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Protein

ATPase inhibitor, mitochondrial

Gene

Atpif1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endogenous F1F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F1F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F1F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase inhibitor, mitochondrial
Alternative name(s):
Inhibitor of F(1)F(o)-ATPase
Short name:
IF(1)
Short name:
IF1
Gene namesi
Name:Atpif1
Synonyms:Atpi, If1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1196457. Atpif1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionBy similarityAdd
BLAST
Chaini26 – 10681ATPase inhibitor, mitochondrialPRO_0000002548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei103 – 1031N6-succinyllysineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35143.
PaxDbiO35143.
PeptideAtlasiO35143.
PRIDEiO35143.
TopDownProteomicsiO35143.

PTM databases

iPTMnetiO35143.
PhosphoSiteiO35143.

Expressioni

Gene expression databases

BgeeiENSMUSG00000054428.
CleanExiMM_ATPIF1.
ExpressionAtlasiO35143. baseline and differential.
GenevisibleiO35143. MM.

Interactioni

Subunit structurei

Homodimer; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198273. 1 interaction.
IntActiO35143. 1 interaction.
MINTiMINT-4088754.
STRINGi10090.ENSMUSP00000064282.

Structurei

3D structure databases

ProteinModelPortaliO35143.
SMRiO35143. Positions 37-103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 5227N-terminal inhibitory regionBy similarityAdd
BLAST
Regioni74 – 10633Antiparallel alpha-helical coiled coil regionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili60 – 10647Sequence analysisAdd
BLAST

Domaini

Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-52) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5A1-ATP5B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5C1). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (By similarity).By similarity

Sequence similaritiesi

Belongs to the ATPase inhibitor family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiO35143.
OMAiHHEDEIS.
OrthoDBiEOG091G1B33.
TreeFamiTF320659.

Family and domain databases

InterProiIPR007648. ATPase_inhibitor_mt.
[Graphical view]
PfamiPF04568. IATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O35143-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSALAVRA RFGVWGMKVL QTRGFVSDSS DSMDTGAGSI REAGGAFGKR
60 70 80 90 100
EKAEEDRYFR EKTKEQLAAL RKHHEDEIDH HSKEIERLQK QIERHKKKIQ

QLKNNH
Length:106
Mass (Da):12,159
Last modified:October 3, 2012 - v2
Checksum:i78C0FE0CD04FA2D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931E → D in AAB69647 (PubMed:9497501).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002718 mRNA. Translation: AAB69647.1.
AK008346 mRNA. Translation: BAB25618.1.
AK152389 mRNA. Translation: BAE31177.1.
AL805897 Genomic DNA. Translation: CAM26517.1.
CH466552 Genomic DNA. Translation: EDL30101.1.
BC012680 mRNA. Translation: AAH12680.1.
CCDSiCCDS18727.1.
RefSeqiNP_031538.2. NM_007512.4.
XP_006538565.1. XM_006538502.1.
UniGeneiMm.2171.

Genome annotation databases

EnsembliENSMUST00000067496; ENSMUSP00000064282; ENSMUSG00000054428.
GeneIDi11983.
KEGGimmu:11983.
UCSCiuc008vbl.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002718 mRNA. Translation: AAB69647.1.
AK008346 mRNA. Translation: BAB25618.1.
AK152389 mRNA. Translation: BAE31177.1.
AL805897 Genomic DNA. Translation: CAM26517.1.
CH466552 Genomic DNA. Translation: EDL30101.1.
BC012680 mRNA. Translation: AAH12680.1.
CCDSiCCDS18727.1.
RefSeqiNP_031538.2. NM_007512.4.
XP_006538565.1. XM_006538502.1.
UniGeneiMm.2171.

3D structure databases

ProteinModelPortaliO35143.
SMRiO35143. Positions 37-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198273. 1 interaction.
IntActiO35143. 1 interaction.
MINTiMINT-4088754.
STRINGi10090.ENSMUSP00000064282.

PTM databases

iPTMnetiO35143.
PhosphoSiteiO35143.

Proteomic databases

EPDiO35143.
PaxDbiO35143.
PeptideAtlasiO35143.
PRIDEiO35143.
TopDownProteomicsiO35143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067496; ENSMUSP00000064282; ENSMUSG00000054428.
GeneIDi11983.
KEGGimmu:11983.
UCSCiuc008vbl.3. mouse.

Organism-specific databases

CTDi93974.
MGIiMGI:1196457. Atpif1.

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiO35143.
OMAiHHEDEIS.
OrthoDBiEOG091G1B33.
TreeFamiTF320659.

Miscellaneous databases

PROiO35143.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000054428.
CleanExiMM_ATPIF1.
ExpressionAtlasiO35143. baseline and differential.
GenevisibleiO35143. MM.

Family and domain databases

InterProiIPR007648. ATPase_inhibitor_mt.
[Graphical view]
PfamiPF04568. IATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATIF1_MOUSE
AccessioniPrimary (citable) accession number: O35143
Secondary accession number(s): Q9D879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 3, 2012
Last modified: September 7, 2016
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.