Q91VR2 (ATPG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit gamma, mitochondrial

Alternative name(s):
F-ATPase gamma subunit

Gene names

Name:

Atp5c1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
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. Mitochondrion inner membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the ATPase gamma chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion
	Chain	26 – 298	273	ATP synthase subunit gamma, mitochondrial		PRO_0000002686
Amino acid modifications
	Modified residue	55	1	N6-acetyllysine By similarity
	Modified residue	79	1	N6-acetyllysine Ref.3
	Modified residue	90	1	N6-acetyllysine Ref.3
	Modified residue	115	1	N6-acetyllysine Ref.3
	Modified residue	146	1	Phosphoserine Ref.4
	Modified residue	154	1	N6-acetyllysine By similarity
	Modified residue	197	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91VR2 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 9BD63134AEFF3ABA	FASTA	298	32,886
	10 20 30 40 50 60 MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 70 80 90 100 110 120 RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKNEVAA 130 140 150 160 170 180 LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL VSFKDVGRKP PTFGDASVIA LELLNSGYEF 190 200 210 220 230 240 DEGSIIFNQF KSVISYKTEE KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY 250 260 270 280 290 SLKESTTSEQ SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[2]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 68-79; 91-136; 144-154; 263-277 AND 286-298, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[3]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-90 AND LYS-115, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC010700 mRNA. Translation: AAH10700.1.
IPI	IPI00313475.
RefSeq	NP_065640.2. NM_020615.4.
UniGene	Mm.12677.
3D structure databases
ProteinModelPortal	Q91VR2.
SMR	Q91VR2. Positions 26-297.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91VR2. 5 interactions.
STRING	Q91VR2.
PTM databases
PhosphoSite	Q91VR2.
2D gel databases
UCD-2DPAGE	Q91VR2.
Proteomic databases
PRIDE	Q91VR2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
GeneID	11949.
KEGG	mmu:11949.
Organism-specific databases
CTD	509.
MGI	MGI:1261437. Atp5c1.
Phylogenomic databases
HOGENOM	HBG586593.
HOVERGEN	HBG000933.
InParanoid	Q91VR2.
OMA	SARRNAM.
PhylomeDB	Q91VR2.
Gene expression databases
ArrayExpress	Q91VR2.
Bgee	Q91VR2.
Genevestigator	Q91VR2.
GermOnline	ENSMUSG00000025781. Mus musculus.
Family and domain databases
InterPro	IPR000131. ATPase_F1-cplx_gsu. IPR023632. ATPase_F1_gsu_CS. IPR023633. ATPase_F1_gsu_dom. [Graphical view]
KO	K02136.
PANTHER	PTHR11693. ATPase_F1_gamma. 1 hit.
Pfam	PF00231. ATP-synt. 1 hit. [Graphical view]
PRINTS	PR00126. ATPASEGAMMA.
SUPFAM	SSF52943. ATPase_gamma. 1 hit.
TIGRFAMs	TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITE	PS00153. ATPASE_GAMMA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280065.
SOURCE	Search...

Entry information

Entry name

ATPG_MOUSE

Accession

Primary (citable) accession number: Q91VR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program