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P51881 (ADT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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:
ADP/ATP translocase 2
Alternative name(s):
ADP,ATP carrier protein 2
Adenine nucleotide translocator 2
Short name=ANT 2
Solute carrier family 25 member 5

Cleaved into the following chain:

  1. ADP/ATP translocase 2, N-terminally processed
Gene names
Name:Slc25a5
Synonyms:Ant2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length298 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 exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation By similarity.

Subunit structure

Homodimer. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5 By similarity.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Miscellaneous

The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue 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

Chain1 – 298298ADP/ATP translocase 2
PRO_0000423221
Initiator methionine11Removed; alternate Ref.7
Chain2 – 298297ADP/ATP translocase 2, N-terminally processed
PRO_0000090580

Regions

Transmembrane5 – 3935Helical; Name=1; By similarity
Transmembrane75 – 10026Helical; Name=2; By similarity
Transmembrane109 – 14335Helical; Name=3; By similarity
Transmembrane176 – 20227Helical; Name=4; By similarity
Transmembrane207 – 24135Helical; Name=5; By similarity
Transmembrane273 – 29826Helical; Name=6; By similarity
Repeat6 – 9893Solcar 1
Repeat111 – 20191Solcar 2
Repeat212 – 29786Solcar 3
Motif235 – 2406Substrate recognition By similarity

Sites

Binding site801Nucleotide By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylthreonine; in ADP/ATP translocase 2, N-terminally processed Ref.7
Modified residue231N6-acetyllysine; alternate Probable
Modified residue231N6-malonyllysine; alternate By similarity
Modified residue431N6-succinyllysine Ref.9
Modified residue521N6,N6-dimethyllysine; alternate By similarity
Modified residue521N6-methyllysine; alternate By similarity
Modified residue921N6-acetyllysine; alternate Probable
Modified residue921N6-malonyllysine; alternate By similarity
Modified residue961N6-malonyllysine By similarity
Modified residue1051N6-acetyllysine; alternate Ref.9 Ref.10
Modified residue1051N6-succinyllysine; alternate Ref.9
Modified residue1471N6-acetyllysine; alternate Ref.10
Modified residue1471N6-malonyllysine; alternate By similarity
Modified residue1471N6-succinyllysine; alternate Ref.9
Modified residue1551N6-acetyllysine; alternate Ref.10
Modified residue1551N6-succinyllysine; alternate Ref.9
Modified residue1631N6-acetyllysine Ref.10
Modified residue1661N6-acetyllysine Ref.10
Modified residue2681N6-acetyllysine; alternate Ref.10
Modified residue2681N6-succinyllysine; alternate Ref.9

Sequences

Sequence LengthMass (Da)Tools
P51881 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0798E04B987EFE20

FASTA29832,931
        10         20         30         40         50         60 
MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR 

        70         80         90        100        110        120 
IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW RYFAGNLASG 

       130        140        150        160        170        180 
GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFKGLGDC LVKIYKSDGI KGLYQGFNVS 

       190        200        210        220        230        240 
VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI FISWMIAQSV TAVAGLTSYP FDTVRRRMMM 

       250        260        270        280        290 
QSGRKGTDIM YTGTLDCWRK IARDEGSKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT 

« Hide

References

« Hide 'large scale' references
[1]"Rapid evolution of human pseudoautosomal genes and their mouse homologs."
Ellison J.W., Li X., Francke U., Shapiro L.J.
Mamm. Genome 7:25-30(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]Sheldon J.G.
Thesis (1995), University of Cambridge, United Kingdom
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Skeletal muscle.
[3]Costet P., Laplace C.
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/Sv.
[4]Laplace C.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"Expression and sequence analysis of the mouse adenine nucleotide translocase 1 and 2 genes."
Levy S.E., Chen Y.-S., Graham B.H., Wallace D.C.
Gene 254:57-66(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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/6 and FVB/N.
Tissue: Brain and Mammary gland.
[7]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-31; 34-43; 64-72; 81-92; 97-106 AND 189-199, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"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-105, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-105; LYS-147; LYS-155 AND LYS-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[10]"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-105; LYS-147; LYS-155; LYS-163; LYS-166 AND LYS-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27316 mRNA. Translation: AAC52838.1.
U10404 mRNA. Translation: AAA19009.1.
X70847 mRNA. Translation: CAA50196.1.
AF240003 Genomic DNA. Translation: AAF64471.1.
BC004570 mRNA. Translation: AAH04570.1.
BC086756 mRNA. Translation: AAH86756.1.
CCDSCCDS30062.1.
PIRS31814.
RefSeqNP_031477.1. NM_007451.3.
UniGeneMm.371544.

3D structure databases

ProteinModelPortalP51881.
SMRP51881. Positions 2-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198106. 12 interactions.
DIPDIP-31399N.
IntActP51881. 11 interactions.
MINTMINT-1839032.

PTM databases

PhosphoSiteP51881.

Proteomic databases

MaxQBP51881.
PaxDbP51881.
PRIDEP51881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016463; ENSMUSP00000016463; ENSMUSG00000016319.
GeneID11740.
KEGGmmu:11740.
UCSCuc009sxs.1. mouse.

Organism-specific databases

CTD292.
MGIMGI:1353496. Slc25a5.

Phylogenomic databases

eggNOGNOG238123.
HOGENOMHOG000165727.
HOVERGENHBG108348.
InParanoidP51881.
KOK05863.
OMASSYSAMN.
OrthoDBEOG7T1RBR.
PhylomeDBP51881.
TreeFamTF300743.

Gene expression databases

BgeeP51881.
GenevestigatorP51881.

Family and domain databases

Gene3D1.50.40.10. 1 hit.
InterProIPR002113. Aden_trnslctor.
IPR002067. Mit_carrier.
IPR018108. Mitochondrial_sb/sol_carrier.
IPR023395. Mt_carrier_dom.
[Graphical view]
PfamPF00153. Mito_carr. 3 hits.
[Graphical view]
PRINTSPR00927. ADPTRNSLCASE.
PR00926. MITOCARRIER.
SUPFAMSSF103506. SSF103506. 1 hit.
PROSITEPS50920. SOLCAR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio279467.
PROP51881.
SOURCESearch...

Entry information

Entry nameADT2_MOUSE
AccessionPrimary (citable) accession number: P51881
Secondary accession number(s): Q61311
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 131 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