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P05631 (ATPG_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene names
Name:ATP5C1
Synonyms:ATP5C
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6

Subcellular location

Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the ATPase gamma chain family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Liver (identifier: P05631-1)

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.
Isoform Heart (identifier: P05631-2)

Also known as: H;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion Ref.3 Ref.4
Chain26 – 298273ATP synthase subunit gamma, mitochondrial
PRO_0000002684

Amino acid modifications

Modified residue551N6-acetyllysine By similarity
Modified residue791N6-acetyllysine By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue1151N6-acetyllysine By similarity
Modified residue1461Phosphoserine By similarity
Modified residue1541N6-acetyllysine By similarity
Modified residue1971N6-acetyllysine By similarity

Natural variations

Alternative sequence2981Missing in isoform Heart.
VSP_000438

Experimental info

Sequence conflict2491E → G in AAI02467. Ref.2

Secondary structure

1 ......................................... 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Liver (L) [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: C1F41767CDABAD92

FASTA29833,072
        10         20         30         40         50         60 
MFSRAGVAGL SAWTVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 

        70         80         90        100        110        120 
RELKPARVYG VGSLALYEKA DIKTPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKSEAAN 

       130        140        150        160        170        180 
LAAAGKEVKI IGVGDKIRSI LHRTHSDQFL VTFKEVGRRP PTFGDASVIA LELLNSGYEF 

       190        200        210        220        230        240 
DEGSIIFNRF RSVISYKTEE KPIFSLDTIS SAESMSIYDD IDADVLRNYQ EYSLANIIYY 

       250        260        270        280        290 
SLKESTTSEQ SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD

« Hide

Isoform Heart (H) [UniParc].

Checksum: 241767CDABAD92D7
Show »

FASTA29732,957

References

« Hide 'large scale' references
[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(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-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(1985) [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(1991) [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(1993) [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(2007) [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(1994) [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(1996) [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(1998) [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(2003) [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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-297 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5D AND ATP5E.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X55389 mRNA. Translation: CAA39064.1.
M22463 Genomic DNA. Translation: AAA30398.1.
BC102466 mRNA. Translation: AAI02467.1.
IPIIPI00691827.
IPI00699915.
PIRPWBOG. A32019.
RefSeqNP_001068604.1. NM_001075136.2.
UniGeneBt.20727.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP05631.
SMRP05631. Positions 26-297.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47546N.
MINTMINT-5006919.
STRING9913.ENSBTAP00000018505.

Proteomic databases

PaxDbP05631.
PRIDEP05631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000018505; ENSBTAP00000018505; ENSBTAG00000013930.
GeneID327668.
KEGGbta:327668.

Organism-specific databases

CTD509.

Phylogenomic databases

eggNOGCOG0224.
GeneTreeENSGT00390000006837.
HOGENOMHOG000215911.
HOVERGENHBG000933.
InParanoidP05631.
KOK02136.
OMAQQRGMAT.
OrthoDBEOG4FJ899.

Family and domain databases

InterProIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERPTHR11693. PTHR11693. 1 hit.
PfamPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSPR00126. ATPASEGAMMA.
SUPFAMSSF52943. ATPase_gamma. 1 hit.
TIGRFAMsTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05631.
NextBio20810133.

Entry information

Entry nameATPG_BOVIN
AccessionPrimary (citable) accession number: P05631
Secondary accession number(s): Q3T0B4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents