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Showing Protein Mitochondrial 2-oxoglutarate/malate carrier protein (HMDBP01116)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP01116
Secondary Accession Numbers
  • 6409
Name Mitochondrial 2-oxoglutarate/malate carrier protein
Synonyms
  1. OGCP
  2. Solute carrier family 25 member 11
Gene Name SLC25A11
Protein Type Enzyme
Biological Properties
General Function Involved in transporter activity
Specific 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.
Pathways
  • Fructose-1,6-diphosphatase deficiency
  • Gluconeogenesis
  • Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
  • Glycogenosis, Type IA. Von gierke disease
  • Glycogenosis, Type IB
  • Glycogenosis, Type IC
  • Malate-Aspartate Shuttle
  • Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
  • Transfer of Acetyl Groups into Mitochondria
  • Triosephosphate isomerase
Reactions Not Available
GO Classification
Biological Process
small molecule metabolic process
gluconeogenesis
Cellular Component
mitochondrial inner membrane
integral to plasma membrane
Component
membrane
cell part
organelle membrane
organelle inner membrane
mitochondrial inner membrane
Function
binding
transporter activity
Molecular Function
oxoglutarate:malate antiporter activity
Process
establishment of localization
transport
transmembrane transport
Cellular Location
  1. Mitochondrion inner membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 17
Locus 17p13.3
SNPs SLC25A11
Gene Sequence 
>945 bp
ATGGCGGCGACGGCGAGTGCCGGGGCCGGCGGGATAGACGGGAAGCCCCGTACCTCCCCT
AAGTCCGTCAAGTTCCTGTTTGGGGGCCTGGCCGGGATGGGAGCTACAGTTTTTGTCCAG
CCCCTGGACCTGGTGAAGAACCGGATGCAGTTGAGCGGGGAAGGGGCCAAGACTCGAGAG
TACAAAACCAGCTTCCATGCCCTCACCAGTATCCTGAAGGCAGAAGGCCTGAGGGGCATT
TACACTGGGCTGTCGGCTGGCCTGCTGCGTCAGGCCACCTACACCACTACCCGCCTTGGC
ATCTATACCGTGCTGTTTGAGCGCCTGACTGGGGCTGATGGTACTCCCCCTGGCTTTCTG
CTGAAGGCTGTGATTGGCATGACCGCAGGTGCCACTGGTGCCTTTGTGGGAACACCAGCC
GAAGTGGCTCTTATCCGCATGACTGCCGATGGCCGGCTTCCAGCTGACCAGCGCCGTGGC
TACAAAAATGTGTTTAACGCCCTGATTCGAATCACCCGGGAAGAGGGTGTCCTCACACTG
TGGCGGGGCTGCATCCCTACCATGGCTCGGGCCGTCGTCGTCAATGCTGCCCAGCTCGCC
TCCTACTCCCAATCCAAGCAGTTCTTACTGGACTCAGGCTACTTCTCTGACAACATCTTG
TGCCACTTCTGTGCCAGCATGATCAGCGGTCTTGTCACCACTGCTGCCTCCATGCCTGTG
GACATTGCCAAGACCCGAATCCAGAACATGCGGATGATTGATGGGAAGCCGGAATACAAG
AACGGGCTGGACGTGCTGTTCAAAGTTGTCCGCTACGAGGGCTTCTTCAGCCTGTGGAAG
GGCTTCACGCCGTACTATGCCCGCCTGGGCCCCCACACCGTCCTCACCTTCATCTTCTTG
GAGCAGATGAACAAGGCCTACAAGCGTCTCTTCCTCAGTGGCTGA
Protein Properties
Number of Residues 314
Molecular Weight 34061.405
Theoretical pI 9.908
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Mitochondrial 2-oxoglutarate/malate carrier protein
MAATASAGAGGIDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTRE
YKTSFHALTSILKAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFL
LKAVIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALIRITREEGVLTL
WRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPV
DIAKTRIQNMRMIDGKPEYKNGLDVLFKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFL
EQMNKAYKRLFLSG
GenBank ID Protein 3387911
UniProtKB/Swiss-Prot ID Q02978
UniProtKB/Swiss-Prot Entry Name M2OM_HUMAN
PDB IDs Not Available
GenBank Gene ID AF070548
GeneCard ID SLC25A11
GenAtlas ID SLC25A11
HGNC ID HGNC:10981
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Iacobazzi V, Palmieri F, Runswick MJ, Walker JE: Sequences of the human and bovine genes for the mitochondrial 2-oxoglutarate carrier. DNA Seq. 1992;3(2):79-88. [PubMed:1457818 ]