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Protein

ATP synthase subunit beta, mitochondrial

Gene

Atp5f1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Nucleotide bindingi206 – 213ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrialCurated (EC:3.6.3.14)
Alternative name(s):
ATP synthase F1 subunit betaBy similarity
Gene namesi
Name:Atp5f1bBy similarity
Synonyms:Atp5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:107801 Atp5b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 46MitochondrionBy similarityAdd BLAST46
ChainiPRO_000000244447 – 529ATP synthase subunit beta, mitochondrialAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106O-linked (GlcNAc) serineBy similarity1
Modified residuei124N6-acetyllysine; alternateCombined sources1
Modified residuei124N6-succinyllysine; alternateCombined sources1
Modified residuei133N6-acetyllysine; alternateCombined sources1
Modified residuei133N6-succinyllysine; alternateCombined sources1
Modified residuei161N6-acetyllysine; alternateCombined sources1
Modified residuei161N6-succinyllysine; alternateCombined sources1
Modified residuei198N6-acetyllysineCombined sources1
Modified residuei259N6-acetyllysine; alternateCombined sources1
Modified residuei259N6-succinyllysine; alternateCombined sources1
Modified residuei264N6-acetyllysine; alternateCombined sources1
Modified residuei264N6-succinyllysine; alternateCombined sources1
Modified residuei312PhosphothreonineCombined sources1
Modified residuei426N6-acetyllysineCombined sources1
Modified residuei433PhosphoserineBy similarity1
Modified residuei480N6-acetyllysineCombined sources1
Modified residuei485N6-acetyllysineCombined sources1
Modified residuei522N6-acetyllysine; alternateCombined sources1
Modified residuei522N6-succinyllysine; alternateCombined sources1
Modified residuei529PhosphoserineCombined sources1

Post-translational modificationi

Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP56480
MaxQBiP56480
PaxDbiP56480
PeptideAtlasiP56480
PRIDEiP56480
TopDownProteomicsiP56480

2D gel databases

COMPLUYEAST-2DPAGEiP56480
REPRODUCTION-2DPAGEiIPI00468481
P56480
SWISS-2DPAGEiP56480
UCD-2DPAGEiP56480

PTM databases

CarbonylDBiP56480
iPTMnetiP56480
PhosphoSitePlusiP56480
SwissPalmiP56480

Expressioni

Gene expression databases

BgeeiENSMUSG00000025393
GenevisibleiP56480 MM

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, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68 (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 efficency (By similarity). Interacts with CLN5 and PPT1 (PubMed:19941651).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198254, 10 interactors
IntActiP56480, 34 interactors
MINTiP56480
STRINGi10090.ENSMUSP00000026459

Structurei

3D structure databases

ProteinModelPortaliP56480
SMRiP56480
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
HOVERGENiHBG004307
InParanoidiP56480
KOiK02133
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
PhylomeDBiP56480
TreeFamiTF105640

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

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

P56480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA
60 70 80 90 100
SAAPKAGTAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA
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 NIVGNEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
Length:529
Mass (Da):56,300
Last modified:May 2, 2002 - v2
Checksum:iF3E1100C390A78A7
GO

Sequence cautioni

The sequence AAH37127 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25A → V in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti43A → V in BAE35088 (PubMed:16141072).Curated1
Sequence conflicti76D → G in BAE40961 (PubMed:16141072).Curated1
Sequence conflicti92D → E in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti134I → V in BAE31497 (PubMed:16141072).Curated1
Sequence conflicti239R → K in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti271Q → R in BAE38888 (PubMed:16141072).Curated1
Sequence conflicti271Q → R in BAE39301 (PubMed:16141072).Curated1
Sequence conflicti279 – 280RA → PT in AAB86421 (PubMed:10657236).Curated2
Sequence conflicti288T → A in BAE31497 (PubMed:16141072).Curated1
Sequence conflicti288T → A in BAE31630 (PubMed:16141072).Curated1
Sequence conflicti375T → N in BAE30095 (PubMed:16141072).Curated1
Sequence conflicti383T → S in BAB22802 (PubMed:16141072).Curated1
Sequence conflicti433 – 434SL → FF in AAB86421 (PubMed:10657236).Curated2
Sequence conflicti466Q → H in BAB22802 (PubMed:16141072).Curated1
Sequence conflicti469Q → R in BAE39797 (PubMed:16141072).Curated1
Sequence conflicti518A → V in BAE35331 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030559 mRNA Translation: AAB86421.1
AK003460 mRNA Translation: BAB22802.1
AK010314 mRNA Translation: BAB26846.1
AK084009 mRNA Translation: BAC39095.1
AK145684 mRNA Translation: BAE26587.1
AK148891 mRNA Translation: BAE28692.1
AK150599 mRNA Translation: BAE29691.1
AK151081 mRNA Translation: BAE30095.1
AK151600 mRNA Translation: BAE30540.1
AK152788 mRNA Translation: BAE31497.1
AK152976 mRNA Translation: BAE31630.1
AK153099 mRNA Translation: BAE31720.1
AK159444 mRNA Translation: BAE35088.1
AK159737 mRNA Translation: BAE35331.1
AK159978 mRNA Translation: BAE35529.1
AK160199 mRNA Translation: BAE35689.1
AK160608 mRNA Translation: BAE35911.1
AK164383 mRNA Translation: BAE37764.1
AK166525 mRNA Translation: BAE38829.1
AK166603 mRNA Translation: BAE38888.1
AK166979 mRNA Translation: BAE39161.1
AK167119 mRNA Translation: BAE39267.1
AK167160 mRNA Translation: BAE39301.1
AK167728 mRNA Translation: BAE39769.1
AK167764 mRNA Translation: BAE39797.1
AK168692 mRNA Translation: BAE40537.1
AK168941 mRNA Translation: BAE40749.1
AK169184 mRNA Translation: BAE40961.1
BC018392 mRNA Translation: AAH18392.1
BC037127 mRNA Translation: AAH37127.1 Different initiation.
BC046616 mRNA Translation: AAH46616.1
DQ403100 mRNA Translation: ABD77233.1
CCDSiCCDS24259.1
RefSeqiNP_058054.2, NM_016774.3
UniGeneiMm.238973

Genome annotation databases

EnsembliENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393
GeneIDi11947
KEGGimmu:11947
UCSCiuc007hle.1 mouse

Similar proteinsi

Entry informationi

Entry nameiATPB_MOUSE
AccessioniPrimary (citable) accession number: P56480
Secondary accession number(s): Q0QEP4
, Q3TFD7, Q3TIP9, Q3TK44, Q3TWD5, Q3TX28, Q3U6U4, Q3U774, Q3UB69, Q3UF69, Q8CI65, Q8VEJ5, Q9CTI7, Q9CWX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: April 25, 2018
This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health