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Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATP5C1

Organism
Bos taurus (Bovine)
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

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.
R-BTA-8949613. Cristae formation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:ATP5C1
Synonyms:ATP5C
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 13

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL612444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25Mitochondrion2 PublicationsAdd BLAST25
ChainiPRO_000000268426 – 298ATP synthase subunit gamma, mitochondrialAdd BLAST273

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei39N6-acetyllysineBy similarity1
Modified residuei49N6-succinyllysineBy similarity1
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei115N6-acetyllysine; alternateBy similarity1
Modified residuei115N6-succinyllysine; alternateBy similarity1
Modified residuei146PhosphoserineBy similarity1
Modified residuei154N6-acetyllysine; alternateBy similarity1
Modified residuei154N6-succinyllysine; alternateBy similarity1
Modified residuei197N6-acetyllysineBy similarity1
Modified residuei270N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP05631.
PeptideAtlasiP05631.
PRIDEiP05631.

PTM databases

iPTMnetiP05631.

Expressioni

Gene expression databases

BgeeiENSBTAG00000013930.

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 MP68.3 Publications

Protein-protein interaction databases

CORUMiP05631.
DIPiDIP-47546N.
IntActiP05631. 6 interactors.
MINTiMINT-5006919.
STRINGi9913.ENSBTAP00000018505.

Chemistry databases

BindingDBiP05631.

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 60Combined sources33
Beta strandi61 – 64Combined sources4
Helixi106 – 112Combined sources7
Helixi135 – 141Combined sources7
Turni142 – 144Combined sources3
Beta strandi147 – 149Combined sources3
Beta strandi157 – 159Combined sources3
Helixi163 – 171Combined sources9
Beta strandi174 – 176Combined sources3
Beta strandi190 – 192Combined sources3
Helixi235 – 295Combined sources61

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BMFX-ray2.85G26-297[»]
1COWX-ray3.10G26-297[»]
1E1QX-ray2.61G26-297[»]
1E1RX-ray2.50G26-297[»]
1E79X-ray2.40G26-297[»]
1EFRX-ray3.10G26-297[»]
1H8EX-ray2.00G26-297[»]
1H8HX-ray2.90G26-297[»]
1NBMX-ray3.00G26-297[»]
1OHHX-ray2.80G26-297[»]
1QO1X-ray3.90G26-69[»]
G102-115[»]
G234-297[»]
1W0JX-ray2.20G26-297[»]
1W0KX-ray2.85G26-297[»]
2CK3X-ray1.90G26-297[»]
2JDIX-ray1.90G26-298[»]
2JIZX-ray2.30G/N26-297[»]
2JJ1X-ray2.70G/N26-297[»]
2JJ2X-ray2.40G/N26-297[»]
2V7QX-ray2.10G26-297[»]
2W6EX-ray6.50G1-298[»]
2W6FX-ray6.00G1-298[»]
2W6GX-ray6.00G1-298[»]
2W6HX-ray5.00G1-298[»]
2W6IX-ray4.00G1-298[»]
2W6JX-ray3.84G1-298[»]
2WSSX-ray3.20G/P26-297[»]
2XNDX-ray3.50G26-297[»]
4ASUX-ray2.60G26-298[»]
4TSFX-ray3.20G26-298[»]
4TT3X-ray3.21G26-298[»]
4YXWX-ray3.10G26-298[»]
4Z1MX-ray3.30G26-298[»]
5ARAelectron microscopy6.70G26-298[»]
5AREelectron microscopy7.40G26-298[»]
5ARHelectron microscopy7.20G26-298[»]
5ARIelectron microscopy7.40G26-298[»]
5FIJelectron microscopy7.40G26-298[»]
5FIKelectron microscopy6.40G26-298[»]
5FILelectron microscopy7.10G26-298[»]
ProteinModelPortaliP05631.
SMRiP05631.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05631.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1531. Eukaryota.
COG0224. LUCA.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiP05631.
KOiK02136.
OMAiDRGMCGG.
OrthoDBiEOG091G0XX7.
TreeFamiTF105765.

Family and domain databases

CDDicd12151. F1-ATPase_gamma. 1 hit.
InterProiView protein in InterPro
IPR035968. ATP_synth_F1_ATPase_gsu.
IPR000131. ATP_synth_F1_gsu.
IPR023632. ATP_synth_F1_gsu_CS.
PfamiView protein in Pfam
PF00231. ATP-synt. 1 hit.
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiView protein in PROSITE
PS00153. ATPASE_GAMMA. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Liver (identifier: P05631-1) [UniParc]FASTAAdd to basket
Also known as: L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM
60 70 80 90 100
VAAAKYARAE RELKPARVYG VGSLALYEKA DIKTPEDKKK HLIIGVSSDR
110 120 130 140 150
GLCGAIHSSV AKQMKSEAAN LAAAGKEVKI IGVGDKIRSI LHRTHSDQFL
160 170 180 190 200
VTFKEVGRRP PTFGDASVIA LELLNSGYEF DEGSIIFNRF RSVISYKTEE
210 220 230 240 250
KPIFSLDTIS SAESMSIYDD IDADVLRNYQ EYSLANIIYY SLKESTTSEQ
260 270 280 290
SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
Length:298
Mass (Da):33,072
Last modified:June 1, 1994 - v3
Checksum:iC1F41767CDABAD92
GO
Isoform Heart (identifier: P05631-2) [UniParc]FASTAAdd to basket
Also known as: H

The sequence of this isoform differs from the canonical sequence as follows:
     298-298: Missing.

Show »
Length:297
Mass (Da):32,957
Checksum:i241767CDABAD92D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti249E → G in AAI02467 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000438298Missing in isoform Heart. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55389 mRNA. Translation: CAA39064.1.
M22463 Genomic DNA. Translation: AAA30398.1.
BC102466 mRNA. Translation: AAI02467.1.
PIRiA32019. PWBOG.
RefSeqiNP_001068604.1. NM_001075136.2.
XP_005214178.1. XM_005214121.3. [P05631-2]
XP_005214179.1. XM_005214122.3. [P05631-2]
UniGeneiBt.20727.

Genome annotation databases

EnsembliENSBTAT00000018505; ENSBTAP00000018505; ENSBTAG00000013930. [P05631-1]
GeneIDi327668.
KEGGibta:327668.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiATPG_BOVIN
AccessioniPrimary (citable) accession number: P05631
Secondary accession number(s): Q3T0B4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: June 1, 1994
Last modified: November 22, 2017
This is version 164 of the entry and version 3 of the sequence. See 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