P56480 · ATPB_MOUSE
- ProteinATP synthase subunit beta, mitochondrial
- GeneAtp5f1b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids529 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. 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 activity
- ATP + 4 H+(in) + H2O = ADP + 5 H+(out) + phosphateThis reaction proceeds in the backward direction.
CHEBI:30616 + 4 H+ (in)CHEBI:15378+ CHEBI:15377 = CHEBI:456216 + 5 H+ (out)CHEBI:15378+ CHEBI:43474
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP synthase subunit beta, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP56480
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-46 | Mitochondrion | ||||
Sequence: MLSLVGRVASASASGALRGLSPSAALPQAQLLLRAAPAGVHPARDY | ||||||
Chain | PRO_0000002444 | 47-529 | ATP synthase subunit beta, mitochondrial | |||
Sequence: AAQASAAPKAGTATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRDSRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS | ||||||
Glycosylation | 106 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 124 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 124 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 198 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 259 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 264 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 264 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 312 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 426 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 433 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 480 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 485 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 522 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 522 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 529 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
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 ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity).
Interacts with PPIF (PubMed:21281446).
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 efficiency (By similarity).
Interacts with CLN5 and PPT1 (PubMed:19941651).
Interacts with S100A1; this interaction increases F1-ATPase activity (PubMed:17438143).
Interacts with MTLN (By similarity).
Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production (By similarity).
Interacts with PPIF (PubMed:21281446).
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 efficiency (By similarity).
Interacts with CLN5 and PPT1 (PubMed:19941651).
Interacts with S100A1; this interaction increases F1-ATPase activity (PubMed:17438143).
Interacts with MTLN (By similarity).
Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length529
- Mass (Da)56,300
- Last updated2002-05-02 v2
- ChecksumF3E1100C390A78A7
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 25 | in Ref. 1; AAB86421 | ||||
Sequence: A → V | ||||||
Sequence conflict | 43 | in Ref. 2; BAE35088 | ||||
Sequence: A → V | ||||||
Sequence conflict | 76 | in Ref. 2; BAE40961 | ||||
Sequence: D → G | ||||||
Sequence conflict | 92 | in Ref. 1; AAB86421 | ||||
Sequence: D → E | ||||||
Sequence conflict | 134 | in Ref. 2; BAE31497 | ||||
Sequence: I → V | ||||||
Sequence conflict | 239 | in Ref. 1; AAB86421 | ||||
Sequence: R → K | ||||||
Sequence conflict | 271 | in Ref. 2; BAE38888/BAE39301 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 279-280 | in Ref. 1; AAB86421 | ||||
Sequence: RA → PT | ||||||
Sequence conflict | 288 | in Ref. 2; BAE31497/BAE31630 | ||||
Sequence: T → A | ||||||
Sequence conflict | 375 | in Ref. 2; BAE30095 | ||||
Sequence: T → N | ||||||
Sequence conflict | 383 | in Ref. 2; BAB22802 | ||||
Sequence: T → S | ||||||
Sequence conflict | 433-434 | in Ref. 1; AAB86421 | ||||
Sequence: SL → FF | ||||||
Sequence conflict | 466 | in Ref. 2; BAB22802 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 469 | in Ref. 2; BAE39797 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 518 | in Ref. 2; BAE35331 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF030559 EMBL· GenBank· DDBJ | AAB86421.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003460 EMBL· GenBank· DDBJ | BAB22802.1 EMBL· GenBank· DDBJ | mRNA | ||
AK010314 EMBL· GenBank· DDBJ | BAB26846.1 EMBL· GenBank· DDBJ | mRNA | ||
AK084009 EMBL· GenBank· DDBJ | BAC39095.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145684 EMBL· GenBank· DDBJ | BAE26587.1 EMBL· GenBank· DDBJ | mRNA | ||
AK148891 EMBL· GenBank· DDBJ | BAE28692.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150599 EMBL· GenBank· DDBJ | BAE29691.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151081 EMBL· GenBank· DDBJ | BAE30095.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151600 EMBL· GenBank· DDBJ | BAE30540.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152788 EMBL· GenBank· DDBJ | BAE31497.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152976 EMBL· GenBank· DDBJ | BAE31630.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153099 EMBL· GenBank· DDBJ | BAE31720.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159444 EMBL· GenBank· DDBJ | BAE35088.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159737 EMBL· GenBank· DDBJ | BAE35331.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159978 EMBL· GenBank· DDBJ | BAE35529.1 EMBL· GenBank· DDBJ | mRNA | ||
AK160199 EMBL· GenBank· DDBJ | BAE35689.1 EMBL· GenBank· DDBJ | mRNA | ||
AK160608 EMBL· GenBank· DDBJ | BAE35911.1 EMBL· GenBank· DDBJ | mRNA | ||
AK164383 EMBL· GenBank· DDBJ | BAE37764.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166525 EMBL· GenBank· DDBJ | BAE38829.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166603 EMBL· GenBank· DDBJ | BAE38888.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166979 EMBL· GenBank· DDBJ | BAE39161.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167119 EMBL· GenBank· DDBJ | BAE39267.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167160 EMBL· GenBank· DDBJ | BAE39301.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167728 EMBL· GenBank· DDBJ | BAE39769.1 EMBL· GenBank· DDBJ | mRNA | ||
AK167764 EMBL· GenBank· DDBJ | BAE39797.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168692 EMBL· GenBank· DDBJ | BAE40537.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168941 EMBL· GenBank· DDBJ | BAE40749.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169184 EMBL· GenBank· DDBJ | BAE40961.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018392 EMBL· GenBank· DDBJ | AAH18392.1 EMBL· GenBank· DDBJ | mRNA | ||
BC037127 EMBL· GenBank· DDBJ | AAH37127.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC046616 EMBL· GenBank· DDBJ | AAH46616.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ403100 EMBL· GenBank· DDBJ | ABD77233.1 EMBL· GenBank· DDBJ | mRNA |