEAKDHPGETEVPLDLPADSRKEDEYRRNIWK FT GFLISIPYSASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLL FT AGWLWI -> GIEPNTFLSEERLKLQAPLVIRLGQITESGQWNMSGNDVCNFRVLSFLP FT GGM (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_006123" FT VAR_SEQ 182..292 FT /note="AVRRNGLHTVPTEMQFLASTEAKDHPGETEVPLDLPADSRKEDEYRRNIWKG FT FLISIPYSASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLLA FT -> KTTLGRQRFHWICRLTPGRRMNIVGTSGRASSSPSPTQPVLGAQPHSRAQPLTSSC FT LASSR (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015292" FT VAR_SEQ 298..602 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_006124" FT VAR_SEQ 340..374 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_015293" FT VAR_SEQ 375..388 FT /note="FLSDAVTGVAIVTI -> CKMGIISISTIQKM (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_015294" FT VAR_SEQ 389..602 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_015295" FT VARIANT 254 FT /note="A -> D (in ARLIAK; unable to transport succinate, FT 2-oxoglutarate and N-acetylaspartate; dbSNP:rs1568927501)" FT /evidence="ECO:0000269|PubMed:30635937" FT /id="VAR_082121" FT VARIANT 548 FT /note="G -> S (in ARLIAK; severely decreased transport of FT succinate, 2-oxoglutarate and N-acetylaspartate; FT dbSNP:rs1568904872)" FT /evidence="ECO:0000269|PubMed:30635937" FT /id="VAR_082122" FT CONFLICT 94 FT /note="L -> P (in Ref. 3; BAC04834)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="I -> V (in Ref. 6; AAH35966)" FT /evidence="ECO:0000305" FT CONFLICT 572 FT /note="Q -> P (in Ref. 3; BAB71262)" FT /evidence="ECO:0000305" SQ SEQUENCE 602 AA; 66841 MW; 611A50994BA37687 CRC64; MAALAAAAKK VWSARRLLVL LFTPLALLPV VFALPPKEGR CLFVILLMAV YWCTEALPLS VTALLPIVLF PFMGILPSNK VCPQYFLDTN FLFLSGLIMA SAIEEWNLHR RIALKILMLV GVQPARLILG MMVTTSFLSM WLSNTASTAM MLPIANAILK SLFGQKEVRK DPSQESEENT AAVRRNGLHT VPTEMQFLAS TEAKDHPGET EVPLDLPADS RKEDEYRRNI WKGFLISIPY SASIGGTATL TGTAPNLILL GQLKSFFPQC DVVNFGSWFI FAFPLMLLFL LAGWLWISFL YGGLSFRGWR KNKSEIRTNA EDRARAVIRE EYQNLGPIKF AEQAVFILFC MFAILLFTRD PKFIPGWASL FNPGFLSDAV TGVAIVTILF FFPSQRPSLK WWFDFKAPNT ETEPLLTWKK AQETVPWNII LLLGGGFAMA KGCEESGLSV WIGGQLHPLE NVPPALAVLL ITVVIAFFTE FASNTATIII FLPVLAELAI RLRVHPLYLM IPGTVGCSFA FMLPVSTPPN SIAFASGHLL VKDMVRTGLL MNLMGVLLLS LAMNTWAQTI FQLGTFPDWA DMYSVNVTAL PPTLANDTFR TL //