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P26855 (ATP9_MARPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP synthase subunit 9, mitochondrial
Alternative name(s):
Lipid-binding protein
Gene names
Name:ATP9
Encoded onMitochondrion
OrganismMarchantia polymorpha (Liverwort) (Marchantia aquatica)
Taxonomic identifier3197 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaMarchantiophytaMarchantiopsidaMarchantiidaeMarchantialesMarchantiaceaeMarchantia

Protein attributes

Sequence length74 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7474ATP synthase subunit 9, mitochondrial
PRO_0000112216

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane45 – 7228Helical; Potential

Sites

Site571Reversibly protonated during proton transport By similarity

Sequences

Sequence LengthMass (Da)Tools
P26855 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: CA94C81A0E58F5E3

FASTA747,534
        10         20         30         40         50         60 
MLEGAKLIGA GAATIALAGA AVGIGNVFSS LINSVARNPS LAKQLFGYAI LGFALTEAIA 

        70 
LFALMMAFLI LFVF 

« Hide

References

[1]"Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome."
Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K., Kanegae T., Ogura Y., Kohchi T., Ohyama K.
J. Mol. Biol. 223:1-7(1992) [PubMed: 1731062] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68929 Genomic DNA. Translation: AAC09459.1.
PIRS25960.
RefSeqNP_054462.1. NC_001660.1.

3D structure databases

ProteinModelPortalP26855.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2702626.

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.
SUPFAMSSF81333. ATPase_F0/V0_c. 1 hit.
PROSITEPS00605. ATPASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATP9_MARPO
AccessionPrimary (citable) accession number: P26855
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families