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Protein

ATP synthase subunit gamma, mitochondrial

Gene

Atp5c1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

  • ATP metabolic process Source: RGD
  • ATP synthesis coupled proton transport Source: InterPro
  • oxidative phosphorylation Source: RGD
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:Atp5c1
Synonyms:Atp5c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620011. Atp5c1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial envelope Source: RGD
  • mitochondrial inner membrane Source: RGD
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273ATP synthase subunit gamma, mitochondrialPRO_0000073430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei24 – 241N6-succinyllysineBy similarity
Modified residuei30 – 301N6-acetyllysineBy similarity
Modified residuei90 – 901N6-acetyllysine; alternateBy similarity
Modified residuei90 – 901N6-succinyllysine; alternateBy similarity
Modified residuei113 – 1131N6-acetyllysineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei172 – 1721N6-acetyllysineBy similarity
Modified residuei245 – 2451N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP35435.
PRIDEiP35435.

2D gel databases

World-2DPAGE0004:P35435.

PTM databases

iPTMnetiP35435.
PhosphoSiteiP35435.

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 MP68.1 Publication

Protein-protein interaction databases

BioGridi250485. 1 interaction.
IntActiP35435. 2 interactions.
STRINGi10116.ENSRNOP00000049879.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 4136Combined sources
Turni43 – 464Combined sources
Turni81 – 877Combined sources
Helixi212 – 23221Combined sources
Helixi234 – 25825Combined sources
Helixi261 – 2699Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80G5-273[»]
2F43X-ray3.00G1-273[»]
ProteinModelPortaliP35435.
SMRiP35435. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35435.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Phylogenomic databases

eggNOGiKOG1531. Eukaryota.
KOG2389. Eukaryota.
COG0224. LUCA.
HOVERGENiHBG000933.
InParanoidiP35435.

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.

P35435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ATLKDITRRL KSIKNIQKIT KSMKMVAAAK YARAERELKP ARVYGTGSLA
60 70 80 90 100
LYEKAEIKGP EDKKKHLIIG VSSDRGLCGA IHSSVAKQMK NDMAALTAAG
110 120 130 140 150
KEVMIVGIGE KIKSILYRTH SDQFLVSFKD VGRKPPTFGD ASVIALELLN
160 170 180 190 200
SGYEFDEGSI IFNQFKSVIS YKTEEKPIFS FSTVVAAENM SIYDDIDADV
210 220 230 240 250
LQNYQEYNLA NIIYYSLKES TTSEQSARMT AMDNASKNAS DMIDKLTLTF
260 270
NRTRQAVITK ELIEIISGAA ALD
Length:273
Mass (Da):30,191
Last modified:February 1, 1995 - v2
Checksum:iBD02D3F7F7583916
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41K → R in AAA41776 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19927 mRNA. Translation: AAA41776.1.
PIRiA33160.
RefSeqiXP_006254293.1. XM_006254231.2.
UniGeneiRn.63959.

Genome annotation databases

GeneIDi116550.
UCSCiRGD:620011. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19927 mRNA. Translation: AAA41776.1.
PIRiA33160.
RefSeqiXP_006254293.1. XM_006254231.2.
UniGeneiRn.63959.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80G5-273[»]
2F43X-ray3.00G1-273[»]
ProteinModelPortaliP35435.
SMRiP35435. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250485. 1 interaction.
IntActiP35435. 2 interactions.
STRINGi10116.ENSRNOP00000049879.

PTM databases

iPTMnetiP35435.
PhosphoSiteiP35435.

2D gel databases

World-2DPAGE0004:P35435.

Proteomic databases

PaxDbiP35435.
PRIDEiP35435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116550.
UCSCiRGD:620011. rat.

Organism-specific databases

CTDi509.
RGDi620011. Atp5c1.

Phylogenomic databases

eggNOGiKOG1531. Eukaryota.
KOG2389. Eukaryota.
COG0224. LUCA.
HOVERGENiHBG000933.
InParanoidiP35435.

Miscellaneous databases

EvolutionaryTraceiP35435.
PROiP35435.

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

  1. "Molecular cloning, expression and characterization of the rat liver mitochondrial ATP synthase gamma subunit."
    Choi S.H., Thomas P.J., Lee J.E., Pedersen P.L.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-273.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Godinot C.
    Submitted (FEB-1991) to the PIR data bank
    Cited for: PROTEIN SEQUENCE OF 1-20.
  3. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 91-101, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Identification of two proteins associated with mammalian ATP synthase."
    Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.
    Mol. Cell. Proteomics 6:1690-1699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  5. "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis."
    Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiATPG_RAT
AccessioniPrimary (citable) accession number: P35435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.