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A3KNL5 (ATF1A_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:atpif1
Synonyms:atpia, atpif1a, pnt
ORF Names:Zgc:162207
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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.

Subcellular location

Mitochondrion By similarity.

Domain

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.

Disruption phenotype

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. Ref.3

Sequence similarities

Belongs to the ATPase inhibitor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 105ATPase inhibitor A, mitochondrialPRO_0000421768

Regions

Region22 – 5130N-terminal inhibitory region By similarity
Region73 – 10533Antiparallel alpha-helical coiled coil region By similarity
Coiled coil58 – 10548 Potential

Sequences

Sequence LengthMass (Da)Tools
A3KNL5 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 851D1A097A16239E

FASTA10511,944
        10         20         30         40         50         60 
MARLLLRRGF FSSHIRMSSD QLGELGTGAG KGGGGGGSVR AAGGSFGRRE AAEEERYFRQ 

        70         80         90        100 
KEREQLAALK NHHEEEIDHH KKEIERLQRE IDRHKGKIRK LKHDD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Mitochondrial Atpif1 regulates haem synthesis in developing erythroblasts."
Shah D.I., Takahashi-Makise N., Cooney J.D., Li L., Schultz I.J., Pierce E.L., Narla A., Seguin A., Hattangadi S.M., Medlock A.E., Langer N.B., Dailey T.A., Hurst S.N., Faccenda D., Wiwczar J.M., Heggers S.K., Vogin G., Chen W. expand/collapse author list , Chen C., Campagna D.R., Brugnara C., Zhou Y., Ebert B.L., Danial N.N., Fleming M.D., Ward D.M., Campanella M., Dailey H.A., Kaplan J., Paw B.H.
Nature 491:608-612(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633999 Genomic DNA. No translation available.
CU634003 Genomic DNA. No translation available.
BC133905 mRNA. Translation: AAI33906.1.
RefSeqNP_001082990.1. NM_001089521.1.
UniGeneDr.51212.

3D structure databases

ProteinModelPortalA3KNL5.
SMRA3KNL5. Positions 43-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000081676.

Proteomic databases

PRIDEA3KNL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000087242; ENSDARP00000081676; ENSDARG00000067975.
GeneID100037369.
KEGGdre:100037369.

Organism-specific databases

CTD100037369.
ZFINZDB-GENE-070410-36. atpif1a.

Phylogenomic databases

eggNOGNOG72683.
GeneTreeENSGT00390000006264.
HOGENOMHOG000247022.
HOVERGENHBG061381.
InParanoidA3KNL5.
OMAHEDEISH.
OrthoDBEOG7TQV31.
PhylomeDBA3KNL5.
TreeFamTF320659.

Family and domain databases

InterProIPR007648. ATPase_inhibitor_IATP_mt.
[Graphical view]
PfamPF04568. IATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20788532.

Entry information

Entry nameATF1A_DANRE
AccessionPrimary (citable) accession number: A3KNL5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families