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2.A.29.1.7
ADP:ATP carrier 2, Aac2 (Lethal with loss of Sal1, (2.A.29.23.2) but independent of its AAC activity (Kucejova et al., 2008)).  The x-ray structure suggests a novel domain-based alternating-access transport mechanism (Ruprecht et al. 2014).

Accession Number:P18239
Protein Name:Aac2
Length:318
Molecular Weight:34426.00
Species:(Baker's yeast) [4932]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Mitochondrion inner membrane1 / Multi-pass membrane protein2
Substrate ATP, ADP

Cross database links:

Genevestigator: P18239
eggNOG: fuNOG06875
HEGENOM: HBG610399
DIP: DIP-2917N
RefSeq: NP_009523.1   
Entrez Gene ID: 852250   
Pfam: PF00153   
KEGG: sce:YBL030C   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005743 C:mitochondrial inner membrane
GO:0005471 F:ATP:ADP antiporter activity
GO:0005488 F:binding
GO:0015866 P:ADP transport
GO:0009060 P:aerobic respiration
GO:0009061 P:anaerobic respiration
GO:0006915 P:apoptosis
GO:0015867 P:ATP transport
GO:0015886 P:heme transport
GO:0006839 P:mitochondrial transport
GO:0055085 P:transmembrane transport

References (7)

[1] “Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae. Isolation and analysis of AAC2.”  Lawson J.E.et.al.   2844786
[2] “A third ADP/ATP translocator gene in yeast.”  Kolarov J.et.al.   2165073
[3] “Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen.”  van Dyck L.et.al.   7725803
[4] “Complete DNA sequence of yeast chromosome II.”  Feldmann H.et.al.   7813418
[5] “Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.”  Nelson D.R.et.al.   8487299
[6] “Function-based mapping of the yeast mitochondrial ADP/ATP translocator by selection for second site revertants.”  Nelson D.R.et.al.   7683726
[7] “Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.”  Reinders J.et.al.   17761666
Structure:
4C9G   4C9H     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSSNAQVKTP LPPAPAPKKE SNFLIDFLMG GVSAAVAKTA ASPIERVKLL IQNQDEMLKQ 
61:	GTLDRKYAGI LDCFKRTATQ EGVISFWRGN TANVIRYFPT QALNFAFKDK IKAMFGFKKE 
121:	EGYAKWFAGN LASGGAAGAL SLLFVYSLDY ARTRLAADSK SSKKGGARQF NGLIDVYKKT 
181:	LKSDGVAGLY RGFLPSVVGI VVYRGLYFGM YDSLKPLLLT GSLEGSFLAS FLLGWVVTTG 
241:	ASTCSYPLDT VRRRMMMTSG QAVKYDGAFD CLRKIVAAEG VGSLFKGCGA NILRGVAGAG 
301:	VISMYDQLQM ILFGKKFK