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Q9CR62 (M2OM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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:
Mitochondrial 2-oxoglutarate/malate carrier protein

Short name=OGCP
Alternative name(s):
Solute carrier family 25 member 11
Gene names
Name:Slc25a11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism By similarity.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein By similarity.

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

Initiator methionine11Removed By similarity
Chain2 – 314313Mitochondrial 2-oxoglutarate/malate carrier protein
PRO_0000090626

Regions

Transmembrane24 – 4219Helical; Name=1; Potential
Transmembrane83 – 10119Helical; Name=2; Potential
Transmembrane119 – 14022Helical; Name=3; Potential
Transmembrane183 – 20220Helical; Name=4; Potential
Transmembrane222 – 24019Helical; Name=5; Potential
Transmembrane281 – 30020Helical; Name=6; Potential
Repeat23 – 10886Solcar 1
Repeat117 – 20892Solcar 2
Repeat217 – 30690Solcar 3

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue571N6-succinyllysine Ref.5
Modified residue731N6-acetyllysine By similarity
Modified residue1021Phosphotyrosine Ref.4
Modified residue2561N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9CR62 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1B19A5DB093941A3

FASTA31434,155
        10         20         30         40         50         60 
MAATASPGAG RMDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVKNRMQ LSGEGAKTRE 

        70         80         90        100        110        120 
YKTSFHALTS ILKTEGLKGI YTGLSAGLLR QATYTTTRLG IYTVLFERLT GADGTPPGFL 

       130        140        150        160        170        180 
LKALIGMTAG ATGAFVGTPA EVALIRMTAD GRLPADQRRG YKNVFNALVR IAREEGVPTL 

       190        200        210        220        230        240 
WRGCIPTMAR AVVVNAAQLA SYSQSKQFLL DSGYFSDNIL CHFCASMISG LVTTAASMPV 

       250        260        270        280        290        300 
DIVKTRIQNM RMIDGKPEYK NGLDVLLKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL 

       310 
EQMNKAYKRL FLSG 

« 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.
Tissue: Tongue.
[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: C57BL/6J.
Tissue: Mammary gland.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-90; 99-146; 163-170; 174-182; 191-206 AND 289-205, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[5]"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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009824 mRNA. Translation: BAB26524.1.
AK009487 mRNA. Translation: BAB26319.1.
BC003455 mRNA. Translation: AAH03455.1.
BC019631 mRNA. Translation: AAH19631.1.
RefSeqNP_077173.1. NM_024211.3.
UniGeneMm.296082.
Mm.466994.

3D structure databases

ProteinModelPortalQ9CR62.
SMRQ9CR62. Positions 22-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212490. 2 interactions.
IntActQ9CR62. 5 interactions.
MINTMINT-1851446.

Protein family/group databases

TCDB2.A.29.2.11. the mitochondrial carrier (mc) family.

PTM databases

PhosphoSiteQ9CR62.

Proteomic databases

PaxDbQ9CR62.
PRIDEQ9CR62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000014750; ENSMUSP00000014750; ENSMUSG00000014606.
GeneID67863.
KEGGmmu:67863.
UCSCuc007jvr.2. mouse.

Organism-specific databases

CTD8402.
MGIMGI:1915113. Slc25a11.

Phylogenomic databases

eggNOGNOG300113.
GeneTreeENSGT00750000117384.
HOGENOMHOG000165139.
HOVERGENHBG009528.
InParanoidQ9CR62.
KOK15104.
OMAFRISKHE.
OrthoDBEOG793B7Z.
PhylomeDBQ9CR62.
TreeFamTF354262.

Gene expression databases

ArrayExpressQ9CR62.
BgeeQ9CR62.
GenevestigatorQ9CR62.

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

ChiTaRSSLC25A11. mouse.
NextBio325753.
PROQ9CR62.
SOURCESearch...

Entry information

Entry nameM2OM_MOUSE
AccessionPrimary (citable) accession number: Q9CR62
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 112 of the entry and version 3 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