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Protein

ATPase inhibitor, mitochondrial

Gene

ATPIF1

Organism
Bos taurus (Bovine)
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.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei51 – 511Participates in pH sensing
Sitei74 – 741Participates in pH sensing

GO - Molecular functioni

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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi47 – 471F → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi49 – 491K → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi50 – 501R → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi51 – 511E → A: No effect on F(1)F(o)-ATP synthase-binding. 2 Publications
Mutagenesisi51 – 511E → A: Retains its inhibitory activity at pH 8.2 although it still form a homotetramer at high pH. 2 Publications
Mutagenesisi52 – 521Q → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi53 – 531A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi54 – 541E → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi55 – 551E → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi56 – 561E → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi57 – 571R → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi58 – 581Y → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi59 – 591F → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi60 – 601R → A: No effect on F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi62 – 621R → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi64 – 641K → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi65 – 651E → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi66 – 661Q → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi67 – 671L → A: Impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi68 – 681A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi69 – 691A → V: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi70 – 701L → A: Strongly impairs F(1)F(o)-ATP synthase-binding. 1 Publication
Mutagenesisi74 – 741H → K: Retains its inhibitory activity at pH 8.2 and does not form a homotetramer at high pH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525Mitochondrion1 PublicationAdd
BLAST
Chaini26 – 10984ATPase inhibitor, mitochondrialPRO_0000002546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-succinyllysineBy similarity

Proteomic databases

PaxDbiP01096.
PRIDEiP01096.

Expressioni

Gene expression databases

BgeeiENSBTAG00000006342.

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 7.0.6 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

DIPiDIP-46311N.
STRINGi9913.ENSBTAP00000008319.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 323Combined sources
Helixi33 – 353Combined sources
Helixi39 – 424Combined sources
Helixi46 – 7328Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMJX-ray2.20A/B/C/D26-109[»]
1HF9NMR-A/B69-109[»]
1OHHX-ray2.80H26-109[»]
2V7QX-ray2.10J26-85[»]
4TSFX-ray3.20H/I26-85[»]
4TT3X-ray3.21H/I/J26-85[»]
4Z1MX-ray3.30H/I/J26-85[»]
ProteinModelPortaliP01096.
SMRiP01096. Positions 29-65, 69-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01096.

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili69 – 10941Add
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 26-62) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-62) 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 (PubMed:11742976, PubMed:12923572 and PubMed:17895376).

Sequence similaritiesi

Belongs to the ATPase inhibitor family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiP01096.
OMAiSHHAKEI.
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.

P01096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATALAART RQAVWSVWAM QGRGFGSESG DNVRSSAGAV RDAGGAFGKR
60 70 80 90 100
EQAEEERYFR ARAKEQLAAL KKHHENEISH HAKEIERLQK EIERHKQSIK

KLKQSEDDD
Length:109
Mass (Da):12,301
Last modified:January 1, 1990 - v2
Checksum:i0F8816DECCAABA7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551E → Q AA sequence (PubMed:6461003).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22559 mRNA. Translation: AAA30396.1.
BC111645 mRNA. Translation: AAI11646.1.
PIRiC27382. IWBO.
RefSeqiNP_787010.1. NM_175816.3.
UniGeneiBt.59150.

Genome annotation databases

EnsembliENSBTAT00000008319; ENSBTAP00000008319; ENSBTAG00000006342.
GeneIDi327699.
KEGGibta:327699.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22559 mRNA. Translation: AAA30396.1.
BC111645 mRNA. Translation: AAI11646.1.
PIRiC27382. IWBO.
RefSeqiNP_787010.1. NM_175816.3.
UniGeneiBt.59150.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMJX-ray2.20A/B/C/D26-109[»]
1HF9NMR-A/B69-109[»]
1OHHX-ray2.80H26-109[»]
2V7QX-ray2.10J26-85[»]
4TSFX-ray3.20H/I26-85[»]
4TT3X-ray3.21H/I/J26-85[»]
4Z1MX-ray3.30H/I/J26-85[»]
ProteinModelPortaliP01096.
SMRiP01096. Positions 29-65, 69-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46311N.
STRINGi9913.ENSBTAP00000008319.

Proteomic databases

PaxDbiP01096.
PRIDEiP01096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008319; ENSBTAP00000008319; ENSBTAG00000006342.
GeneIDi327699.
KEGGibta:327699.

Organism-specific databases

CTDi93974.

Phylogenomic databases

eggNOGiENOG410J2TJ. Eukaryota.
ENOG41127Z5. LUCA.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiP01096.
OMAiSHHAKEI.
OrthoDBiEOG091G1B33.
TreeFamiTF320659.

Miscellaneous databases

EvolutionaryTraceiP01096.

Gene expression databases

BgeeiENSBTAG00000006342.

Family and domain databases

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

Entry informationi

Entry nameiATIF1_BOVIN
AccessioniPrimary (citable) accession number: P01096
Secondary accession number(s): Q2M2T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: September 7, 2016
This is version 123 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.