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A3KNL5

- ATF1A_DANRE

UniProt

A3KNL5 - ATF1A_DANRE

Protein

ATPase inhibitor A, mitochondrial

Gene

atpif1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
  1. 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

    1. ATPase binding Source: UniProtKB
    2. ATPase inhibitor activity Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. erythrocyte differentiation Source: UniProtKB
    2. heme biosynthetic process Source: UniProtKB
    3. negative regulation of hydrolase activity Source: UniProtKB
    4. negative regulation of nucleotide metabolic process Source: InterPro
    5. protein homotetramerization Source: UniProtKB

    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: Chromosome 19

    Organism-specific databases

    ZFINiZDB-GENE-070410-36. atpif1a.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    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

    MARLLLRRGF FSSHIRMSSD QLGELGTGAG KGGGGGGSVR AAGGSFGRRE    50
    AAEEERYFRQ KEREQLAALK NHHEEEIDHH KKEIERLQRE IDRHKGKIRK 100
    LKHDD 105
    Length:105
    Mass (Da):11,944
    Last modified:April 3, 2007 - v1
    Checksum:i851D1A097A16239E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU633999 Genomic DNA. No translation available.
    CU634003 Genomic DNA. No translation available.
    BC133905 mRNA. Translation: AAI33906.1 .
    RefSeqi NP_001082990.1. NM_001089521.1.
    UniGenei Dr.51212.

    3D structure databases

    ProteinModelPortali A3KNL5.
    SMRi A3KNL5. Positions 43-105.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000081676.

    Proteomic databases

    PRIDEi A3KNL5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000087242 ; ENSDARP00000081676 ; ENSDARG00000067975 .
    GeneIDi 100037369.
    KEGGi dre:100037369.

    Organism-specific databases

    CTDi 100037369.
    ZFINi ZDB-GENE-070410-36. atpif1a.

    Phylogenomic databases

    eggNOGi NOG72683.
    GeneTreei ENSGT00390000006264.
    HOGENOMi HOG000247022.
    HOVERGENi HBG061381.
    InParanoidi A3KNL5.
    OMAi HEDEISH.
    OrthoDBi EOG7TQV31.
    PhylomeDBi A3KNL5.
    TreeFami TF320659.

    Miscellaneous databases

    NextBioi 20788532.

    Family and domain databases

    InterProi IPR007648. ATPase_inhibitor_IATP_mt.
    [Graphical view ]
    Pfami PF04568. IATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 56 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