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Q91VR2 (ATPG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene names
Name:Atp5c1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.

Subcellular location

Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the ATPase gamma chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 298273ATP synthase subunit gamma, mitochondrial
PRO_0000002686

Amino acid modifications

Modified residue391N6-acetyllysine Ref.4
Modified residue491N6-succinyllysine Ref.3
Modified residue551N6-acetyllysine By similarity
Modified residue1151N6-acetyllysine; alternate Ref.4
Modified residue1151N6-succinyllysine; alternate Ref.3
Modified residue1381N6-acetyllysine Ref.4
Modified residue1541N6-acetyllysine; alternate Ref.4
Modified residue1541N6-succinyllysine; alternate Ref.3
Modified residue1971N6-acetyllysine By similarity
Modified residue2701N6-succinyllysine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q91VR2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9BD63134AEFF3ABA

FASTA29832,886
        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 

« Hide

References

« Hide '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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[3]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-49; LYS-115; LYS-154 AND LYS-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-115; LYS-138 AND LYS-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC010700 mRNA. Translation: AAH10700.1.
RefSeqNP_065640.2. NM_020615.4.
UniGeneMm.12677.

3D structure databases

ProteinModelPortalQ91VR2.
SMRQ91VR2. Positions 26-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198255. 5 interactions.
IntActQ91VR2. 7 interactions.
MINTMINT-1842256.

PTM databases

PhosphoSiteQ91VR2.

2D gel databases

UCD-2DPAGEQ91VR2.

Proteomic databases

PaxDbQ91VR2.
PRIDEQ91VR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
GeneID11949.
KEGGmmu:11949.
UCSCuc008ihm.3. mouse.

Organism-specific databases

CTD509.
MGIMGI:1261437. Atp5c1.

Phylogenomic databases

eggNOGCOG0224.
GeneTreeENSGT00390000006837.
HOGENOMHOG000215911.
HOVERGENHBG000933.
InParanoidQ91VR2.
KOK02136.
OMATKTMKIV.
PhylomeDBQ91VR2.
TreeFamTF105765.

Gene expression databases

BgeeQ91VR2.
GenevestigatorQ91VR2.

Family and domain databases

InterProIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERPTHR11693. PTHR11693. 1 hit.
PfamPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSPR00126. ATPASEGAMMA.
SUPFAMSSF52943. SSF52943. 1 hit.
TIGRFAMsTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5C1. mouse.
NextBio280065.
PROQ91VR2.
SOURCESearch...

Entry information

Entry nameATPG_MOUSE
AccessionPrimary (citable) accession number: Q91VR2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot