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2.A.29.1.9
ADP/ATP carrier #3, AAC3 (90% identical to 2.A.29.1.7) (#2)). Prolines in TMSs 1,3, and 5 are important for function (Babot et al., 2012).  The x-ray structure suggests a novel domain-based alternating-access transport mechanism (Ruprecht et al. 2014).  Although the transporter catalyzes the translocation of substrate, the substrate also facilitates interconversion between alternating states (Brüschweiler et al. 2015).

Accession Number:P18238
Protein Name:ADP,ATP carrier protein 3
Length:307
Molecular Weight:33313.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Mitochondrion inner membrane1 / Multi-pass membrane protein2
Substrate ADP, ATP

Cross database links:

DIP: DIP-6289N
Entrez Gene ID: 852380   
Pfam: PF00153   
KEGG: sce:YBR085W   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005743 C:mitochondrial inner membrane
GO:0005488 F:binding
GO:0005215 F:transporter activity
GO:0009061 P:anaerobic respiration
GO:0015886 P:heme transport
GO:0055085 P:transmembrane transport

References (3)

[1] “A third ADP/ATP translocator gene in yeast.”  Kolarov J.et.al.   2165073
[2] “Complete DNA sequence of yeast chromosome II.”  Feldmann H.et.al.   7813418
[3] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
Structure:
4C9J   4C9Q     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MSSDAKQQET NFAINFLMGG VSAAIAKTAA SPIERVKILI QNQDEMIKQG TLDKKYSGIV 
61:	DCFKRTAKQE GLISFWRGNT ANVIRYFPTQ ALNFAFKDKI KLMFGFKKEE GYGKWFAGNL 
121:	ASGGAAGALS LLFVYSLDFA RTRLAADAKS SKKGGARQFN GLTDVYKKTL KSDGIAGLYR 
181:	GFMPSVVGIV VYRGLYFGMF DSLKPLVLTG SLDGSFLASF LLGWVVTTGA STCSYPLDTV 
241:	RRRMMMTSGQ AVKYNGAIDC LKKIVASEGV GSLFKGCGAN ILRSVAGAGV ISMYDQLQMI 
301:	LFGKKFK