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Protein

ATP synthase subunit 4, mitochondrial

Gene

ATP4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: SGD
  • protein complex oligomerization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33985-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit 4, mitochondrial
Gene namesi
Name:ATP4
Ordered Locus Names:YPL078C
ORF Names:LPF7C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL078C.
SGDiS000005999. ATP4.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial proton-transporting ATP synthase, stator stalk Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Mitochondrion1 PublicationAdd
BLAST
Chaini36 – 244209ATP synthase subunit 4, mitochondrialPRO_0000002524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05626.

PTM databases

iPTMnetiP05626.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.

Protein-protein interaction databases

BioGridi36102. 67 interactions.
DIPiDIP-3036N.
IntActiP05626. 5 interactions.
MINTiMINT-674963.

Structurei

3D structure databases

ProteinModelPortaliP05626.
SMRiP05626. Positions 113-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase B chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000158315.
InParanoidiP05626.
KOiK02127.
OMAiDSWVRFE.
OrthoDBiEOG77Q571.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSMGVRGL ALRSVSKTLF SQGVRCPSMV IGARYMSSTP EKQTDPKAKA
60 70 80 90 100
NSIINAIPGN NILTKTGVLG TSAAAVIYAI SNELYVINDE SILLLTFLGF
110 120 130 140 150
TGLVAKYLAP AYKDFADARM KKVSDVLNAS RNKHVEAVKD RIDSVSQLQN
160 170 180 190 200
VAETTKVLFD VSKETVELES EAFELKQKVE LAHEAKAVLD SWVRYEASLR
210 220 230 240
QLEQRQLAKS VISRVQSELG NPKFQEKVLQ QSISEIEQLL SKLK
Length:244
Mass (Da):26,925
Last modified:October 5, 2010 - v2
Checksum:iBDBE0F6AD6E5392C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → L in AAT92995 (PubMed:17322287).Curated
Sequence conflicti172 – 1721A → R in CAA29909 (PubMed:2892678).Curated
Sequence conflicti172 – 1721A → R in CAA34703 (PubMed:2553130).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06732 Genomic DNA. Translation: CAA29909.1.
X16721 Genomic DNA. Translation: CAA34703.1.
U41849 Genomic DNA. Translation: AAB68260.1.
AY692976 Genomic DNA. Translation: AAT92995.1.
BK006949 Genomic DNA. Translation: DAA11354.1.
PIRiS61109. PWBYBC.
RefSeqiNP_015247.1. NM_001183892.1.

Genome annotation databases

EnsemblFungiiYPL078C; YPL078C; YPL078C.
GeneIDi856027.
KEGGisce:YPL078C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06732 Genomic DNA. Translation: CAA29909.1.
X16721 Genomic DNA. Translation: CAA34703.1.
U41849 Genomic DNA. Translation: AAB68260.1.
AY692976 Genomic DNA. Translation: AAT92995.1.
BK006949 Genomic DNA. Translation: DAA11354.1.
PIRiS61109. PWBYBC.
RefSeqiNP_015247.1. NM_001183892.1.

3D structure databases

ProteinModelPortaliP05626.
SMRiP05626. Positions 113-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36102. 67 interactions.
DIPiDIP-3036N.
IntActiP05626. 5 interactions.
MINTiMINT-674963.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiP05626.

Proteomic databases

MaxQBiP05626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL078C; YPL078C; YPL078C.
GeneIDi856027.
KEGGisce:YPL078C.

Organism-specific databases

EuPathDBiFungiDB:YPL078C.
SGDiS000005999. ATP4.

Phylogenomic databases

HOGENOMiHOG000158315.
InParanoidiP05626.
KOiK02127.
OMAiDSWVRFE.
OrthoDBiEOG77Q571.

Enzyme and pathway databases

BioCyciYEAST:G3O-33985-MONOMER.

Miscellaneous databases

PROiP05626.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ATP4, the structural gene for yeast F0F1 ATPase subunit 4."
    Velours J., Durrens P., Aigle M., Guerin B.
    Eur. J. Biochem. 170:637-642(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The yeast ATP synthase subunit 4: structure and function."
    Velours J., Arselin G., Paul M.-F., Galante M., Durrens P., Aigle M., Guerin B.
    Biochimie 71:903-915(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Subunit 4 of ATP synthase (F0F1) from yeast mitochondria. Purification, amino-acid composition and partial N-terminal sequence."
    Velours J., Arselin de Chateaubodeau G., Galante M., Guerin B.
    Eur. J. Biochem. 164:579-584(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 36-45.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiATPF_YEAST
AccessioniPrimary (citable) accession number: P05626
Secondary accession number(s): D6W3T8, E9P905, Q02830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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.