TXTP_HUMAN
ID TXTP_HUMAN Reviewed; 311 AA.
AC P53007; A8K8E8; Q9BSK6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Tricarboxylate transport protein, mitochondrial;
DE AltName: Full=Citrate transport protein;
DE Short=CTP;
DE AltName: Full=Solute carrier family 25 member 1;
DE AltName: Full=Tricarboxylate carrier protein;
DE Flags: Precursor;
GN Name=SLC25A1; Synonyms=SLC20A3;
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].
RX PubMed=8666394; DOI=10.1006/geno.1995.9982;
RA Heisterkamp N., Mulder M.P., Langeveld A., ten Hoeve J., Wang Z., Roe B.,
RA Groffen J.;
RT "Localization of the human mitochondrial citrate transporter protein gene
RT to chromosome 22q11 in the DiGeorge syndrome critical region.";
RL Genomics 29:451-456(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain;
RX PubMed=8660975; DOI=10.1006/geno.1996.0191;
RA Goldmuntz E., Wang Z., Roe B.A., Budarf M.L.;
RT "Cloning, genomic organization, and chromosomal localization of human
RT citrate transport protein to the DiGeorge/velocardiofacial syndrome minimal
RT critical region.";
RL Genomics 33:271-276(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, INVOLVEMENT IN CMS23, AND VARIANT CMS23 GLN-247.
RX PubMed=26870663; DOI=10.3233/jnd-140021;
RA Chaouch A., Porcelli V., Cox D., Edvardson S., Scarcia P., De Grassi A.,
RA Pierri C.L., Cossins J., Laval S.H., Griffin H., Mueller J.S.,
RA Evangelista T., Toepf A., Abicht A., Huebner A., von der Hagen M.,
RA Bushby K., Straub V., Horvath R., Elpeleg O., Palace J., Senderek J.,
RA Beeson D., Palmieri L., Lochmueller H.;
RT "Mutations in the mitochondrial citrate carrier SLC25A1 are associated with
RT impaired neuromuscular transmission.";
RL J. Neuromuscul. Dis. 1:75-90(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS
RP D2L2AD LEU-45; ASP-130; GLN-144; TRP-193; HIS-198; THR-202; CYS-282;
RP GLY-282; HIS-282 AND CYS-297, AND CHARACTERIZATION OF VARIANT CMS23
RP GLN-247.
RX PubMed=29031613; DOI=10.1016/j.bbabio.2017.10.002;
RA Majd H., King M.S., Smith A.C., Kunji E.R.S.;
RT "Pathogenic mutations of the human mitochondrial citrate carrier SLC25A1
RT lead to impaired citrate export required for lipid, dolichol, ubiquinone
RT and sterol synthesis.";
RL Biochim. Biophys. Acta 1859:1-7(2018).
RN [12]
RP FUNCTION, VARIANTS D2L2AD THR-28; ASN-40; LYS-47; ASP-93; TRP-193 AND
RP ARG-262, AND CHARACTERIZATION OF VARIANTS D2L2AD THR-28; ASN-40; LYS-47;
RP ASP-93; TRP-193; 256-TYR--ASP-311 DEL AND ARG-262.
RX PubMed=29238895; DOI=10.1007/s10545-017-0106-7;
RA Pop A., Williams M., Struys E.A., Monne M., Jansen E.E.W., De Grassi A.,
RA Kanhai W.A., Scarcia P., Ojeda M.R.F., Porcelli V., van Dooren S.J.M.,
RA Lennertz P., Nota B., Abdenur J.E., Coman D., Das A.M., El-Gharbawy A.,
RA Nuoffer J.M., Polic B., Santer R., Weinhold N., Zuccarelli B., Palmieri F.,
RA Palmieri L., Salomons G.S.;
RT "An overview of combined D-2- and L-2-hydroxyglutaric aciduria: functional
RT analysis of CIC variants.";
RL J. Inherit. Metab. Dis. 41:169-180(2018).
RN [13]
RP VARIANTS D2L2AD LEU-45; GLN-144; ARG-167; TRP-193; THR-202;
RP 256-TYR--ASP-311 DEL; CYS-282; GLY-282 AND CYS-297, AND CHARACTERIZATION OF
RP VARIANT D2L2AD 256-TYR--ASP-311 DEL.
RX PubMed=23561848; DOI=10.1016/j.ajhg.2013.03.009;
RA Nota B., Struys E.A., Pop A., Jansen E.E., Fernandez Ojeda M.R.,
RA Kanhai W.A., Kranendijk M., van Dooren S.J., Bevova M.R., Sistermans E.A.,
RA Nieuwint A.W., Barth M., Ben-Omran T., Hoffmann G.F., de Lonlay P.,
RA McDonald M.T., Meberg A., Muntau A.C., Nuoffer J.M., Parini R., Read M.H.,
RA Renneberg A., Santer R., Strahleck T., van Schaftingen E.,
RA van der Knaap M.S., Jakobs C., Salomons G.S.;
RT "Deficiency in SLC25A1, encoding the mitochondrial citrate carrier, causes
RT combined D-2- and L-2-hydroxyglutaric aciduria.";
RL Am. J. Hum. Genet. 92:627-631(2013).
RN [14]
RP VARIANTS D2L2AD ASP-130 AND HIS-282.
RX PubMed=23393310; DOI=10.1136/jmedgenet-2012-101485;
RA Edvardson S., Porcelli V., Jalas C., Soiferman D., Kellner Y., Shaag A.,
RA Korman S.H., Pierri C.L., Scarcia P., Fraenkel N.D., Segel R.,
RA Schechter A., Frumkin A., Pines O., Saada A., Palmieri L., Elpeleg O.;
RT "Agenesis of corpus callosum and optic nerve hypoplasia due to mutations in
RT SLC25A1 encoding the mitochondrial citrate transporter.";
RL J. Med. Genet. 50:240-245(2013).
RN [15]
RP VARIANT D2L2AD LEU-45.
RX PubMed=25614306; DOI=10.1007/8904_2014_378;
RA Prasun P., Young S., Salomons G., Werneke A., Jiang Y.H., Struys E.,
RA Paige M., Avantaggiati M.L., McDonald M.;
RT "Expanding the clinical spectrum of mitochondrial citrate carrier (SLC25A1)
RT deficiency: Facial dysmorphism in siblings with epileptic encephalopathy
RT and combined D,L-2-hydroxyglutaric aciduria.";
RL JIMD Rep. 19:111-115(2015).
RN [16]
RP VARIANT D2L2AD HIS-198.
RX PubMed=27306203; DOI=10.1007/8904_2016_536;
RG FORGE Canada Consortium;
RA Smith A., McBride S., Marcadier J.L., Michaud J., Al-Dirbashi O.Y.,
RA Schwartzentruber J., Beaulieu C.L., Katz S.L., Majewski J., Bulman D.E.,
RA Geraghty M.T., Harper M.E., Chakraborty P., Lines M.A.;
RT "Severe neonatal presentation of mitochondrial citrate carrier (SLC25A1)
RT deficiency.";
RL JIMD Rep. 30:73-79(2016).
RN [17]
RP VARIANT D2L2AD SER-238.
RX PubMed=29226520; DOI=10.1002/ajmg.a.38574;
RA Cohen I., Staretz-Chacham O., Wormser O., Perez Y., Saada A., Kadir R.,
RA Birk O.S.;
RT "A novel homozygous SLC25A1 mutation with impaired mitochondrial complex V:
RT Possible phenotypic expansion.";
RL Am. J. Med. Genet. A 176:330-336(2018).
CC -!- FUNCTION: Citrate transporter that mediates the exchange of
CC mitochondrial citrate for cytosolic malate (PubMed:29031613,
CC PubMed:29238895). Also able to mediate the exchange of citrate for
CC isocitrate, phosphoenolpyruvate, cis- but not trans-aconitate and to a
CC lesser extend maleate and succinate (PubMed:29031613). Important for
CC the bioenergetics of hepatic cells as it provides a carbon source for
CC fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic
CC pathway. Required for proper neuromuscular junction formation
CC (Probable). {ECO:0000269|PubMed:29031613, ECO:0000269|PubMed:29238895,
CC ECO:0000305|PubMed:26870663}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 uM for citrate {ECO:0000269|PubMed:29031613};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8JZU2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISEASE: Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD)
CC [MIM:615182]: An autosomal recessive neurometabolic disorder
CC characterized by neonatal-onset encephalopathy with severe muscular
CC weakness, intractable seizures, respiratory distress, and lack of
CC psychomotor development resulting in early death. Brain imaging shows
CC abnormalities including enlarged ventricles, delayed myelination, and
CC germinal layer cysts. {ECO:0000269|PubMed:23393310,
CC ECO:0000269|PubMed:23561848, ECO:0000269|PubMed:25614306,
CC ECO:0000269|PubMed:27306203, ECO:0000269|PubMed:29031613,
CC ECO:0000269|PubMed:29226520, ECO:0000269|PubMed:29238895}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 23, presynaptic (CMS23)
CC [MIM:618197]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features include easy fatigability
CC and muscle weakness. CMS23 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:26870663, ECO:0000269|PubMed:29031613}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; U25147; AAB08515.1; -; mRNA.
DR EMBL; L76134; AAL40091.1; -; Genomic_DNA.
DR EMBL; L75823; AAL40090.1; -; mRNA.
DR EMBL; AK292313; BAF85002.1; -; mRNA.
DR EMBL; BC004980; AAH04980.1; -; mRNA.
DR EMBL; BC008061; AAH08061.1; -; mRNA.
DR CCDS; CCDS13758.1; -.
DR PIR; G01789; G01789.
DR RefSeq; NP_005975.1; NM_005984.4.
DR AlphaFoldDB; P53007; -.
DR SMR; P53007; -.
DR BioGRID; 112464; 229.
DR IntAct; P53007; 99.
DR MINT; P53007; -.
DR STRING; 9606.ENSP00000215882; -.
DR DrugBank; DB09154; Sodium citrate.
DR TCDB; 2.A.29.7.2; the mitochondrial carrier (mc) family.
DR iPTMnet; P53007; -.
DR PhosphoSitePlus; P53007; -.
DR SwissPalm; P53007; -.
DR BioMuta; SLC25A1; -.
DR DMDM; 20141931; -.
DR CPTAC; CPTAC-586; -.
DR CPTAC; CPTAC-587; -.
DR EPD; P53007; -.
DR jPOST; P53007; -.
DR MassIVE; P53007; -.
DR MaxQB; P53007; -.
DR PaxDb; P53007; -.
DR PeptideAtlas; P53007; -.
DR PRIDE; P53007; -.
DR ProteomicsDB; 56567; -.
DR TopDownProteomics; P53007; -.
DR Antibodypedia; 22859; 155 antibodies from 23 providers.
DR DNASU; 6576; -.
DR Ensembl; ENST00000215882.10; ENSP00000215882.5; ENSG00000100075.10.
DR GeneID; 6576; -.
DR KEGG; hsa:6576; -.
DR MANE-Select; ENST00000215882.10; ENSP00000215882.5; NM_005984.5; NP_005975.1.
DR UCSC; uc002zoz.6; human.
DR CTD; 6576; -.
DR DisGeNET; 6576; -.
DR GeneCards; SLC25A1; -.
DR GeneReviews; SLC25A1; -.
DR HGNC; HGNC:10979; SLC25A1.
DR HPA; ENSG00000100075; Tissue enhanced (liver).
DR MalaCards; SLC25A1; -.
DR MIM; 190315; gene.
DR MIM; 615182; phenotype.
DR MIM; 618197; phenotype.
DR neXtProt; NX_P53007; -.
DR OpenTargets; ENSG00000100075; -.
DR Orphanet; 356978; D,L-2-hydroxyglutaric aciduria.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA35855; -.
DR VEuPathDB; HostDB:ENSG00000100075; -.
DR eggNOG; KOG0756; Eukaryota.
DR GeneTree; ENSGT00550000074856; -.
DR HOGENOM; CLU_015166_5_1_1; -.
DR InParanoid; P53007; -.
DR OMA; CPAFIVG; -.
DR PhylomeDB; P53007; -.
DR TreeFam; TF105786; -.
DR PathwayCommons; P53007; -.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR SignaLink; P53007; -.
DR SIGNOR; P53007; -.
DR BioGRID-ORCS; 6576; 73 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC25A1; human.
DR GeneWiki; SLC25A1; -.
DR GenomeRNAi; 6576; -.
DR Pharos; P53007; Tbio.
DR PRO; PR:P53007; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P53007; protein.
DR Bgee; ENSG00000100075; Expressed in endometrium epithelium and 192 other tissues.
DR ExpressionAtlas; P53007; baseline and differential.
DR Genevisible; P53007; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0071913; F:citrate secondary active transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; TAS:UniProtKB.
DR GO; GO:0015142; F:tricarboxylic acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006843; P:mitochondrial citrate transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Congenital myasthenic syndrome; Disease variant; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P32089"
FT CHAIN 14..311
FT /note="Tricarboxylate transport protein, mitochondrial"
FT /id="PRO_0000019262"
FT TRANSMEM 29..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 23..111
FT /note="Solcar 1"
FT REPEAT 122..208
FT /note="Solcar 2"
FT REPEAT 218..303
FT /note="Solcar 3"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 28
FT /note="A -> T (in D2L2AD; unknown pathological
FT significance; very mild decrease of citrate transport
FT rates)"
FT /evidence="ECO:0000269|PubMed:29238895"
FT /id="VAR_081661"
FT VARIANT 40
FT /note="I -> N (in D2L2AD; reduced rates of citrate
FT transport)"
FT /evidence="ECO:0000269|PubMed:29238895"
FT /id="VAR_081662"
FT VARIANT 45
FT /note="P -> L (in D2L2AD; severely reduced rates of citrate
FT transport)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:25614306, ECO:0000269|PubMed:29031613"
FT /id="VAR_069490"
FT VARIANT 47
FT /note="E -> K (in D2L2AD; severely reduced rates of citrate
FT transport; dbSNP:rs1555923307)"
FT /evidence="ECO:0000269|PubMed:29238895"
FT /id="VAR_081663"
FT VARIANT 93
FT /note="G -> D (in D2L2AD; severely reduced rates of citrate
FT transport)"
FT /evidence="ECO:0000269|PubMed:29238895"
FT /id="VAR_081664"
FT VARIANT 130
FT /note="G -> D (in D2L2AD; severely reduced rates of citrate
FT transport; dbSNP:rs368647424)"
FT /evidence="ECO:0000269|PubMed:23393310,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_081665"
FT VARIANT 144
FT /note="E -> Q (in D2L2AD; abolishes citrate transport)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_069491"
FT VARIANT 167
FT /note="G -> R (in D2L2AD)"
FT /evidence="ECO:0000269|PubMed:23561848"
FT /id="VAR_069492"
FT VARIANT 193
FT /note="S -> W (in D2L2AD; reduced rates of citrate
FT transport; dbSNP:rs781925968)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613, ECO:0000269|PubMed:29238895"
FT /id="VAR_069493"
FT VARIANT 198
FT /note="R -> H (in D2L2AD; severely reduced rates of citrate
FT transport; dbSNP:rs1331417017)"
FT /evidence="ECO:0000269|PubMed:27306203,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_077511"
FT VARIANT 202
FT /note="M -> T (in D2L2AD; reduced rates of citrate
FT transport; dbSNP:rs782335811)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_069494"
FT VARIANT 238
FT /note="N -> S (in D2L2AD; disease phenotype may include
FT decreased activity of mitochondrial respiratory chain
FT complex V)"
FT /evidence="ECO:0000269|PubMed:29226520"
FT /id="VAR_081666"
FT VARIANT 247
FT /note="R -> Q (in CMS23; reduced rates of citrate
FT transport; dbSNP:rs781908532)"
FT /evidence="ECO:0000269|PubMed:26870663,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_081667"
FT VARIANT 256..311
FT /note="Missing (in D2L2AD; no protein detected by Western
FT blot in patient fibroblasts; severely reduced rates of
FT citrate transport)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29238895"
FT /id="VAR_081668"
FT VARIANT 262
FT /note="C -> R (in D2L2AD; reduced rates of citrate
FT transport)"
FT /evidence="ECO:0000269|PubMed:29238895"
FT /id="VAR_081669"
FT VARIANT 282
FT /note="R -> C (in D2L2AD; abolishes citrate transport;
FT dbSNP:rs431905509)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_069495"
FT VARIANT 282
FT /note="R -> G (in D2L2AD; abolishes citrate transport;
FT dbSNP:rs431905509)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_069496"
FT VARIANT 282
FT /note="R -> H (in D2L2AD; abolishes citrate transport;
FT dbSNP:rs431905510)"
FT /evidence="ECO:0000269|PubMed:23393310,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_081670"
FT VARIANT 297
FT /note="Y -> C (in D2L2AD; reduced rates of citrate
FT transport)"
FT /evidence="ECO:0000269|PubMed:23561848,
FT ECO:0000269|PubMed:29031613"
FT /id="VAR_069497"
FT CONFLICT 26
FT /note="G -> E (in Ref. 1; AAB08515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34013 MW; F1341629924953D6 CRC64;
MPAPRAPRAL AAAAPASGKA KLTHPGKAIL AGGLAGGIEI CITFPTEYVK TQLQLDERSH
PPRYRGIGDC VRQTVRSHGV LGLYRGLSSL LYGSIPKAAV RFGMFEFLSN HMRDAQGRLD
STRGLLCGLG AGVAEAVVVV CPMETIKVKF IHDQTSPNPK YRGFFHGVRE IVREQGLKGT
YQGLTATVLK QGSNQAIRFF VMTSLRNWYR GDNPNKPMNP LITGVFGAIA GAASVFGNTP
LDVIKTRMQG LEAHKYRNTW DCGLQILKKE GLKAFYKGTV PRLGRVCLDV AIVFVIYDEV
VKLLNKVWKT D
