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Protein

ATP synthase F(0) complex subunit B1, mitochondrial

Gene

ATP5F1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit B1, mitochondrial
Alternative name(s):
ATP synthase subunit b
Short name:
ATPase subunit b
Gene namesi
Name:ATP5F1
Synonyms:ATP5F
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242Mitochondrion2 PublicationsAdd
BLAST
Chaini43 – 256214ATP synthase F(0) complex subunit B1, mitochondrialPRO_0000071671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311N6-succinyllysineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei162 – 1621N6-acetyllysineBy similarity
Modified residuei221 – 2211N6-acetyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei244 – 2441N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP13619.
PeptideAtlasiP13619.
PRIDEiP13619.

Expressioni

Gene expression databases

BgeeiENSBTAG00000006441.

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 MP68.1 Publication

Protein-protein interaction databases

DIPiDIP-38983N.
IntActiP13619. 2 interactions.
MINTiMINT-5006961.
STRINGi9913.ENSBTAP00000008447.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi122 – 15938Combined sources
Helixi161 – 1633Combined sources
Helixi164 – 22360Combined sources
Helixi231 – 2333Combined sources
Helixi235 – 24814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLYX-ray2.80A/D43-256[»]
2WSSX-ray3.20T/X141-256[»]
4B2Qelectron microscopy37.00T/t121-249[»]
5ARAelectron microscopy6.70T76-249[»]
5AREelectron microscopy7.40T76-249[»]
5ARHelectron microscopy7.20T76-249[»]
5ARIelectron microscopy7.40T76-249[»]
5FIJelectron microscopy7.40T76-249[»]
5FIKelectron microscopy6.40T76-249[»]
5FILelectron microscopy7.10T76-249[»]
ProteinModelPortaliP13619.
SMRiP13619. Positions 121-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13619.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase B chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410INNH. Eukaryota.
ENOG4111WYE. LUCA.
GeneTreeiENSGT00390000001958.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiP13619.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG091G0DPN.
TreeFamiTF313250.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRVVLSAA AAAAPSLKNA ALLGPGVLQA TRIFHTGQPS LAPVPPLPEH
60 70 80 90 100
GGKVRFGLIP EEFFQFLYPK TGVTGPYVLG TGLILYLLSK EIYVITPETF
110 120 130 140 150
SAISTIGFLV YIVKKYGASV GEFADKLNEQ KIAQLEEVKQ ASIKQIQDAI
160 170 180 190 200
DMEKSQQALV QKRHYLFDVQ RNNIAMALEV TYRERLHRVY REVKNRLDYH
210 220 230 240 250
ISVQNMMRQK EQEHMINWVE KRVVQSISAQ QEKETIAKCI ADLKLLSKKA

QAQPVM
Length:256
Mass (Da):28,822
Last modified:July 25, 2006 - v2
Checksum:i5766369D254B3D9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531K → Y AA sequence (PubMed:1827992).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC110212 mRNA. Translation: AAI10213.1.
X06088 mRNA. Translation: CAA29472.1.
PIRiS00763.
RefSeqiNP_001033590.1. NM_001038501.2.
UniGeneiBt.3867.
Bt.61189.

Genome annotation databases

EnsembliENSBTAT00000008447; ENSBTAP00000008447; ENSBTAG00000006441.
GeneIDi282701.
KEGGibta:282701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC110212 mRNA. Translation: AAI10213.1.
X06088 mRNA. Translation: CAA29472.1.
PIRiS00763.
RefSeqiNP_001033590.1. NM_001038501.2.
UniGeneiBt.3867.
Bt.61189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CLYX-ray2.80A/D43-256[»]
2WSSX-ray3.20T/X141-256[»]
4B2Qelectron microscopy37.00T/t121-249[»]
5ARAelectron microscopy6.70T76-249[»]
5AREelectron microscopy7.40T76-249[»]
5ARHelectron microscopy7.20T76-249[»]
5ARIelectron microscopy7.40T76-249[»]
5FIJelectron microscopy7.40T76-249[»]
5FIKelectron microscopy6.40T76-249[»]
5FILelectron microscopy7.10T76-249[»]
ProteinModelPortaliP13619.
SMRiP13619. Positions 121-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38983N.
IntActiP13619. 2 interactions.
MINTiMINT-5006961.
STRINGi9913.ENSBTAP00000008447.

Proteomic databases

PaxDbiP13619.
PeptideAtlasiP13619.
PRIDEiP13619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008447; ENSBTAP00000008447; ENSBTAG00000006441.
GeneIDi282701.
KEGGibta:282701.

Organism-specific databases

CTDi515.

Phylogenomic databases

eggNOGiENOG410INNH. Eukaryota.
ENOG4111WYE. LUCA.
GeneTreeiENSGT00390000001958.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiP13619.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG091G0DPN.
TreeFamiTF313250.

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP13619.

Gene expression databases

BgeeiENSBTAG00000006441.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAT5F1_BOVIN
AccessioniPrimary (citable) accession number: P13619
Secondary accession number(s): Q2TBH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 25, 2006
Last modified: September 7, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.