S13A3_HUMAN
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 03-AUG-2022, entry version 179.
DE RecName: Full=Solute carrier family 13 member 3;
DE AltName: Full=Na(+)/dicarboxylate cotransporter 3;
DE Short=NaDC-3;
DE Short=hNaDC3;
DE AltName: Full=Sodium-dependent high-affinity dicarboxylate transporter 2;
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).
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 SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
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 [9]
RP FUNCTION, INVOLVEMENT IN ARLIAK, VARIANTS ARLIAK ASP-254 AND SER-548, AND
RP CHARACTERIZATION OF VARIANTS ARLIAK ASP-254 AND SER-548.
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, including succinate,
CC alpha-ketoglutarate and N-acetylaspartate (PubMed:30635937). The
CC stoichiometry is probably 3 Na(+) for 1 divalent succinate.
CC {ECO:0000269|PubMed:30635937}.
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:17426067};
CC Multi-pass membrane protein {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. Detected in
CC placenta, brain, liver and pancreas.
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};
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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; 11.
DR IntAct; Q8WWT9; 11.
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 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; Q8WWT9; -.
DR PeptideAtlas; Q8WWT9; -.
DR PRIDE; 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; 130 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 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; NFSICLM; -.
DR OrthoDB; 389981at2759; -.
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; 13 hits in 1085 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 157 other tissues.
DR ExpressionAtlas; Q8WWT9; baseline and differential.
DR Genevisible; Q8WWT9; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0098656; P:anion transmembrane transport; IBA:GO_Central.
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:0071422; P:succinate transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR001898; SLC13A/DASS.
DR Pfam; PF00939; Na_sulph_symp; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="Solute carrier family 13 member 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 alpha-ketoglutarate and N-acetylaspartate;
FT 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, alpha-ketoglutarate 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
