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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

  1. poly(A) RNA binding Source: Ensembl
  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_339395. 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
ProteomesiUP000009136 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. 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 – 2525Mitochondrion2 PublicationsAdd
BLAST
Chaini26 – 298273ATP synthase subunit gamma, mitochondrialPRO_0000002684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysineBy similarity
Modified residuei49 – 491N6-succinyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
Modified residuei154 – 1541N6-acetyllysine; alternateBy similarity
Modified residuei154 – 1541N6-succinyllysine; alternateBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP05631.
PRIDEiP05631.

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 interaction.
MINTiMINT-5006919.
STRINGi9913.ENSBTAP00000018505.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 6942Combined sources
Turni74 – 763Combined sources
Helixi77 – 793Combined sources
Beta strandi93 – 964Combined sources
Helixi106 – 1105Combined sources
Beta strandi115 – 1173Combined sources
Turni118 – 1203Combined sources
Beta strandi130 – 1345Combined sources
Helixi135 – 1406Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 1483Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi157 – 1593Combined sources
Helixi163 – 17210Combined sources
Turni175 – 1773Combined sources
Beta strandi181 – 19010Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi195 – 2039Combined sources
Turni207 – 2104Combined sources
Helixi213 – 2175Combined sources
Turni223 – 2253Combined sources
Turni227 – 2293Combined sources
Helixi232 – 29564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray3.90G26-297[»]
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[»]
ProteinModelPortaliP05631.
SMRiP05631. Positions 26-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05631.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase gamma chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiP05631.
KOiK02136.
OMAiLYWALAE.
OrthoDBiEOG7QK0D3.
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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491E → G in AAI02467 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei298 – 2981Missing in isoform Heart. CuratedVSP_000438

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_005214121.2. [P05631-2]
XP_005214179.1. XM_005214122.2. [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_005214121.2. [P05631-2]
XP_005214179.1. XM_005214122.2. [P05631-2]
UniGeneiBt.20727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray3.90G26-297[»]
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[»]
ProteinModelPortaliP05631.
SMRiP05631. Positions 26-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP05631.
ChEMBLiCHEMBL612444.

Proteomic databases

PaxDbiP05631.
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

eggNOGiCOG0224.
GeneTreeiENSGT00390000006837.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiP05631.
KOiK02136.
OMAiLYWALAE.
OrthoDBiEOG7QK0D3.
TreeFamiTF105765.

Enzyme and pathway databases

ReactomeiREACT_339395. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP05631.
NextBioi20810133.

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. "ATP synthase from bovine mitochondria: complementary DNA sequence of the mitochondrial import precursor of the gamma-subunit and the genomic sequence of the mature protein."
    Dyer M.R., Gay N.J., Powell S.J., Walker J.E.
    Biochemistry 28:3670-3680(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
    Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
    J. Mol. Biol. 184:677-701(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 174-297, PROTEIN SEQUENCE OF 26-297.
  4. "Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
    Walker J.E., Lutter R., Dupuis A., Runswick M.J.
    Biochemistry 30:5369-5378(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-30.
    Tissue: Heart.
  5. "Tissue-specific isoforms of the bovine mitochondrial ATP synthase gamma-subunit."
    Matsuda C., Endo H., Hirata H., Morosawa H., Nakanishi M., Kagawa Y.
    FEBS Lett. 325:281-284(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 286-298, ALTERNATIVE SPLICING.
    Tissue: Heart and Liver.
  6. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
    Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
    FEBS Lett. 581:3145-3148(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  7. "Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
    Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
    Nature 370:621-628(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  8. "The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
    Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
    Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  9. "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
    Orriss G.L., Leslie A.G., Braig K., Walker J.E.
    Structure 6:831-837(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  10. "The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
    Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
    Nat. Struct. Biol. 10:744-750(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1; ATP5A1 AND ATP5B.
  11. "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
    Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
    Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5D AND ATP5E.

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: April 1, 2015
This is version 144 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

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.