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Protein

ATP synthase subunit gamma, mitochondrial

Gene

Atp5c1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:Atp5c1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1261437. Atp5c1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. membrane Source: MGI
  3. mitochondrial inner membrane Source: MGI
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. mitochondrion Source: MGI
  6. myelin sheath Source: UniProtKB
  7. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionAdd
BLAST
Chaini26 – 298273ATP synthase subunit gamma, mitochondrialPRO_0000002686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysine1 Publication
Modified residuei49 – 491N6-succinyllysine1 Publication
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysine; alternate1 Publication
Modified residuei115 – 1151N6-succinyllysine; alternate1 Publication
Modified residuei138 – 1381N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine; alternate1 Publication
Modified residuei154 – 1541N6-succinyllysine; alternate1 Publication
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ91VR2.
PaxDbiQ91VR2.
PRIDEiQ91VR2.

2D gel databases

UCD-2DPAGEQ91VR2.

PTM databases

PhosphoSiteiQ91VR2.

Expressioni

Gene expression databases

BgeeiQ91VR2.
ExpressionAtlasiQ91VR2. baseline and differential.
GenevestigatoriQ91VR2.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi198255. 6 interactions.
IntActiQ91VR2. 7 interactions.
MINTiMINT-1842256.

Structurei

3D structure databases

ProteinModelPortaliQ91VR2.
SMRiQ91VR2. Positions 26-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiQ91VR2.
KOiK02136.
OMAiLYWALAE.
PhylomeDBiQ91VR2.
TreeFamiTF105765.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91VR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM
60 70 80 90 100
VAAAKYARAE RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR
110 120 130 140 150
GLCGAIHSSV AKQMKNEVAA LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL
160 170 180 190 200
VSFKDVGRKP PTFGDASVIA LELLNSGYEF DEGSIIFNQF KSVISYKTEE
210 220 230 240 250
KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY SLKESTTSEQ
260 270 280 290
SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
Length:298
Mass (Da):32,886
Last modified:December 1, 2001 - v1
Checksum:i9BD63134AEFF3ABA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC010700 mRNA. Translation: AAH10700.1.
CCDSiCCDS38045.1.
RefSeqiNP_065640.2. NM_020615.4.
UniGeneiMm.12677.

Genome annotation databases

EnsembliENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
GeneIDi11949.
KEGGimmu:11949.
UCSCiuc008ihm.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC010700 mRNA. Translation: AAH10700.1.
CCDSiCCDS38045.1.
RefSeqiNP_065640.2. NM_020615.4.
UniGeneiMm.12677.

3D structure databases

ProteinModelPortaliQ91VR2.
SMRiQ91VR2. Positions 26-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198255. 6 interactions.
IntActiQ91VR2. 7 interactions.
MINTiMINT-1842256.

PTM databases

PhosphoSiteiQ91VR2.

2D gel databases

UCD-2DPAGEQ91VR2.

Proteomic databases

MaxQBiQ91VR2.
PaxDbiQ91VR2.
PRIDEiQ91VR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
GeneIDi11949.
KEGGimmu:11949.
UCSCiuc008ihm.3. mouse.

Organism-specific databases

CTDi509.
MGIiMGI:1261437. Atp5c1.

Phylogenomic databases

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiQ91VR2.
KOiK02136.
OMAiLYWALAE.
PhylomeDBiQ91VR2.
TreeFamiTF105765.

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiAtp5c1. mouse.
NextBioi280065.
PROiQ91VR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VR2.
ExpressionAtlasiQ91VR2. baseline and differential.
GenevestigatoriQ91VR2.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  2. Lubec G., Kang S.U.
    Submitted (MAR-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(2012) [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(2012) [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.

Entry informationi

Entry nameiATPG_MOUSE
AccessioniPrimary (citable) accession number: Q91VR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.