Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. 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
Synonyms:ATP5C
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

DIPiDIP-47546N.
IntActiP05631. 1 interactor.
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 – 69Combined sources42
Turni74 – 76Combined sources3
Helixi77 – 79Combined sources3
Beta strandi93 – 96Combined sources4
Helixi106 – 110Combined sources5
Beta strandi115 – 117Combined sources3
Turni118 – 120Combined sources3
Beta strandi130 – 134Combined sources5
Helixi135 – 140Combined sources6
Helixi143 – 145Combined sources3
Helixi146 – 148Combined sources3
Beta strandi149 – 154Combined sources6
Beta strandi157 – 159Combined sources3
Helixi163 – 172Combined sources10
Turni175 – 177Combined sources3
Beta strandi181 – 190Combined sources10
Beta strandi192 – 194Combined sources3
Beta strandi195 – 203Combined sources9
Turni207 – 210Combined sources4
Helixi213 – 217Combined sources5
Turni223 – 225Combined sources3
Turni227 – 229Combined sources3
Helixi232 – 295Combined sources64

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.
OMAiYQEFALV.
OrthoDBiEOG091G0XX7.
TreeFamiTF105765.

Family and domain databases

CDDicd12151. F1-ATPase_gamma. 1 hit.
InterProiIPR000131. ATP_synth_F1_gsu.
IPR023632. ATP_synth_F1_gsu_CS.
[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]

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

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.
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.

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...

Protein-protein interaction databases

DIPiDIP-47546N.
IntActiP05631. 1 interactor.
MINTiMINT-5006919.
STRINGi9913.ENSBTAP00000018505.

Chemistry databases

BindingDBiP05631.
ChEMBLiCHEMBL612444.

PTM databases

iPTMnetiP05631.

Proteomic databases

PaxDbiP05631.
PeptideAtlasiP05631.
PRIDEiP05631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi509.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP05631.

Gene expression databases

BgeeiENSBTAG00000013930.

Family and domain databases

CDDicd12151. F1-ATPase_gamma. 1 hit.
InterProiIPR000131. ATP_synth_F1_gsu.
IPR023632. ATP_synth_F1_gsu_CS.
[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...

Entry informationi

Entry nameiATPG_BOVIN
AccessioniPrimary (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: November 30, 2016
This is version 158 of the entry and version 3 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.