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Tricarboxylate transport protein, mitochondrial (Citrate transport protein) (CTP) (Solute carrier family 25 member 1) (Tricarboxylate carrier protein)

 TXTP_HUMAN              Reviewed;         311 AA.
P53007; A8K8E8; Q9BSK6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-FEB-2002, sequence version 2.
18-JUL-2018, entry version 175.
RecName: Full=Tricarboxylate transport protein, mitochondrial;
AltName: Full=Citrate transport protein;
Short=CTP;
AltName: Full=Solute carrier family 25 member 1;
AltName: Full=Tricarboxylate carrier protein;
Flags: Precursor;
Name=SLC25A1; Synonyms=SLC20A3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8666394; DOI=10.1006/geno.1995.9982;
Heisterkamp N., Mulder M.P., Langeveld A., ten Hoeve J., Wang Z.,
Roe B., Groffen J.;
"Localization of the human mitochondrial citrate transporter protein
gene to chromosome 22q11 in the DiGeorge syndrome critical region.";
Genomics 29:451-456(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Brain;
PubMed=8660975; DOI=10.1006/geno.1996.0191;
Goldmuntz E., Wang Z., Roe B.A., Budarf M.L.;
"Cloning, genomic organization, and chromosomal localization of human
citrate transport protein to the DiGeorge/velocardiofacial syndrome
minimal critical region.";
Genomics 33:271-276(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
VARIANTS D2L2AD LEU-45; GLN-144; ARG-167; TRP-193; THR-202; CYS-282;
GLY-282 AND CYS-297.
PubMed=23561848; DOI=10.1016/j.ajhg.2013.03.009;
Nota B., Struys E.A., Pop A., Jansen E.E., Fernandez Ojeda M.R.,
Kanhai W.A., Kranendijk M., van Dooren S.J., Bevova M.R.,
Sistermans E.A., Nieuwint A.W., Barth M., Ben-Omran T., Hoffmann G.F.,
de Lonlay P., McDonald M.T., Meberg A., Muntau A.C., Nuoffer J.M.,
Parini R., Read M.H., Renneberg A., Santer R., Strahleck T.,
van Schaftingen E., van der Knaap M.S., Jakobs C., Salomons G.S.;
"Deficiency in SLC25A1, encoding the mitochondrial citrate carrier,
causes combined D-2- and L-2-hydroxyglutaric aciduria.";
Am. J. Hum. Genet. 92:627-631(2013).
[11]
VARIANT D2L2AD HIS-198.
PubMed=27306203; DOI=10.1007/8904_2016_536;
FORGE Canada Consortium;
Smith A., McBride S., Marcadier J.L., Michaud J., Al-Dirbashi O.Y.,
Schwartzentruber J., Beaulieu C.L., Katz S.L., Majewski J.,
Bulman D.E., Geraghty M.T., Harper M.E., Chakraborty P., Lines M.A.;
"Severe neonatal presentation of mitochondrial citrate carrier
(SLC25A1) deficiency.";
JIMD Rep. 30:73-79(2016).
-!- FUNCTION: Involved in citrate-H(+)/malate exchange. Important for
the bioenergetics of hepatic cells as it provides a carbon source
for fatty acid and sterol biosyntheses, and NAD(+) for the
glycolytic pathway.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
membrane protein.
-!- DISEASE: Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD)
[MIM:615182]: An autosomal recessive neurometabolic disorder
characterized by neonatal-onset encephalopathy with severe
muscular weakness, intractable seizures, respiratory distress, and
lack of psychomotor development resulting in early death. Brain
imaging shows abnormalities including enlarged ventricles, delayed
myelination, and germinal layer cysts.
{ECO:0000269|PubMed:23561848, ECO:0000269|PubMed:27306203}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U25147; AAB08515.1; -; mRNA.
EMBL; L76134; AAL40091.1; -; Genomic_DNA.
EMBL; L75823; AAL40090.1; -; mRNA.
EMBL; AK292313; BAF85002.1; -; mRNA.
EMBL; BC004980; AAH04980.1; -; mRNA.
EMBL; BC008061; AAH08061.1; -; mRNA.
CCDS; CCDS13758.1; -.
PIR; G01789; G01789.
RefSeq; NP_005975.1; NM_005984.4.
UniGene; Hs.111024; -.
ProteinModelPortal; P53007; -.
SMR; P53007; -.
BioGrid; 112464; 50.
IntAct; P53007; 49.
MINT; P53007; -.
STRING; 9606.ENSP00000215882; -.
TCDB; 2.A.29.7.2; the mitochondrial carrier (mc) family.
iPTMnet; P53007; -.
PhosphoSitePlus; P53007; -.
SwissPalm; P53007; -.
DMDM; 20141931; -.
EPD; P53007; -.
MaxQB; P53007; -.
PaxDb; P53007; -.
PeptideAtlas; P53007; -.
PRIDE; P53007; -.
ProteomicsDB; 56567; -.
TopDownProteomics; P53007; -.
DNASU; 6576; -.
Ensembl; ENST00000215882; ENSP00000215882; ENSG00000100075.
GeneID; 6576; -.
KEGG; hsa:6576; -.
UCSC; uc002zoz.6; human.
CTD; 6576; -.
DisGeNET; 6576; -.
EuPathDB; HostDB:ENSG00000100075.9; -.
GeneCards; SLC25A1; -.
H-InvDB; HIX0040279; -.
HGNC; HGNC:10979; SLC25A1.
MalaCards; SLC25A1; -.
MIM; 190315; gene.
MIM; 615182; phenotype.
neXtProt; NX_P53007; -.
OpenTargets; ENSG00000100075; -.
Orphanet; 356978; D,L-2-hydroxyglutaric aciduria.
Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
PharmGKB; PA35855; -.
eggNOG; KOG0756; Eukaryota.
eggNOG; ENOG410YAYP; LUCA.
GeneTree; ENSGT00550000074856; -.
HOVERGEN; HBG103009; -.
InParanoid; P53007; -.
KO; K15100; -.
OMA; LTFWSGA; -.
OrthoDB; EOG091G0KE7; -.
PhylomeDB; P53007; -.
TreeFam; TF105786; -.
Reactome; R-HSA-70263; Gluconeogenesis.
Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
ChiTaRS; SLC25A1; human.
GeneWiki; SLC25A1; -.
GenomeRNAi; 6576; -.
PRO; PR:P53007; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100075; -.
CleanEx; HS_SLC25A1; -.
ExpressionAtlas; P53007; baseline and differential.
Genevisible; P53007; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0015137; F:citrate transmembrane transporter activity; TAS:UniProtKB.
GO; GO:0015142; F:tricarboxylic acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0006843; P:mitochondrial citrate transmembrane transport; IBA:GO_Central.
GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
Gene3D; 1.50.40.10; -; 1.
InterPro; IPR002067; Mit_carrier.
InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
InterPro; IPR023395; Mt_carrier_dom_sf.
Pfam; PF00153; Mito_carr; 3.
PRINTS; PR00926; MITOCARRIER.
SUPFAM; SSF103506; SSF103506; 1.
PROSITE; PS50920; SOLCAR; 3.
1: Evidence at protein level;
Complete proteome; Disease mutation; Membrane; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
Repeat; Transit peptide; Transmembrane; Transmembrane helix;
Transport.
TRANSIT 1 13 Mitochondrion.
{ECO:0000250|UniProtKB:P32089}.
CHAIN 14 311 Tricarboxylate transport protein,
mitochondrial.
/FTId=PRO_0000019262.
TRANSMEM 29 46 Helical; Name=1. {ECO:0000255}.
TRANSMEM 86 105 Helical; Name=2. {ECO:0000255}.
TRANSMEM 129 143 Helical; Name=3. {ECO:0000255}.
TRANSMEM 183 202 Helical; Name=4. {ECO:0000255}.
TRANSMEM 224 241 Helical; Name=5. {ECO:0000255}.
TRANSMEM 278 297 Helical; Name=6. {ECO:0000255}.
REPEAT 23 111 Solcar 1.
REPEAT 122 208 Solcar 2.
REPEAT 218 303 Solcar 3.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 45 45 P -> L (in D2L2AD).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069490.
VARIANT 144 144 E -> Q (in D2L2AD).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069491.
VARIANT 167 167 G -> R (in D2L2AD).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069492.
VARIANT 193 193 S -> W (in D2L2AD; dbSNP:rs781925968).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069493.
VARIANT 198 198 R -> H (in D2L2AD).
{ECO:0000269|PubMed:27306203}.
/FTId=VAR_077511.
VARIANT 202 202 M -> T (in D2L2AD; dbSNP:rs782335811).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069494.
VARIANT 282 282 R -> C (in D2L2AD; dbSNP:rs431905509).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069495.
VARIANT 282 282 R -> G (in D2L2AD; dbSNP:rs431905509).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069496.
VARIANT 297 297 Y -> C (in D2L2AD).
{ECO:0000269|PubMed:23561848}.
/FTId=VAR_069497.
CONFLICT 26 26 G -> E (in Ref. 1; AAB08515).
{ECO:0000305}.
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


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