P18238 · ADT3_YEAST

Function

function

ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:2165073).
Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).

Miscellaneous

Present with 1080 molecules/cell in log phase SD medium.

Catalytic activity

Activity regulation

The matrix-open state (m-state) is inhibited by the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open state (c-state) is inhibited by the membrane-impermeable toxic inhibitor carboxyatractyloside (CATR).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site85ADP (UniProtKB | ChEBI)
Binding site97ADP (UniProtKB | ChEBI)
Binding site241ADP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Molecular FunctionATP:ADP antiporter activity
Molecular Functionidentical protein binding
Biological Processanaerobic respiration
Biological Processheme transport
Biological Processmitochondrial ADP transmembrane transport
Biological Processmitochondrial ATP transmembrane transport
Biological Processtransmembrane transport

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    ADP,ATP carrier protein 3
  • Alternative names
    • ADP/ATP translocase 3
    • Adenine nucleotide translocator 3 (ANT 3)

Gene names

    • Name
      AAC3
    • ORF names
      YBR0753
    • Ordered locus names
      YBR085W

Organism names

Accessions

  • Primary accession
    P18238
  • Secondary accessions
    • D6VQ85

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-39Helical; Name=1
Transmembrane80-104Helical; Name=2
Transmembrane112-132Helical; Name=3
Transmembrane182-203Helical; Name=4
Transmembrane217-237Helical; Name=5
Transmembrane277-297Helical; Name=6

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000905951-307ADP,ATP carrier protein 3

Proteomic databases

PTM databases

Interaction

Subunit

Monomer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P18238AAC3 P182382EBI-2300, EBI-2300

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for repeat, region, motif.

TypeIDPosition(s)Description
Repeat10-103Solcar 1
Repeat114-206Solcar 2
Repeat214-300Solcar 3
Region241-246Important for transport activity
Motif241-246Nucleotide carrier signature motif

Domain

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.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    307
  • Mass (Da)
    33,313
  • Last updated
    1990-11-01 v1
  • Checksum
    D0C1329FEC1B4DC8
MSSDAKQQETNFAINFLMGGVSAAIAKTAASPIERVKILIQNQDEMIKQGTLDKKYSGIVDCFKRTAKQEGLISFWRGNTANVIRYFPTQALNFAFKDKIKLMFGFKKEEGYGKWFAGNLASGGAAGALSLLFVYSLDFARTRLAADAKSSKKGGARQFNGLTDVYKKTLKSDGIAGLYRGFMPSVVGIVVYRGLYFGMFDSLKPLVLTGSLDGSFLASFLLGWVVTTGASTCSYPLDTVRRRMMMTSGQAVKYNGAIDCLKKIVASEGVGSLFKGCGANILRSVAGAGVISMYDQLQMILFGKKFK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M34076
EMBL· GenBank· DDBJ
AAA97485.1
EMBL· GenBank· DDBJ
Genomic DNA
Z35954
EMBL· GenBank· DDBJ
CAA85031.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006936
EMBL· GenBank· DDBJ
DAA07205.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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