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Protein

Mitochondrial pyruvate carrier 2

Gene

Mpc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the uptake of pyruvate into mitochondria.1 Publication

GO - Biological processi

  • mitochondrial acetyl-CoA biosynthetic process from pyruvate Source: MGI
  • mitochondrial pyruvate transmembrane transport Source: MGI
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial pyruvate carrier 2
Alternative name(s):
Brain protein 44
Gene namesi
Name:Mpc2
Synonyms:Brp44
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1917706. Mpc2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei41 – 6121HelicalSequence analysisAdd
BLAST
Transmembranei73 – 9018HelicalSequence analysisAdd
BLAST
Transmembranei93 – 11523HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Mitochondrial pyruvate carrier 2PRO_0000212794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D023.
MaxQBiQ9D023.
PaxDbiQ9D023.
PeptideAtlasiQ9D023.
PRIDEiQ9D023.

PTM databases

iPTMnetiQ9D023.
PhosphoSiteiQ9D023.

Expressioni

Gene expression databases

BgeeiQ9D023.
CleanExiMM_BRP44.
ExpressionAtlasiQ9D023. baseline and differential.
GenevisibleiQ9D023. MM.

Interactioni

Subunit structurei

The functional 150 kDa pyruvate import complex is a heteromer of MPC1 and MPC2.1 Publication

Protein-protein interaction databases

BioGridi214064. 1 interaction.
IntActiQ9D023. 3 interactions.
MINTiMINT-1846500.
STRINGi10090.ENSMUSP00000027853.

Structurei

3D structure databases

ProteinModelPortaliQ9D023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1589. Eukaryota.
ENOG4111UER. LUCA.
GeneTreeiENSGT00510000047120.
HOGENOMiHOG000188910.
HOVERGENiHBG023934.
InParanoidiQ9D023.
OMAiASYHRIL.
OrthoDBiEOG7W155Q.
PhylomeDBiQ9D023.
TreeFamiTF300066.

Family and domain databases

InterProiIPR005336. MPC.
[Graphical view]
PfamiPF03650. MPC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGARGLR ATYHRLMDKV ELLLPKKLRP LYNHPAGPRT VFFWAPIMKW
60 70 80 90 100
GLVCAGLADM ARPAEKLSTA QSTVLMATGF IWSRYSLVII PKNWSLFAVN
110 120
FFVGSAGASQ LFRIWRYNQE LKSKGIQ
Length:127
Mass (Da):14,286
Last modified:June 1, 2001 - v1
Checksum:iBE8AEC9DF74405A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002233 mRNA. Translation: BAC24983.1.
AK011889 mRNA. Translation: BAB27898.1.
AK151522 mRNA. Translation: BAE30471.1.
BC018324 mRNA. Translation: AAH18324.1.
CCDSiCCDS15442.1.
RefSeqiNP_081706.1. NM_027430.2.
UniGeneiMm.195625.
Mm.450001.

Genome annotation databases

EnsembliENSMUST00000027853; ENSMUSP00000027853; ENSMUSG00000026568.
GeneIDi70456.
KEGGimmu:70456.
UCSCiuc007djd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002233 mRNA. Translation: BAC24983.1.
AK011889 mRNA. Translation: BAB27898.1.
AK151522 mRNA. Translation: BAE30471.1.
BC018324 mRNA. Translation: AAH18324.1.
CCDSiCCDS15442.1.
RefSeqiNP_081706.1. NM_027430.2.
UniGeneiMm.195625.
Mm.450001.

3D structure databases

ProteinModelPortaliQ9D023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214064. 1 interaction.
IntActiQ9D023. 3 interactions.
MINTiMINT-1846500.
STRINGi10090.ENSMUSP00000027853.

PTM databases

iPTMnetiQ9D023.
PhosphoSiteiQ9D023.

Proteomic databases

EPDiQ9D023.
MaxQBiQ9D023.
PaxDbiQ9D023.
PeptideAtlasiQ9D023.
PRIDEiQ9D023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027853; ENSMUSP00000027853; ENSMUSG00000026568.
GeneIDi70456.
KEGGimmu:70456.
UCSCiuc007djd.1. mouse.

Organism-specific databases

CTDi25874.
MGIiMGI:1917706. Mpc2.

Phylogenomic databases

eggNOGiKOG1589. Eukaryota.
ENOG4111UER. LUCA.
GeneTreeiENSGT00510000047120.
HOGENOMiHOG000188910.
HOVERGENiHBG023934.
InParanoidiQ9D023.
OMAiASYHRIL.
OrthoDBiEOG7W155Q.
PhylomeDBiQ9D023.
TreeFamiTF300066.

Miscellaneous databases

PROiQ9D023.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D023.
CleanExiMM_BRP44.
ExpressionAtlasiQ9D023. baseline and differential.
GenevisibleiQ9D023. MM.

Family and domain databases

InterProiIPR005336. MPC.
[Graphical view]
PfamiPF03650. MPC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    Tissue: Bone marrow, Embryo and Kidney.
  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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "Identification and functional expression of the mitochondrial pyruvate carrier."
    Herzig S., Raemy E., Montessuit S., Veuthey J.L., Zamboni N., Westermann B., Kunji E.R., Martinou J.C.
    Science 337:93-96(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  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-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMPC2_MOUSE
AccessioniPrimary (citable) accession number: Q9D023
Secondary accession number(s): Q3UA44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.