ATP5F1B ATP synthase F1 subunit beta [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: ATP5F1Bprovided by VGNC
Official Full Name: ATP synthase F1 subunit betaprovided by VGNC
Primary source: VGNC:VGNC:26300
See related: BGD:BT12445; Ensembl:ENSBTAG00000013315
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: ATP5B
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 5

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
RS_2023_09	current	ARS-UCD2.0 (GCF_002263795.3)	5	NC_037332.1 (56789641..56795014)

Chromosome 5 - NC_037332.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:: NC_037332.1 Chromosome 5 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Combining cryoelectron microscopy data with bioinformatic analysis allowed the authors to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits.
Title: Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
These data indicate that interaction with the alpha-phosphate is not crucial for efficient catalysis, but likely contributes to avoid formation of ADP-inhibited intermediates.
Title: Effects of an ATP analogue, adenosine 5'-[α-thio]-triphosphate, on F1-ATPase rotary catalysis, torque generation, and inhibited intermediated formation.
Molecular dynamics simulations show that the nucleotide-free beta subunit, initially in the open, low-affinity state, undergoes a spontaneous closing transition to the half-open state in response to the gamma rotation in the synthesis direction.
Title: Rotation triggers nucleotide-independent conformational transition of the empty β subunit of F₁-ATPase.
analysis of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
Title: Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria.
Molecular dynamics simulations of F1-ATPase suggest that the equilibrium conformation of a nucleotide-free beta-subunit is the open conformation and that the transition from the closed to the open conformation can occur in a few tens of nanoseconds.
Title: Domain motion of individual F1-ATPase β-subunits during unbiased molecular dynamics simulations.
molecular dynamic analysis of interaction between the gamma-subunit and a C-terminal fragment of the beta-subunit of F1-ATPase
Title: A molecular dynamic analysis of interaction between the gamma-subunit and a C-terminal fragment of the beta-subunit of F1-ATPase.
The catalytic sites of beef heart mitochondrial F1-ATPase were studied by electron spin echo envelope modulation (ESEEM) spectroscopy, using Mn(II) as a paramagnetic probe
Title: Conformational role of the divalent metal in bovine heart mitochondrial F1-ATPase: an electron spin echo envelope modulation study.
Inhibition arises by IF(1) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP) interface, thereby preventing it from hydrolyzing the bound ATP.
Title: How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria.
The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis
Title: Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols.

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General gene information

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Markers

MARC_26134-26135:1030377217:1 (e-PCR)
- UniSTS:268952

ATP5B (e-PCR)
- UniSTS:504033

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info	PubMed
enables proton-transporting ATP synthase activity, rotational mechanism	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in proton motive force-driven mitochondrial ATP synthesis	IEA Inferred from Electronic Annotation more info	PubMed
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
part_of proton-transporting ATP synthase complex, catalytic core F(1)	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: ATP synthase subunit beta, mitochondrial

Names: ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide; F1-ATPase beta-subunit; mitochondrial ATP synthase beta subunit

NP_786990.1

EC 7.1.2.2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.