ATP synthase subunit b, mitochondrial precursor

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P13619 (AT5F1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit b, mitochondrial
Short name=ATPase subunit b

Gene names

Name:	ATP5F1
Synonyms:	ATP5F

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subcellular location	Mitochondrion. Mitochondrion inner membrane.
Sequence similarities	Belongs to the eukaryotic ATPase B chain family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from sequence or structural similarity. Source: RefGenome
Cellular component	mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from sequence or structural similarity. Source: RefGenome
Molecular function	hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from sequence or structural similarity. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 42

Mitochondrion Ref.2 Ref.3

Chain

43 – 256

214

ATP synthase subunit b, mitochondrial

PRO_0000071671

Amino acid modifications

Modified residue

115

N6-acetyllysine By similarity

Modified residue

131

N6-acetyllysine By similarity

Modified residue

162

N6-acetyllysine By similarity

Modified residue

221

N6-acetyllysine By similarity

Modified residue

233

N6-acetyllysine By similarity

Experimental info

Sequence conflict

K → Y AA sequence Ref.3

Secondary structure

256

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13619 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 5766369D254B3D9A
Show »

FASTA

256

28,822

        10         20         30         40         50         60 
MLSRVVLSAA AAAAPSLKNA ALLGPGVLQA TRIFHTGQPS LAPVPPLPEH GGKVRFGLIP 

        70         80         90        100        110        120 
EEFFQFLYPK TGVTGPYVLG TGLILYLLSK EIYVITPETF SAISTIGFLV YIVKKYGASV 

       130        140        150        160        170        180 
GEFADKLNEQ KIAQLEEVKQ ASIKQIQDAI DMEKSQQALV QKRHYLFDVQ RNNIAMALEV 

       190        200        210        220        230        240 
TYRERLHRVY REVKNRLDYH ISVQNMMRQK EQEHMINWVE KRVVQSISAQ QEKETIAKCI 

       250 
ADLKLLSKKA QAQPVM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.
[2]	"ATP synthase from bovine mitochondria. The characterization and sequence analysis of two membrane-associated sub-units and of the corresponding cDNAs." Walker J.E., Runswick M.J., Poulter L. J. Mol. Biol. 197:89-100(1987) [PubMed: 2890767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-256, PROTEIN SEQUENCE OF 43-256.
[3]	"Identification of the subunits of F1F0-ATPase from bovine heart mitochondria." Walker J.E., Lutter R., Dupuis A., Runswick M.J. Biochemistry 30:5369-5378(1991) [PubMed: 1827992] [Abstract] Cited for: PROTEIN SEQUENCE OF 43-53. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC110212 mRNA. Translation: AAI10213.1.
X06088 mRNA. Translation: CAA29472.1.

IPI

IPI00693235.

PIR

S00763.

RefSeq

NP_001033590.1. NM_001038501.1.

UniGene

Bt.3867.
Bt.61189.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CLY	X-ray	2.80	A/D	43-256	[»]
2WSS	X-ray	3.20	T/X	141-256	[»]

ProteinModelPortal

P13619.

SMR

P13619. Positions 121-225.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38983N.

IntAct

P13619. 1 interaction.

MINT

MINT-5006961.

STRING

P13619.

Proteomic databases

PRIDE

P13619.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000008447; ENSBTAP00000008447; ENSBTAG00000006441.

GeneID

282701.

KEGG

bta:282701.

Organism-specific databases

CTD

515.

Phylogenomic databases

eggNOG

maNOG05007.

GeneTree

ENSGT00390000001958.

HOVERGEN

HBG050604.

InParanoid

P13619.

OMA

FRERAMN.

OrthoDB

EOG4K3KXB.

PhylomeDB

P13619.

Family and domain databases

InterPro

IPR008688. ATPase_F0-cplx_bsu_mt.
IPR013837. ATPase_F0-cplx_bsu_mt_met.
[Graphical view]

K02127.

PANTHER

PTHR12733. ATPase_F0_B_mt_met. 1 hit.

Pfam

PF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AT5F1_BOVIN

Accession

Primary (citable) accession number: P13619
Secondary accession number(s): Q2TBH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 25, 2006
Last modified:	November 16, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents