UniProtKB - P05631 (ATPG_BOVIN)
ATP synthase subunit gamma, mitochondrial
ATP5F1C
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
- proton-transporting ATP synthase activity, rotational mechanism Source: Ensembl
GO - Biological processi
- ATP synthesis coupled proton transport Source: GO_Central
- mitochondrial ATP synthesis coupled proton transport Source: Ensembl
Keywordsi
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Enzyme and pathway databases
Reactomei | R-BTA-163210, Formation of ATP by chemiosmotic coupling R-BTA-8949613, Cristae formation |
Names & Taxonomyi
Protein namesi | Recommended name: ATP synthase subunit gamma, mitochondrialCuratedAlternative name(s): ATP synthase F1 subunit gammaBy similarity F-ATPase gamma subunit |
Gene namesi | |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | HostDB:ENSBTAG00000013930 |
VGNCi | VGNC:26301, ATP5F1C |
Subcellular locationi
Mitochondrion
- Mitochondrion inner membrane 6 Publications; Peripheral membrane protein 5 Publications; Matrix side 2 Publications
Mitochondrion
- mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
- mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) Source: GO_Central
Keywords - Cellular componenti
CF(1), Membrane, Mitochondrion, Mitochondrion inner membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 25 | Mitochondrion2 PublicationsAdd BLAST | 25 | |
ChainiPRO_0000002684 | 26 – 298 | ATP synthase subunit gamma, mitochondrialAdd BLAST | 273 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 39 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 49 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 55 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 115 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 115 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 146 | PhosphoserineBy similarity | 1 | |
Modified residuei | 154 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 154 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 197 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 270 | N6-succinyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | P05631 |
PeptideAtlasi | P05631 |
PRIDEi | P05631 |
PTM databases
iPTMneti | P05631 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000013930, Expressed in heart and 99 other tissues |
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 ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ.
10 PublicationsProtein-protein interaction databases
CORUMi | P05631 |
DIPi | DIP-47546N |
IntActi | P05631, 5 interactors |
MINTi | P05631 |
STRINGi | 9913.ENSBTAP00000018505 |
Chemistry databases
BindingDBi | P05631 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P05631 |
SMRi | P05631 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05631 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1531, Eukaryota |
GeneTreei | ENSGT00390000006837 |
HOGENOMi | CLU_050669_4_0_1 |
InParanoidi | P05631 |
OMAi | MQITSAM |
OrthoDBi | 841252at2759 |
TreeFami | TF105765 |
Family and domain databases
CDDi | cd12151, F1-ATPase_gamma, 1 hit |
InterProi | View protein in InterPro IPR035968, ATP_synth_F1_ATPase_gsu IPR000131, ATP_synth_F1_gsu IPR023632, ATP_synth_F1_gsu_CS |
PANTHERi | PTHR11693, PTHR11693, 1 hit |
Pfami | View protein in Pfam PF00231, ATP-synt, 1 hit |
PRINTSi | PR00126, ATPASEGAMMA |
SUPFAMi | SSF52943, SSF52943, 1 hit |
TIGRFAMsi | TIGR01146, ATPsyn_F1gamma, 1 hit |
PROSITEi | View protein in PROSITE PS00153, ATPASE_GAMMA, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
The sequence of this isoform differs from the canonical sequence as follows:
298-298: Missing.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 249 | E → G in AAI02467 (Ref. 2) Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000438 | 298 | Missing in isoform Heart. Curated | 1 |
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 |
PIRi | A32019, PWBOG |
RefSeqi | NP_001068604.1, NM_001075136.2 XP_005214178.1, XM_005214121.3 [P05631-2] XP_005214179.1, XM_005214122.3 [P05631-2] |
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
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 |
PIRi | A32019, PWBOG |
RefSeqi | NP_001068604.1, NM_001075136.2 XP_005214178.1, XM_005214121.3 [P05631-2] XP_005214179.1, XM_005214122.3 [P05631-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BMF | X-ray | 2.85 | G | 26-297 | [»] | |
1COW | X-ray | 3.10 | G | 26-297 | [»] | |
1E1Q | X-ray | 2.61 | G | 26-297 | [»] | |
1E1R | X-ray | 2.50 | G | 26-297 | [»] | |
1E79 | X-ray | 2.40 | G | 26-297 | [»] | |
1EFR | X-ray | 3.10 | G | 26-297 | [»] | |
1H8E | X-ray | 2.00 | G | 26-297 | [»] | |
1H8H | X-ray | 2.90 | G | 26-297 | [»] | |
1NBM | X-ray | 3.00 | G | 26-297 | [»] | |
1OHH | X-ray | 2.80 | G | 26-297 | [»] | |
1QO1 | X-ray | 3.90 | G | 26-69 | [»] | |
G | 102-115 | [»] | ||||
G | 234-297 | [»] | ||||
1W0J | X-ray | 2.20 | G | 26-297 | [»] | |
1W0K | X-ray | 2.85 | G | 26-297 | [»] | |
2CK3 | X-ray | 1.90 | G | 26-297 | [»] | |
2JDI | X-ray | 1.90 | G | 26-298 | [»] | |
2JIZ | X-ray | 2.30 | G/N | 26-297 | [»] | |
2JJ1 | X-ray | 2.70 | G/N | 26-297 | [»] | |
2JJ2 | X-ray | 2.40 | G/N | 26-297 | [»] | |
2V7Q | X-ray | 2.10 | G | 26-297 | [»] | |
2W6E | X-ray | 6.50 | G | 1-298 | [»] | |
2W6F | X-ray | 6.00 | G | 1-298 | [»] | |
2W6G | X-ray | 6.00 | G | 1-298 | [»] | |
2W6H | X-ray | 5.00 | G | 1-298 | [»] | |
2W6I | X-ray | 4.00 | G | 1-298 | [»] | |
2W6J | X-ray | 3.84 | G | 1-298 | [»] | |
2WSS | X-ray | 3.20 | G/P | 26-297 | [»] | |
2XND | X-ray | 3.50 | G | 26-297 | [»] | |
4ASU | X-ray | 2.60 | G | 26-298 | [»] | |
4TSF | X-ray | 3.20 | G | 26-298 | [»] | |
4TT3 | X-ray | 3.21 | G | 26-298 | [»] | |
4YXW | X-ray | 3.10 | G | 26-298 | [»] | |
4Z1M | X-ray | 3.30 | G | 26-298 | [»] | |
5ARA | electron microscopy | 6.70 | G | 26-298 | [»] | |
5ARE | electron microscopy | 7.40 | G | 26-298 | [»] | |
5ARH | electron microscopy | 7.20 | G | 26-298 | [»] | |
5ARI | electron microscopy | 7.40 | G | 26-298 | [»] | |
5FIJ | electron microscopy | 7.40 | G | 26-298 | [»] | |
5FIK | electron microscopy | 6.40 | G | 26-298 | [»] | |
5FIL | electron microscopy | 7.10 | G | 26-298 | [»] | |
6TT7 | electron microscopy | 3.50 | G | 1-298 | [»] | |
6YY0 | electron microscopy | 3.23 | G | 26-298 | [»] | |
6Z1R | electron microscopy | 3.29 | G | 26-298 | [»] | |
6Z1U | electron microscopy | 3.47 | G | 26-298 | [»] | |
6ZG7 | electron microscopy | 3.49 | G | 26-298 | [»] | |
6ZG8 | electron microscopy | 3.49 | G | 26-298 | [»] | |
6ZIK | electron microscopy | 3.66 | G | 26-298 | [»] | |
6ZPO | electron microscopy | 4.00 | G | 26-298 | [»] | |
6ZQM | electron microscopy | 3.29 | G | 26-298 | [»] | |
6ZQN | electron microscopy | 4.00 | G | 26-298 | [»] | |
7AJB | electron microscopy | 9.20 | AG/G | 26-298 | [»] | |
7AJC | electron microscopy | 11.90 | AG/G | 26-298 | [»] | |
7AJD | electron microscopy | 9.00 | AG/G | 26-298 | [»] | |
7AJE | electron microscopy | 9.40 | AG/G | 26-298 | [»] | |
7AJF | electron microscopy | 8.45 | AG/G | 26-298 | [»] | |
7AJG | electron microscopy | 10.70 | AG/G | 26-298 | [»] | |
7AJH | electron microscopy | 9.70 | AG/G | 26-298 | [»] | |
7AJI | electron microscopy | 11.40 | AG/G | 26-298 | [»] | |
7AJJ | electron microscopy | 13.10 | AG/G | 26-298 | [»] | |
AlphaFoldDBi | P05631 | |||||
SMRi | P05631 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P05631 |
DIPi | DIP-47546N |
IntActi | P05631, 5 interactors |
MINTi | P05631 |
STRINGi | 9913.ENSBTAP00000018505 |
Chemistry databases
BindingDBi | P05631 |
ChEMBLi | CHEMBL612444 |
PTM databases
iPTMneti | P05631 |
Proteomic databases
PaxDbi | P05631 |
PeptideAtlasi | P05631 |
PRIDEi | P05631 |
Genome annotation databases
Organism-specific databases
CTDi | 509 |
VEuPathDBi | HostDB:ENSBTAG00000013930 |
VGNCi | VGNC:26301, ATP5F1C |
Phylogenomic databases
eggNOGi | KOG1531, Eukaryota |
GeneTreei | ENSGT00390000006837 |
HOGENOMi | CLU_050669_4_0_1 |
InParanoidi | P05631 |
OMAi | MQITSAM |
OrthoDBi | 841252at2759 |
TreeFami | TF105765 |
Enzyme and pathway databases
Reactomei | R-BTA-163210, Formation of ATP by chemiosmotic coupling R-BTA-8949613, Cristae formation |
Miscellaneous databases
EvolutionaryTracei | P05631 |
Gene expression databases
Bgeei | ENSBTAG00000013930, Expressed in heart and 99 other tissues |
Family and domain databases
CDDi | cd12151, F1-ATPase_gamma, 1 hit |
InterProi | View protein in InterPro IPR035968, ATP_synth_F1_ATPase_gsu IPR000131, ATP_synth_F1_gsu IPR023632, ATP_synth_F1_gsu_CS |
PANTHERi | PTHR11693, PTHR11693, 1 hit |
Pfami | View protein in Pfam PF00231, ATP-synt, 1 hit |
PRINTSi | PR00126, ATPASEGAMMA |
SUPFAMi | SSF52943, SSF52943, 1 hit |
TIGRFAMsi | TIGR01146, ATPsyn_F1gamma, 1 hit |
PROSITEi | View protein in PROSITE PS00153, ATPASE_GAMMA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATPG_BOVIN | |
Accessioni | P05631Primary (citable) accession number: P05631 Secondary accession number(s): Q3T0B4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1988 |
Last sequence update: | June 1, 1994 | |
Last modified: | May 25, 2022 | |
This is version 190 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families