P13547 (ATP9_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit 9, mitochondrial

Alternative name(s):
Lipid-binding protein

Gene names

Name:

ATP9

Encoded on

Mitochondrion

Organism

Triticum aestivum (Wheat)

Taxonomic identifier

4565 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	74 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
RNA editing	Edited at positions 7, 28, 45, 64, 71 and 75. The stop codon at position 75 is created by RNA editing.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion
Coding sequence diversity	RNA editing
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 74	74	ATP synthase subunit 9, mitochondrial		PRO_0000112226
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	50 – 70	21	Helical; Potential
Sites
	Site	57	1	Reversibly protonated during proton transport By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13547 [UniParc]. Last modified December 1, 1992. Version 3. Checksum: CA932F847058F5E3	FASTA	74	7,557
	10 20 30 40 50 60 MLEGAKLIGA GAATIALAGA AVGIGNVFSS LIHSVARNPS LAKQLFGYAI LGFALTEAIA 70 LFALMMAFLI LFVF

References

[1]	"Wheat mitochondrial DNA: organization and sequences of the atpA and atp9 genes." Schulte E., Staubach S., Laser B., Kueck U. Nucleic Acids Res. 17:7531-7531(1989) [PubMed: 2529479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparison of the wheat mitochondrial atp9 gene sequence with mitochondrial and chloroplast homologues from other plants." Bonhomme S., Bird S., Bonen L. Plant Mol. Biol. 13:395-397(1989) [PubMed: 2535257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Thatcher.
[3]	"RNA editing of the mitochondrial atp9 transcript from wheat." Nowak C., Kueck U. Nucleic Acids Res. 18:7164-7164(1990) [PubMed: 1702206] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"RNA editing of wheat mitochondrial ATP synthase subunit 9: direct protein and cDNA sequencing." Begu D., Graves P.V., Domec C., Arselin G., Litvak S., Araya A. Plant Cell 2:1283-1290(1990) [PubMed: 1726783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-74.
[5]	"Direct protein sequencing of wheat mitochondrial ATP synthase subunit 9 confirms RNA editing in plants." Graves P.V., Begu D., Velours J., Neau E., Belloc F., Litvak S., Araya A. J. Mol. Biol. 214:1-6(1990) [PubMed: 2196374] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15919 Genomic DNA. Translation: CAA34061.1. Sequence problems. X15083 Genomic DNA. Translation: CAA33193.1. Sequence problems. X54621 mRNA. Translation: CAA38441.1. S47364 mRNA. Translation: AAB23976.1.
PIR	LWWTM. S12631.
RefSeq	YP_398394.1. NC_007579.1.
3D structure databases
ProteinModelPortal	P13547.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3800074.
Organism-specific databases
Gramene	P13547.
Family and domain databases
InterPro	IPR000454. ATPase_F0-cplx_csu. IPR020537. ATPase_F0-cplx_csu_DDCD_BS. IPR002379. ATPase_F0/V0-cplx_csu. [Graphical view]
Gene3D	G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.
Pfam	PF00137. ATP-synt_C. 1 hit. [Graphical view]
PRINTS	PR00124. ATPASEC.
SUPFAM	SSF81333. ATPase_F0/V0_c. 1 hit.
PROSITE	PS00605. ATPASE_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATP9_WHEAT

Accession

Primary (citable) accession number: P13547

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	December 1, 1992
Last modified:	January 25, 2012
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program