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Protein

ATP synthase F(0) complex subunit B1, mitochondrial

Gene

Atp5f1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

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

GO - Biological processi

  1. ATP catabolic process Source: MGI
  2. ATP synthesis coupled proton transport Source: GO_Central
  3. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

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 F(0) complex subunit B1, mitochondrial
Alternative name(s):
ATP synthase subunit b
Short name:
ATPase subunit b
Gene namesi
Name:Atp5f1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1100495. Atp5f1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. membrane Source: MGI
  3. mitochondrial inner membrane Source: MGI
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: GO_Central
  6. mitochondrion Source: MGI
  7. myelin sheath Source: UniProtKB
  8. nucleus 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 – 4242MitochondrionBy similarityAdd
BLAST
Chaini43 – 256214ATP synthase F(0) complex subunit B1, mitochondrialPRO_0000002514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311N6-succinyllysine1 Publication
Modified residuei139 – 1391N6-acetyllysine1 Publication
Modified residuei154 – 1541N6-acetyllysine1 Publication
Modified residuei162 – 1621N6-acetyllysine1 Publication
Modified residuei221 – 2211N6-acetyllysine1 Publication
Modified residuei225 – 2251N6-acetyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQQ7.
PaxDbiQ9CQQ7.
PRIDEiQ9CQQ7.

PTM databases

PhosphoSiteiQ9CQQ7.

Expressioni

Gene expression databases

BgeeiQ9CQQ7.
ExpressionAtlasiQ9CQQ7. baseline and differential.
GenevestigatoriQ9CQQ7.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198256. 2 interactions.
IntActiQ9CQQ7. 3 interactions.
MINTiMINT-1841503.
STRINGi10090.ENSMUSP00000088168.

Structurei

3D structure databases

ProteinModelPortaliQ9CQQ7.
SMRiQ9CQQ7. Positions 121-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase B chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG245616.
GeneTreeiENSGT00390000001958.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiQ9CQQ7.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG7V4B02.
PhylomeDBiQ9CQQ7.
TreeFamiTF313250.

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.

Q9CQQ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSRVVLSAA ATAAPCLKNA AALGPGVLQA TRAFHTGQPR LAPLPPLPEY
60 70 80 90 100
GGKVRLGLIP EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF
110 120 130 140 150
STISVVGLIV YVIKKYGASF GEFIDKLNEE KIAQLEEVKQ SSMKQIQDAI
160 170 180 190 200
DMEKAQQALV QKRHYLFDVQ RNNIALALEV TYRERLHKAY KEVKNRLDYH
210 220 230 240 250
ISVQNMMRRK EEEHMIDWVE KHVVKSISVQ QEKETIAKCI EDLKLLAKKA

QAQPIM
Length:256
Mass (Da):28,949
Last modified:June 1, 2001 - v1
Checksum:i6B385AE4DE6CB784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002960 mRNA. Translation: BAB22481.1.
AK011312 mRNA. Translation: BAB27538.1.
CCDSiCCDS17714.1.
RefSeqiNP_033855.2. NM_009725.3.
XP_006500997.1. XM_006500934.1.
UniGeneiMm.251152.

Genome annotation databases

EnsembliENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563.
GeneIDi11950.
KEGGimmu:11950.
UCSCiuc008qvl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002960 mRNA. Translation: BAB22481.1.
AK011312 mRNA. Translation: BAB27538.1.
CCDSiCCDS17714.1.
RefSeqiNP_033855.2. NM_009725.3.
XP_006500997.1. XM_006500934.1.
UniGeneiMm.251152.

3D structure databases

ProteinModelPortaliQ9CQQ7.
SMRiQ9CQQ7. Positions 121-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198256. 2 interactions.
IntActiQ9CQQ7. 3 interactions.
MINTiMINT-1841503.
STRINGi10090.ENSMUSP00000088168.

PTM databases

PhosphoSiteiQ9CQQ7.

Proteomic databases

MaxQBiQ9CQQ7.
PaxDbiQ9CQQ7.
PRIDEiQ9CQQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563.
GeneIDi11950.
KEGGimmu:11950.
UCSCiuc008qvl.1. mouse.

Organism-specific databases

CTDi515.
MGIiMGI:1100495. Atp5f1.

Phylogenomic databases

eggNOGiNOG245616.
GeneTreeiENSGT00390000001958.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiQ9CQQ7.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG7V4B02.
PhylomeDBiQ9CQQ7.
TreeFamiTF313250.

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiAtp5f1. mouse.
NextBioi280069.
PROiQ9CQQ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQQ7.
ExpressionAtlasiQ9CQQ7. baseline and differential.
GenevestigatoriQ9CQQ7.

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. "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.
    Tissue: Brain and Embryo.
  2. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-90; 115-139; 145-154; 164-183 AND 195-221, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  3. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "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-139; LYS-154; LYS-162; LYS-221; LYS-225; LYS-233 AND LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAT5F1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 107 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, 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.