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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	ADP, ATP

Structure:
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
4C9G 4C9H

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CDD Search (Conserved Domain Database)

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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

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).

Cross database links:

Gene Ontology

References (7)

External Searches:

Analyze:

2.A.29.1.7ADP: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).

Cross database links:

Gene Ontology

References (7)

External Searches:

Analyze:

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).