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Reviewed, UniProtKB/Swiss-Prot P60115 (ATP9_OENBI)

Last modified October 13, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP synthase subunit 9, mitochondrial
    EC=3.6.3.14
Alternative name(s):
    Lipid-binding protein
Gene names
Name: ATP9
Encoded onMitochondrion
OrganismOenothera biennis (German evening primrose)
Taxonomic identifier3942 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsMyrtalesOnagraceaeOenothera

Protein attributes

Sequence length74 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

Subcellular location

Mitochondrion membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ATPase C chain family.

RNA editing

Edited at positions 7, 10, 64 and 75.
The stop codon at position 75 is created by RNA editing. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7474ATP synthase subunit 9, mitochondrial
PRO_0000112217

Regions

Transmembrane8 – 2821 Potential
Transmembrane50 – 7021 Potential

Sites

Site571Reversibly protonated during proton transport By similarity

Sequences

Sequence LengthMass (Da)Tools
P60115-1 [UniParc].

Last modified November 28, 2003. Version 1.
Checksum: 65932942A7555E82

FASTA747,589
        10         20         30         40         50         60 
MLEGAKLMGA GAATIALAGA AIGIGNVFSS LIHSVARNPS LAKQLFGYAI LGFALTEAIA 

        70 
LFALMMAFLI LFVF 

« Hide

References

[1]"Conserved sequence elements at putative processing sites in plant mitochondria."
Schuster W., Brennicke A.
Curr. Genet. 15:187-192(1989) [PubMed: 2766381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"RNA editing of ATPase subunit 9 transcripts in Oenothera mitochondria."
Schuster W., Brennicke A.
FEBS Lett. 268:252-256(1990) [PubMed: 1696551] [Abstract]
Cited for: RNA EDITING.

Cross-references

Sequence databases

X15765 Genomic DNA. Translation: CAA33771.1. Sequence problems.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.6.3.14. 308107.

Family and domain databases

InterProIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_F0/V0-cplx_csu.
[Graphical view]
Gene3DG3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
PfamPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSPR00124. ATPASEC.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATP9_OENBI
AccessionPrimary (citable) accession number: P60115
Secondary accession number(s): P14572
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: October 13, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents