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P53007 (TXTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tricarboxylate transport protein, mitochondrial
Alternative name(s):
Citrate transport protein
Short name=CTP
Solute carrier family 25 member 1
Tricarboxylate carrier protein
Gene names
Name:SLC25A1
Synonyms:SLC20A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Sequence similarities

Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification]

Contains 3 Solcar repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1313Mitochondrion By similarity
Chain14 – 311298Tricarboxylate transport protein, mitochondrial
PRO_0000019262

Regions

Transmembrane29 – 4618Helical; Name=1; Potential
Transmembrane86 – 10520Helical; Name=2; Potential
Transmembrane129 – 14315Helical; Name=3; Potential
Transmembrane183 – 20220Helical; Name=4; Potential
Transmembrane224 – 24118Helical; Name=5; Potential
Transmembrane278 – 29720Helical; Name=6; Potential
Repeat23 – 11189Solcar 1
Repeat122 – 20887Solcar 2
Repeat218 – 30386Solcar 3

Amino acid modifications

Modified residue971N6-acetyllysine Ref.5

Experimental info

Sequence conflict261G → E in AAB08515. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53007 [UniParc].

Last modified February 11, 2002. Version 2.
Checksum: F1341629924953D6

FASTA31134,013
        10         20         30         40         50         60 
MPAPRAPRAL AAAAPASGKA KLTHPGKAIL AGGLAGGIEI CITFPTEYVK TQLQLDERSH 

        70         80         90        100        110        120 
PPRYRGIGDC VRQTVRSHGV LGLYRGLSSL LYGSIPKAAV RFGMFEFLSN HMRDAQGRLD 

       130        140        150        160        170        180 
STRGLLCGLG AGVAEAVVVV CPMETIKVKF IHDQTSPNPK YRGFFHGVRE IVREQGLKGT 

       190        200        210        220        230        240 
YQGLTATVLK QGSNQAIRFF VMTSLRNWYR GDNPNKPMNP LITGVFGAIA GAASVFGNTP 

       250        260        270        280        290        300 
LDVIKTRMQG LEAHKYRNTW DCGLQILKKE GLKAFYKGTV PRLGRVCLDV AIVFVIYDEV 

       310 
VKLLNKVWKT D 

« Hide

References

« Hide 'large scale' references
[1]"Localization of the human mitochondrial citrate transporter protein gene to chromosome 22q11 in the DiGeorge syndrome critical region."
Heisterkamp N., Mulder M.P., Langeveld A., ten Hoeve J., Wang Z., Roe B., Groffen J.
Genomics 29:451-456(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning, genomic organization, and chromosomal localization of human citrate transport protein to the DiGeorge/velocardiofacial syndrome minimal critical region."
Goldmuntz E., Wang Z., Roe B.A., Budarf M.L.
Genomics 33:271-276(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, MASS SPECTROMETRY.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25147 mRNA. Translation: AAB08515.1.
L76134 Genomic DNA. Translation: AAL40091.1.
L75823 mRNA. Translation: AAL40090.1.
AK292313 mRNA. Translation: BAF85002.1.
BC004980 mRNA. Translation: AAH04980.1.
BC008061 mRNA. Translation: AAH08061.1.
IPIIPI00294159.
PIRG01789.
RefSeqNP_005975.1. NM_005984.3.
UniGeneHs.111024.

3D structure databases

ProteinModelPortalP53007.
ModBaseSearch...

Protein-protein interaction databases

IntActP53007. 6 interactions.
MINTMINT-1153318.
STRING9606.ENSP00000215882.

Protein family/group databases

TCDB2.A.29.7.2. mitochondrial carrier (MC) family.

PTM databases

PhosphoSiteP53007.

Polymorphism databases

DMDM20141931.

Proteomic databases

PaxDbP53007.
PeptideAtlasP53007.
PRIDEP53007.

Protocols and materials databases

DNASU6576.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215882; ENSP00000215882; ENSG00000100075.
ENST00000598008; ENSP00000472050; ENSG00000268928.
GeneID6576.
KEGGhsa:6576.
UCSCuc002zoy.3. human.

Organism-specific databases

CTD6576.
GeneCardsGC22M019163.
H-InvDBHIX0040279.
HGNCHGNC:10979. SLC25A1.
HPAHPA030183.
MIM190315. gene.
neXtProtNX_P53007.
PharmGKBPA35855.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306627.
HOVERGENHBG103009.
InParanoidP53007.
KOK15100.
OMAFAVTPME.
OrthoDBEOG44BB2X.
PhylomeDBP53007.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP53007.
BgeeP53007.
CleanExHS_SLC25A1.
GenevestigatorP53007.
GermOnlineENSG00000100075. Homo sapiens.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSPR00926. MITOCARRIER.
SUPFAMSSF103506. Mitoch_carrier. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC25A1. human.
GenomeRNAi6576.
NextBio25587.
SOURCESearch...

Entry information

Entry nameTXTP_HUMAN
AccessionPrimary (citable) accession number: P53007
Secondary accession number(s): A8K8E8, Q9BSK6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 11, 2002
Last modified: May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families