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Protein

ATPase inhibitor, mitochondrial

Gene

ATP5IF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. 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.4 Publications

GO - Molecular functioni

  • angiostatin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • ATPase inhibitor activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • enzyme binding Source: CAFA
  • enzyme inhibitor activity Source: ProtInc
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • erythrocyte differentiation Source: UniProtKB
  • generation of precursor metabolites and energy Source: ProtInc
  • heme biosynthetic process Source: UniProtKB
  • mitochondrial depolarization Source: ParkinsonsUK-UCL
  • negative regulation of ATPase activity Source: ParkinsonsUK-UCL
  • negative regulation of endothelial cell proliferation Source: UniProtKB
  • negative regulation of hydrolase activity Source: UniProtKB
  • positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: Ensembl
  • positive regulation of proteolysis involved in cellular protein catabolic process Source: ParkinsonsUK-UCL
  • protein homooligomerization Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • reactive oxygen species metabolic process Source: Ensembl
  • regulation of ATP metabolic process Source: ParkinsonsUK-UCL
  • regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase inhibitor, mitochondrialCurated
Alternative name(s):
ATP synthase F1 subunit epsilonCurated
Inhibitor of F(1)F(o)-ATPase
Short name:
IF(1)
Short name:
IF1
Gene namesi
Name:ATP5IF1Imported
Synonyms:ATPI, ATPIF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000130770.17
HGNCiHGNC:871 ATP5IF1
MIMi614981 gene
neXtProtiNX_Q9UII2

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

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi93974
OpenTargetsiENSG00000130770
PharmGKBiPA25173

Polymorphism and mutation databases

BioMutaiATPIF1
DMDMi12585262

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionCombined sources1 PublicationAdd BLAST25
ChainiPRO_000000254726 – 106ATPase inhibitor, mitochondrialAdd BLAST81

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei39PhosphoserineCombined sources1
Modified residuei63PhosphoserineCombined sources1
Modified residuei103N6-succinyllysineBy similarity1

Post-translational modificationi

Exhibits variability in chain length, mitochondria have distinct pools of protein cleaved after the 24th, 25th, and 26th amino acid.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UII2
PaxDbiQ9UII2
PeptideAtlasiQ9UII2
PRIDEiQ9UII2
ProteomicsDBi84524
84525 [Q9UII2-2]
84526 [Q9UII2-3]
TopDownProteomicsiQ9UII2-1 [Q9UII2-1]
Q9UII2-2 [Q9UII2-2]

PTM databases

iPTMnetiQ9UII2
PhosphoSitePlusiQ9UII2

Expressioni

Gene expression databases

BgeeiENSG00000130770
CleanExiHS_ATPIF1
ExpressionAtlasiQ9UII2 baseline and differential
GenevisibleiQ9UII2 HS

Organism-specific databases

HPAiHPA027999

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

  • angiostatin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • enzyme binding Source: CAFA
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi125063, 25 interactors
CORUMiQ9UII2
IntActiQ9UII2, 15 interactors
MINTiQ9UII2
STRINGi9606.ENSP00000335203

Structurei

3D structure databases

ProteinModelPortaliQ9UII2
SMRiQ9UII2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 52N-terminal inhibitory regionBy similarityAdd BLAST27
Regioni74 – 106Antiparallel alpha-helical coiled coil regionBy similarityAdd BLAST33

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili63 – 106Sequence analysisAdd BLAST44

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) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). 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
InParanoidiQ9UII2
KOiK22255
OMAiAEEEMYF
OrthoDBiEOG091G1B33
PhylomeDBiQ9UII2
TreeFamiTF320659

Family and domain databases

InterProiView protein in InterPro
IPR007648 ATPase_inhibitor_mt
PfamiView protein in Pfam
PF04568 IATP, 1 hit

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UII2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVTALAART WLGVWGVRTM QARGFGSDQS ENVDRGAGSI REAGGAFGKR
60 70 80 90 100
EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK

MLKHDD
Length:106
Mass (Da):12,249
Last modified:May 1, 2000 - v1
Checksum:iA6144431125D5A86
GO
Isoform 2 (identifier: Q9UII2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-106: AQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD → HYRLCFEISLG

Show »
Length:71
Mass (Da):7,912
Checksum:iD7E481A83975E005
GO
Isoform 3 (identifier: Q9UII2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-106: Missing.

Show »
Length:60
Mass (Da):6,592
Checksum:i151FBFCD72F13D1C
GO

Sequence cautioni

The sequence AAH04955 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60R → RR in CAI46227 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04141761 – 106AQSRE…LKHDD → HYRLCFEISLG in isoform 2. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_04141861 – 106Missing in isoform 3. 1 PublicationAdd BLAST46

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029042 mRNA Translation: BAA88422.1
AK316600 mRNA Translation: BAG38187.1
DB030607 mRNA No translation available.
AL050386 mRNA Translation: CAI46227.1
AF114836 mRNA Translation: AAP97235.1
AY005470 Genomic DNA Translation: AAF97495.1
AL583540 mRNA No translation available.
BT009849 mRNA Translation: AAP88851.1
CR457097 mRNA Translation: CAG33378.1
AL353622 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX07704.1
BC004955 mRNA Translation: AAH04955.1 Different initiation.
BC009677 mRNA Translation: AAH09677.1
CCDSiCCDS319.1 [Q9UII2-1]
CCDS320.1 [Q9UII2-2]
CCDS44096.1 [Q9UII2-3]
PIRiJC7175
RefSeqiNP_057395.1, NM_016311.4 [Q9UII2-1]
NP_835497.1, NM_178190.2 [Q9UII2-2]
NP_835498.1, NM_178191.2 [Q9UII2-3]
UniGeneiHs.744914

Genome annotation databases

EnsembliENST00000335514; ENSP00000335203; ENSG00000130770 [Q9UII2-1]
ENST00000465645; ENSP00000437337; ENSG00000130770 [Q9UII2-3]
ENST00000497986; ENSP00000435579; ENSG00000130770 [Q9UII2-2]
ENST00000642464; ENSP00000496122; ENSG00000285390 [Q9UII2-2]
ENST00000647074; ENSP00000494248; ENSG00000285390 [Q9UII2-1]
ENST00000647380; ENSP00000496605; ENSG00000285390 [Q9UII2-3]
GeneIDi93974
KEGGihsa:93974
UCSCiuc001bpp.4 human [Q9UII2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiATIF1_HUMAN
AccessioniPrimary (citable) accession number: Q9UII2
Secondary accession number(s): Q5JXL8, Q6IAQ7, Q9BSL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 18, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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