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Protein

ATP synthase-coupling factor 6, mitochondrial

Gene

Atp5j

Organism
Mus musculus (Mouse)
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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.

GO - Molecular functioni

  1. ATPase activity Source: Ensembl
  2. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: InterPro
  2. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase-coupling factor 6, mitochondrial
Short name:
ATPase subunit F6
Gene namesi
Name:Atp5j
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:107777. Atp5j.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
  4. mitochondrion Source: MGI
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 – 3232MitochondrionBy similarityAdd
BLAST
Chaini33 – 10876ATP synthase-coupling factor 6, mitochondrialPRO_0000002529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-acetyllysine1 Publication
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei84 – 841N6-acetyllysine; alternate1 Publication
Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
Modified residuei94 – 941N6-acetyllysine; alternate1 Publication
Modified residuei94 – 941N6-succinyllysine; alternate1 Publication
Modified residuei99 – 991N6-acetyllysine; alternate1 Publication
Modified residuei99 – 991N6-succinyllysine; alternate1 Publication
Modified residuei105 – 1051N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP97450.
PaxDbiP97450.
PRIDEiP97450.

2D gel databases

SWISS-2DPAGEP97450.

PTM databases

PhosphoSiteiP97450.

Expressioni

Gene expression databases

BgeeiP97450.
ExpressionAtlasiP97450. baseline and differential.
GenevestigatoriP97450.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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 (By similarity).By similarity

Protein-protein interaction databases

IntActiP97450. 2 interactions.
MINTiMINT-1843958.
STRINGi10090.ENSMUSP00000023608.

Structurei

3D structure databases

ProteinModelPortaliP97450.
SMRiP97450. Positions 36-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG265662.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP97450.
KOiK02131.
OMAiDMNTFPN.
OrthoDBiEOG754HRZ.
PhylomeDBiP97450.
TreeFamiTF318998.

Family and domain databases

InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERiPTHR12441. PTHR12441. 1 hit.
PfamiPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMiSSF111357. SSF111357. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P97450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLQRIFRLS SVLRSAVSVH LKRNIGVTAV AFNKELDPVQ KLFVDKIREY
60 70 80 90 100
KSKRQASGGP VDIGPEYQQD LDRELYKLKQ MYGKGEMDTF PTFKFDDPKF

EVIDKPQS
Length:108
Mass (Da):12,496
Last modified:April 30, 1997 - v1
Checksum:iE2A2E63F7F23CEBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77128 mRNA. Translation: AAB19213.1.
AK078484 mRNA. Translation: BAC37301.1.
BC010766 mRNA. Translation: AAH10766.1.
CCDSiCCDS28283.1.
PIRiPD0444.
RefSeqiNP_001289142.1. NM_001302213.1.
NP_001289143.1. NM_001302214.1.
NP_001289144.1. NM_001302215.1.
NP_001289145.1. NM_001302216.1.
NP_058035.1. NM_016755.3.
XP_006522939.1. XM_006522876.1.
XP_006522940.1. XM_006522877.2.
UniGeneiMm.353.

Genome annotation databases

EnsembliENSMUST00000023608; ENSMUSP00000023608; ENSMUSG00000022890.
ENSMUST00000114191; ENSMUSP00000109829; ENSMUSG00000022890.
ENSMUST00000114193; ENSMUSP00000109831; ENSMUSG00000022890.
GeneIDi11957.
KEGGimmu:11957.
UCSCiuc007zth.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77128 mRNA. Translation: AAB19213.1.
AK078484 mRNA. Translation: BAC37301.1.
BC010766 mRNA. Translation: AAH10766.1.
CCDSiCCDS28283.1.
PIRiPD0444.
RefSeqiNP_001289142.1. NM_001302213.1.
NP_001289143.1. NM_001302214.1.
NP_001289144.1. NM_001302215.1.
NP_001289145.1. NM_001302216.1.
NP_058035.1. NM_016755.3.
XP_006522939.1. XM_006522876.1.
XP_006522940.1. XM_006522877.2.
UniGeneiMm.353.

3D structure databases

ProteinModelPortaliP97450.
SMRiP97450. Positions 36-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97450. 2 interactions.
MINTiMINT-1843958.
STRINGi10090.ENSMUSP00000023608.

PTM databases

PhosphoSiteiP97450.

2D gel databases

SWISS-2DPAGEP97450.

Proteomic databases

MaxQBiP97450.
PaxDbiP97450.
PRIDEiP97450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023608; ENSMUSP00000023608; ENSMUSG00000022890.
ENSMUST00000114191; ENSMUSP00000109829; ENSMUSG00000022890.
ENSMUST00000114193; ENSMUSP00000109831; ENSMUSG00000022890.
GeneIDi11957.
KEGGimmu:11957.
UCSCiuc007zth.1. mouse.

Organism-specific databases

CTDi522.
MGIiMGI:107777. Atp5j.

Phylogenomic databases

eggNOGiNOG265662.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP97450.
KOiK02131.
OMAiDMNTFPN.
OrthoDBiEOG754HRZ.
PhylomeDBiP97450.
TreeFamiTF318998.

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiAtp5j. mouse.
NextBioi280077.
PROiP97450.
SOURCEiSearch...

Gene expression databases

BgeeiP97450.
ExpressionAtlasiP97450. baseline and differential.
GenevestigatoriP97450.

Family and domain databases

InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERiPTHR12441. PTHR12441. 1 hit.
PfamiPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMiSSF111357. SSF111357. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Rocha D., Anderson E., Botcherby M., Jordan B., Carrier A.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-94 AND LYS-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-46; LYS-79; LYS-84; LYS-94; LYS-99 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATP5J_MOUSE
AccessioniPrimary (citable) accession number: P97450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: April 30, 1997
Last modified: March 31, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.