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Protein

ATPase inhibitor A, mitochondrial

Gene

atpif1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

  • erythrocyte differentiation Source: UniProtKB
  • heme biosynthetic process Source: UniProtKB
  • negative regulation of hydrolase activity Source: UniProtKB
  • negative regulation of nucleotide metabolic process Source: InterPro
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase inhibitor A, mitochondrial
Alternative name(s):
Inhibitor of F(1)F(o)-ATPase A
Short name:
IF(1) A
Short name:
IF1 A
Protein pinotage
Gene namesi
Name:atpif1
Synonyms:atpia, atpif1a, pnt
ORF Names:Zgc:162207
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 19

Organism-specific databases

ZFINiZDB-GENE-070410-36. atpif1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Defects in circulating erythroid cells. Embryos are anemic despite normal expression of the erythroid cell markers. The erythrocytes from embryos that survive to adult stage exhibit hypochromic, microcytic anemia. Histological analysis of adult haematopoietic tissues does not show morphological defects. Defects are due to changes in the mitochondrial pH-and consequently the redox potential-to change to a level that reduces [2Fe-2S] cluster-containing fech activity, thereby reducing heme synthesis, resulting in hypochromic anemia.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 105ATPase inhibitor A, mitochondrialPRO_0000421768
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PRIDEiA3KNL5.

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

Protein-protein interaction databases

STRINGi7955.ENSDARP00000081676.

Structurei

3D structure databases

ProteinModelPortaliA3KNL5.
SMRiA3KNL5. Positions 43-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 5130N-terminal inhibitory regionBy similarityAdd
BLAST
Regioni73 – 10533Antiparallel alpha-helical coiled coil regionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili58 – 10548Sequence AnalysisAdd
BLAST

Domaini

Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 73-105, leaving each N-terminal inhibitory region (residues 22-51) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 22-51) 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

eggNOGiNOG72683.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiA3KNL5.
OMAiHEDEISH.
OrthoDBiEOG7TQV31.
PhylomeDBiA3KNL5.
TreeFamiTF320659.

Family and domain databases

InterProiIPR007648. ATPase_inhibitor_IATP_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.

A3KNL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLLLRRGF FSSHIRMSSD QLGELGTGAG KGGGGGGSVR AAGGSFGRRE
60 70 80 90 100
AAEEERYFRQ KEREQLAALK NHHEEEIDHH KKEIERLQRE IDRHKGKIRK

LKHDD
Length:105
Mass (Da):11,944
Last modified:April 3, 2007 - v1
Checksum:i851D1A097A16239E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633999 Genomic DNA. No translation available.
CU634003 Genomic DNA. No translation available.
BC133905 mRNA. Translation: AAI33906.1.
RefSeqiNP_001082990.1. NM_001089521.1.
UniGeneiDr.51212.

Genome annotation databases

EnsembliENSDART00000087242; ENSDARP00000081676; ENSDARG00000067975.
GeneIDi100037369.
KEGGidre:100037369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633999 Genomic DNA. No translation available.
CU634003 Genomic DNA. No translation available.
BC133905 mRNA. Translation: AAI33906.1.
RefSeqiNP_001082990.1. NM_001089521.1.
UniGeneiDr.51212.

3D structure databases

ProteinModelPortaliA3KNL5.
SMRiA3KNL5. Positions 43-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000081676.

Proteomic databases

PRIDEiA3KNL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000087242; ENSDARP00000081676; ENSDARG00000067975.
GeneIDi100037369.
KEGGidre:100037369.

Organism-specific databases

CTDi100037369.
ZFINiZDB-GENE-070410-36. atpif1a.

Phylogenomic databases

eggNOGiNOG72683.
GeneTreeiENSGT00390000006264.
HOGENOMiHOG000247022.
HOVERGENiHBG061381.
InParanoidiA3KNL5.
OMAiHEDEISH.
OrthoDBiEOG7TQV31.
PhylomeDBiA3KNL5.
TreeFamiTF320659.

Miscellaneous databases

NextBioi20788532.
PROiA3KNL5.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiATF1A_DANRE
AccessioniPrimary (citable) accession number: A3KNL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: April 3, 2007
Last modified: April 29, 2015
This is version 59 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.