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Protein

ATP synthase subunit f, mitochondrial

Gene

Atp5j2

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. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  1. ATPase activity Source: Ensembl

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB-KW
  2. ATP catabolic process Source: MGI
  3. proton transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit f, mitochondrial
Gene namesi
Name:Atp5j2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1927558. Atp5j2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei57 – 7620HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: MGI
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. mitochondrion Source: MGI
  6. nucleus Source: MGI
  7. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 8887ATP synthase subunit f, mitochondrialPRO_0000194825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei16 – 161N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP56135.
PaxDbiP56135.
PRIDEiP56135.

PTM databases

PhosphoSiteiP56135.

Expressioni

Gene expression databases

BgeeiP56135.
ExpressionAtlasiP56135. baseline and differential.
GenevestigatoriP56135.

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

BioGridi208283. 1 interaction.
IntActiP56135. 2 interactions.
MINTiMINT-1843047.

Structurei

3D structure databases

ProteinModelPortaliP56135.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase F chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292892.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000034215.
HOVERGENiHBG002418.
InParanoidiP56135.
KOiK02130.
OMAiYLWEYDH.
OrthoDBiEOG73JKZ1.
PhylomeDBiP56135.
TreeFamiTF342865.

Family and domain databases

InterProiIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiPF10206. WRW. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56135-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLVPLKEK KLMEVKLGEL PSWIMMRDFT PSGIAGAFRR GYDRYYNKYI
60 70 80
NVRKGSISGI SMVLAAYVVF SYCISYKELK HERRRKYH
Length:88
Mass (Da):10,344
Last modified:January 23, 2007 - v3
Checksum:i89526C72EC436E48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030192 mRNA. Translation: BAA92756.1.
AK002519 mRNA. Translation: BAB22157.1.
AK003235 mRNA. Translation: BAB22660.1.
AK003817 mRNA. Translation: BAB23014.1.
AK013130 mRNA. Translation: BAB28667.1.
AK151737 mRNA. Translation: BAE30651.1.
AK168095 mRNA. Translation: BAE40067.1.
BC029226 mRNA. Translation: AAH29226.1.
CCDSiCCDS39385.1.
RefSeqiNP_065607.1. NM_020582.2.
UniGeneiMm.133551.

Genome annotation databases

EnsembliENSMUST00000161741; ENSMUSP00000125504; ENSMUSG00000038690.
GeneIDi57423.
KEGGimmu:57423.
UCSCiuc009amk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030192 mRNA. Translation: BAA92756.1.
AK002519 mRNA. Translation: BAB22157.1.
AK003235 mRNA. Translation: BAB22660.1.
AK003817 mRNA. Translation: BAB23014.1.
AK013130 mRNA. Translation: BAB28667.1.
AK151737 mRNA. Translation: BAE30651.1.
AK168095 mRNA. Translation: BAE40067.1.
BC029226 mRNA. Translation: AAH29226.1.
CCDSiCCDS39385.1.
RefSeqiNP_065607.1. NM_020582.2.
UniGeneiMm.133551.

3D structure databases

ProteinModelPortaliP56135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208283. 1 interaction.
IntActiP56135. 2 interactions.
MINTiMINT-1843047.

PTM databases

PhosphoSiteiP56135.

Proteomic databases

MaxQBiP56135.
PaxDbiP56135.
PRIDEiP56135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000161741; ENSMUSP00000125504; ENSMUSG00000038690.
GeneIDi57423.
KEGGimmu:57423.
UCSCiuc009amk.1. mouse.

Organism-specific databases

CTDi9551.
MGIiMGI:1927558. Atp5j2.

Phylogenomic databases

eggNOGiNOG292892.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000034215.
HOVERGENiHBG002418.
InParanoidiP56135.
KOiK02130.
OMAiYLWEYDH.
OrthoDBiEOG73JKZ1.
PhylomeDBiP56135.
TreeFamiTF342865.

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

NextBioi313776.
PROiP56135.
SOURCEiSearch...

Gene expression databases

BgeeiP56135.
ExpressionAtlasiP56135. baseline and differential.
GenevestigatoriP56135.

Family and domain databases

InterProiIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiPF10206. WRW. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
    Inoue S., Sano H., Ohta M.
    Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Bone marrow, Embryo and Kidney.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-39, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATPK_MOUSE
AccessioniPrimary (citable) accession number: P56135
Secondary accession number(s): Q3THX9, Q9JMF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 102 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

Complete proteome, Direct protein sequencing, 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.