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Q8VEM8 (MPCP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Phosphate carrier protein, mitochondrial
Alternative name(s):
Phosphate transport protein
Short name=PTP
Solute carrier family 25 member 3
Gene names
Name:Slc25a3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transport of phosphate groups from the cytosol to mitochondrial matrix. Phosphate is cotransported with H+. May play a role regulation of the mitochondrial permeability transition pore (mPTP) By similarity.

Subunit structure

Interacts with PPIF; the interaction is impaired by CsA By similarity.

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 – 4545Mitochondrion By similarity
Chain46 – 357312Phosphate carrier protein, mitochondrial
PRO_0000019257

Regions

Topological domain46 – 5813Mitochondrial intermembrane Potential
Transmembrane59 – 8123Helical; Name=1; Potential
Topological domain82 – 11635Mitochondrial matrix Potential
Transmembrane117 – 13620Helical; Name=2; Potential
Topological domain137 – 15620Mitochondrial intermembrane Potential
Transmembrane157 – 17822Helical; Name=3; Potential
Topological domain179 – 21335Mitochondrial matrix Potential
Transmembrane214 – 23320Helical; Name=4; Potential
Topological domain234 – 25623Mitochondrial intermembrane Potential
Transmembrane257 – 27923Helical; Name=5; Potential
Topological domain280 – 30930Mitochondrial matrix Potential
Transmembrane310 – 32819Helical; Name=6; Potential
Topological domain329 – 35729Mitochondrial intermembrane Potential
Repeat58 – 14285Solcar 1
Repeat155 – 23985Solcar 2
Repeat256 – 33479Solcar 3

Amino acid modifications

Modified residue941N6-acetyllysine By similarity
Modified residue1911Phosphotyrosine By similarity
Modified residue2041N6-acetyllysine Ref.4 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8VEM8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 2887B9ADF034339E

FASTA35739,632
        10         20         30         40         50         60 
MFSSVAHLAR ANPFNAPHLQ LVHDGLSGPR SPPAPPRRSR HLAAAAVEEY SCEFGSMKYY 

        70         80         90        100        110        120 
ALCGFGGVLS CGLTHTAVVP LDLVKCRMQV DPQKYKGIFN GFSITLKEDG VRGLAKGWAP 

       130        140        150        160        170        180 
TLIGYSMQGL CKFGFYEVFK ALYSNILGEE NTYLWRTSLY LASSASAEFF ADIALAPMEA 

       190        200        210        220        230        240 
AKVRIQTQPG YANTLREAVP KMYKEEGLNA FYKGVAPLWM RQIPYTMMKF ACFERTVEAL 

       250        260        270        280        290        300 
YKFVVPKPRS ECTKAEQLVV TFVAGYIAGV FCAIVSHPAD SVVSVLNKEK GSTASQVLQR 

       310        320        330        340        350 
LGFRGVWKGL FARIIMIGTL TALQWFIYDS VKVYFRLPRP PPPEMPESLK KKLGLTE 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Amnion, Bone marrow, Ovary, Thymus and Uterus.
[2]"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].
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 88-94; 97-107; 117-156; 185-196; 202-242; 291-300 AND 337-350, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK077274 mRNA. Translation: BAC36723.1.
AK077723 mRNA. Translation: BAC36982.1.
AK088013 mRNA. Translation: BAC40095.1.
AK150641 mRNA. Translation: BAE29729.1.
AK150729 mRNA. Translation: BAE29806.1.
AK150870 mRNA. Translation: BAE29921.1.
AK151518 mRNA. Translation: BAE30467.1.
AK152006 mRNA. Translation: BAE30870.1.
AK152292 mRNA. Translation: BAE31101.1.
AK152341 mRNA. Translation: BAE31137.1.
AK167197 mRNA. Translation: BAE39327.1.
AK168580 mRNA. Translation: BAE40449.1.
BC018161 mRNA. Translation: AAH18161.1.
CCDSCCDS24121.1.
RefSeqNP_598429.1. NM_133668.3.
UniGeneMm.298.

3D structure databases

ProteinModelPortalQ8VEM8.
SMRQ8VEM8. Positions 53-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202142. 12 interactions.
DIPDIP-32038N.
IntActQ8VEM8. 5 interactions.
MINTMINT-1842913.

Protein family/group databases

TCDB2.A.29.4.5. the mitochondrial carrier (mc) family.

PTM databases

PhosphoSiteQ8VEM8.

Proteomic databases

MaxQBQ8VEM8.
PaxDbQ8VEM8.
PRIDEQ8VEM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076694; ENSMUSP00000075987; ENSMUSG00000061904.
ENSMUST00000164505; ENSMUSP00000132480; ENSMUSG00000061904.
GeneID18674.
KEGGmmu:18674.
UCSCuc007gtn.1. mouse.

Organism-specific databases

CTD5250.
MGIMGI:1353498. Slc25a3.

Phylogenomic databases

eggNOGNOG265500.
GeneTreeENSGT00390000008708.
HOGENOMHOG000164438.
HOVERGENHBG024440.
InParanoidQ8VEM8.
KOK15102.
OMASAWRQIF.
OrthoDBEOG7KQ228.
PhylomeDBQ8VEM8.
TreeFamTF314119.

Gene expression databases

ArrayExpressQ8VEM8.
BgeeQ8VEM8.
GenevestigatorQ8VEM8.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSslc25a3. mouse.
NextBio294694.
PROQ8VEM8.
SOURCESearch...

Entry information

Entry nameMPCP_MOUSE
AccessionPrimary (citable) accession number: Q8VEM8
Secondary accession number(s): Q542V7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot