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Protein

ATP synthase subunit beta, mitochondrial

Gene

Atp5b

Organism
Rattus norvegicus (Rat)
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. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: RGD
  • ATP binding Source: RGD
  • calcium ion binding Source: RGD
  • lipoprotein particle receptor activity Source: RGD
  • proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP metabolic process Source: RGD
  • ATP synthesis coupled proton transport Source: InterPro
  • receptor-mediated endocytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.14. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:Atp5b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621368. Atp5b.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
  • mitochondrion Source: RGD
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion1 PublicationAdd
BLAST
Chaini47 – 529483ATP synthase subunit beta, mitochondrialPRO_0000002445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061O-linked (GlcNAc)1 Publication
Modified residuei124 – 1241N6-acetyllysine; alternateBy similarity
Modified residuei124 – 1241N6-succinyllysine; alternateBy similarity
Modified residuei133 – 1331N6-acetyllysine; alternateBy similarity
Modified residuei133 – 1331N6-succinyllysine; alternateBy similarity
Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
Modified residuei198 – 1981N6-acetyllysineBy similarity
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei264 – 2641N6-acetyllysine; alternateBy similarity
Modified residuei264 – 2641N6-succinyllysine; alternateBy similarity
Modified residuei312 – 3121PhosphothreonineBy similarity
Modified residuei415 – 4151PhosphoserineBy similarity
Modified residuei426 – 4261N6-acetyllysineBy similarity
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei480 – 4801N6-acetyllysineBy similarity
Modified residuei485 – 4851N6-acetyllysineBy similarity
Modified residuei522 – 5221N6-acetyllysine; alternateBy similarity
Modified residuei522 – 5221N6-succinyllysine; alternateBy similarity
Modified residuei529 – 5291PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10719.
PRIDEiP10719.

2D gel databases

UCD-2DPAGEP10719.
World-2DPAGE0004:P10719.

PTM databases

iPTMnetiP10719.
PhosphoSiteiP10719.

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. Interacts with PPIF. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency.2 Publications

Protein-protein interaction databases

BioGridi251212. 4 interactions.
IntActiP10719. 6 interactions.
MINTiMINT-4587159.
STRINGi10116.ENSRNOP00000003965.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 623Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 723Combined sources
Beta strandi75 – 773Combined sources
Beta strandi85 – 906Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 1375Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi164 – 1674Combined sources
Turni173 – 1753Combined sources
Helixi188 – 1914Combined sources
Beta strandi205 – 2128Combined sources
Helixi213 – 22210Combined sources
Turni223 – 2253Combined sources
Beta strandi231 – 2388Combined sources
Helixi240 – 25213Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi265 – 2717Combined sources
Helixi276 – 29419Combined sources
Turni295 – 2984Combined sources
Beta strandi301 – 3066Combined sources
Helixi310 – 3167Combined sources
Helixi320 – 3223Combined sources
Helixi335 – 3439Combined sources
Beta strandi354 – 3574Combined sources
Helixi363 – 3653Combined sources
Helixi372 – 3765Combined sources
Helixi387 – 3904Combined sources
Turni391 – 3933Combined sources
Beta strandi400 – 4023Combined sources
Turni410 – 4145Combined sources
Helixi415 – 43420Combined sources
Turni435 – 4395Combined sources
Helixi448 – 46417Combined sources
Helixi469 – 4713Combined sources
Helixi472 – 4754Combined sources
Beta strandi483 – 4853Combined sources
Turni486 – 4894Combined sources
Helixi490 – 4967Combined sources
Turni498 – 5014Combined sources
Helixi504 – 5074Combined sources
Helixi514 – 5207Combined sources
Turni521 – 5233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80B51-529[»]
2F43X-ray3.00B51-529[»]
ProteinModelPortaliP10719.
SMRiP10719. Positions 51-527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10719.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP10719.
KOiK02133.
PhylomeDBiP10719.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLVGRVAS ASASGALRGL NPLAALPQAH LLLRTAPAGV HPARDYAAQS
60 70 80 90 100
SAAPKAGTAT GQIVAVIGAV VDVQFDEGLP PILNALEVQG RESRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ EILVTGIKVV DLLAPYAKGG
210 220 230 240 250
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM
260 270 280 290 300
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
310 320 330 340 350
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK
360 370 380 390 400
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP
410 420 430 440 450
LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGDYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
Length:529
Mass (Da):56,354
Last modified:April 1, 1990 - v2
Checksum:i9753BFBDBCD30E0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2582NL → KV in AAA40778 (PubMed:2907347).Curated
Sequence conflicti429 – 4302QD → HV in AAA40778 (PubMed:2907347).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099743 mRNA. Translation: AAH99743.1.
M25301 mRNA. Translation: AAA57154.1.
M19044 mRNA. Translation: AAB02288.1. Sequence problems.
M57634 mRNA. Translation: AAA40778.1.
PIRiA28701.
A30160.
RefSeqiNP_599191.1. NM_134364.1.
UniGeneiRn.92965.

Genome annotation databases

GeneIDi171374.
KEGGirno:171374.
UCSCiRGD:621368. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099743 mRNA. Translation: AAH99743.1.
M25301 mRNA. Translation: AAA57154.1.
M19044 mRNA. Translation: AAB02288.1. Sequence problems.
M57634 mRNA. Translation: AAA40778.1.
PIRiA28701.
A30160.
RefSeqiNP_599191.1. NM_134364.1.
UniGeneiRn.92965.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MABX-ray2.80B51-529[»]
2F43X-ray3.00B51-529[»]
ProteinModelPortaliP10719.
SMRiP10719. Positions 51-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251212. 4 interactions.
IntActiP10719. 6 interactions.
MINTiMINT-4587159.
STRINGi10116.ENSRNOP00000003965.

Chemistry

ChEMBLiCHEMBL2176796.

PTM databases

iPTMnetiP10719.
PhosphoSiteiP10719.

2D gel databases

UCD-2DPAGEP10719.
World-2DPAGE0004:P10719.

Proteomic databases

PaxDbiP10719.
PRIDEiP10719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171374.
KEGGirno:171374.
UCSCiRGD:621368. rat.

Organism-specific databases

CTDi506.
RGDi621368. Atp5b.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP10719.
KOiK02133.
PhylomeDBiP10719.

Enzyme and pathway databases

BRENDAi3.6.3.14. 5301.

Miscellaneous databases

EvolutionaryTraceiP10719.
PROiP10719.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Prostate.
  2. "Studies on the biogenesis of the mammalian ATP synthase complex: isolation and characterization of a full-length cDNA encoding the rat F1-beta-subunit."
    Boulet D., Poirier J., Cote C.
    Biochem. Biophys. Res. Commun. 159:1184-1190(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
  3. "N-terminal sequence of the rat liver beta-subunit in the mitochondrial ATPase-ATPsynthase."
    Cretin F., Baggetto L.G., Denoroy L., Godinot C.
    Biochem. Biophys. Res. Commun. 164:1165-1169(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-60.
    Tissue: Liver.
  4. "Beta subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli, and structural relationship to adenylate kinase."
    Garboczi D.N., Fox A.H., Gerring S.L., Pedersen P.L.
    Biochemistry 27:553-560(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-529.
  5. "Mitochondrial ATP synthase F1-beta-subunit is a calcium-binding protein."
    Hubbard M.J., McHugh N.J.
    FEBS Lett. 391:323-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 87-98; 208-219; 225-234; 268-279 AND 433-454, CALCIUM-BINDING.
  6. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 226-239; 242-259; 265-279; 282-345; 388-422; 427-456 AND 463-480, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  7. "Molecular cloning of cDNA for the rat F1-ATPase beta subunit."
    Lee Y.M., Chu L.P., Lee S.C.
    Taiwan Yi Xue Hui Za Zhi 87:933-938(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-529.
  8. "Mass spectrometry and tandem mass spectrometry analysis of rat mitochondrial ATP synthase: up-regulation in pancreatic acinar cells treated with cerulein."
    Yu J.-H., Yun S.-Y., Lim J.-W., Kim H., Kim K.-H.
    Proteomics 3:2437-2445(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Pancreatic acinar cell.
  9. "Identification of two proteins associated with mammalian ATP synthase."
    Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.
    Mol. Cell. Proteomics 6:1690-1699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  10. Cited for: INTERACTION WITH BCL2L1.
  11. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-106.
  13. "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis."
    Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiATPB_RAT
AccessioniPrimary (citable) accession number: P10719
Secondary accession number(s): Q499W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds calcium ions.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.