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Protein

ATP synthase subunit s, mitochondrial

Gene

ATP5S

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H+ conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Magnesium; via carbonyl oxygen1
Metal bindingi93Magnesium1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandMagnesium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit s, mitochondrial
Alternative name(s):
ATP synthase-coupling factor B
Short name:
FB
Mitochondrial ATP synthase regulatory component factor B
Gene namesi
Name:ATP5S
Synonyms:ATPW
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

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(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25Mitochondrion1 PublicationAdd BLAST25
ChainiPRO_000000253726 – 200ATP synthase subunit s, mitochondrialAdd BLAST175

Proteomic databases

PaxDbiP22027
PRIDEiP22027

Expressioni

Gene expression databases

BgeeiENSBTAG00000015202

Interactioni

Subunit structurei

Homotetramer. Associates with ATP synthase.1 Publication

Protein-protein interaction databases

DIPiDIP-46291N
STRINGi9913.ENSBTAP00000020228

Structurei

Secondary structure

1200
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 35Combined sources10
Helixi39 – 45Combined sources7
Helixi47 – 57Combined sources11
Beta strandi61 – 64Combined sources4
Helixi74 – 76Combined sources3
Beta strandi87 – 94Combined sources8
Helixi99 – 105Combined sources7
Beta strandi113 – 118Combined sources6
Helixi124 – 131Combined sources8
Helixi134 – 139Combined sources6
Beta strandi142 – 147Combined sources6
Helixi153 – 158Combined sources6
Helixi159 – 161Combined sources3
Beta strandi167 – 172Combined sources6
Helixi179 – 189Combined sources11
Beta strandi194 – 198Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DZEX-ray1.15A26-200[»]
3E2JX-ray2.90A/B/C/D26-200[»]
3E3ZX-ray1.70A26-200[»]
3E4GX-ray0.96A26-200[»]
ProteinModelPortaliP22027
SMRiP22027
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22027

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati62 – 87LRR 11 PublicationAdd BLAST26
Repeati88 – 116LRR 21 PublicationAdd BLAST29
Repeati117 – 141LRR 31 PublicationAdd BLAST25
Repeati142 – 173LRR 41 PublicationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 61N-terminal domainAdd BLAST61

Sequence similaritiesi

Belongs to the ATP synthase subunit s family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG3864 Eukaryota
ENOG4110375 LUCA
GeneTreeiENSGT00530000063680
HOGENOMiHOG000230741
HOVERGENiHBG050615
InParanoidiP22027
KOiK07554
OMAiIFHNCKH
OrthoDBiEOG091G0WCB
TreeFamiTF315274

Family and domain databases

Gene3Di3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR026063 ATP_synth_s
IPR032675 LRR_dom_sf
PANTHERiPTHR13382:SF1 PTHR13382:SF1, 1 hit

Sequencei

Sequence statusi: Complete.

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

P22027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLFGKISQQ LCGLKKLPWS RDSRYFWGWL NAVFNKVDHD RIRDVGPDRA
60 70 80 90 100
ASEWLLRCGA MVRYHGQQRW QKDYNHLPTG PLDKYKIQAI DATDSCIMSI
110 120 130 140 150
GFDHMEGLQY VEKIRLCKCH YIEDGCLERL SQLENLQKSM LEMEIISCGN
160 170 180 190 200
VTDKGIIALH HFRNLKYLFL SDLPGVKEKE KIVQAFKTSL PSLELKLDLK
Length:200
Mass (Da):23,293
Last modified:June 21, 2005 - v2
Checksum:i2C439BE3835E206D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58C → G AA sequence (PubMed:2148527).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti26Missing in one third of the chains. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY780292 mRNA Translation: AAV52866.1
BC109757 mRNA Translation: AAI09758.1
PIRiS13005
RefSeqiNP_001007813.1, NM_001007812.3
XP_010807544.1, XM_010809242.2
UniGeneiBt.13666

Genome annotation databases

EnsembliENSBTAT00000020228; ENSBTAP00000020228; ENSBTAG00000015202
GeneIDi493709
KEGGibta:493709

Similar proteinsi

Entry informationi

Entry nameiATP5S_BOVIN
AccessioniPrimary (citable) accession number: P22027
Secondary accession number(s): Q32L55, Q5S3X8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 21, 2005
Last modified: April 25, 2018
This is version 115 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health