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Q9CQQ7 (AT5F1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase F(0) complex subunit B1, mitochondrial
Alternative name(s):
ATP synthase subunit b
Short name=ATPase subunit b
Gene names
Name:Atp5f1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length256 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 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.

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 By similarity.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the eukaryotic ATPase B chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion By similarity
Chain43 – 256214ATP synthase F(0) complex subunit B1, mitochondrial
PRO_0000002514

Amino acid modifications

Modified residue1311N6-succinyllysine Ref.3
Modified residue1391N6-acetyllysine Ref.4
Modified residue1541N6-acetyllysine Ref.4
Modified residue1621N6-acetyllysine Ref.4
Modified residue2211N6-acetyllysine Ref.4
Modified residue2251N6-acetyllysine Ref.4
Modified residue2331N6-acetyllysine Ref.4
Modified residue2441N6-acetyllysine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9CQQ7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6B385AE4DE6CB784

FASTA25628,949
        10         20         30         40         50         60 
MLSRVVLSAA ATAAPCLKNA AALGPGVLQA TRAFHTGQPR LAPLPPLPEY GGKVRLGLIP 

        70         80         90        100        110        120 
EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF STISVVGLIV YVIKKYGASF 

       130        140        150        160        170        180 
GEFIDKLNEE KIAQLEEVKQ SSMKQIQDAI DMEKAQQALV QKRHYLFDVQ RNNIALALEV 

       190        200        210        220        230        240 
TYRERLHKAY KEVKNRLDYH ISVQNMMRRK EEEHMIDWVE KHVVKSISVQ QEKETIAKCI 

       250 
EDLKLLAKKA QAQPIM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002960 mRNA. Translation: BAB22481.1.
AK011312 mRNA. Translation: BAB27538.1.
CCDSCCDS17714.1.
RefSeqNP_033855.2. NM_009725.3.
XP_006500997.1. XM_006500934.1.
UniGeneMm.251152.

3D structure databases

ProteinModelPortalQ9CQQ7.
SMRQ9CQQ7. Positions 121-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198256. 2 interactions.
IntActQ9CQQ7. 3 interactions.
MINTMINT-1841503.
STRING10090.ENSMUSP00000088168.

PTM databases

PhosphoSiteQ9CQQ7.

Proteomic databases

MaxQBQ9CQQ7.
PaxDbQ9CQQ7.
PRIDEQ9CQQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563.
GeneID11950.
KEGGmmu:11950.
UCSCuc008qvl.1. mouse.

Organism-specific databases

CTD515.
MGIMGI:1100495. Atp5f1.

Phylogenomic databases

eggNOGNOG245616.
GeneTreeENSGT00390000001958.
HOGENOMHOG000007163.
HOVERGENHBG050604.
InParanoidQ9CQQ7.
KOK02127.
OMAVINHETF.
OrthoDBEOG7V4B02.
PhylomeDBQ9CQQ7.
TreeFamTF313250.

Gene expression databases

ArrayExpressQ9CQQ7.
BgeeQ9CQQ7.
GenevestigatorQ9CQQ7.

Family and domain databases

InterProIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERPTHR12733. PTHR12733. 1 hit.
PfamPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5F1. mouse.
NextBio280069.
PROQ9CQQ7.
SOURCESearch...

Entry information

Entry nameAT5F1_MOUSE
AccessionPrimary (citable) accession number: Q9CQQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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