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Q6UXV4

- MIC27_HUMAN

UniProt

Q6UXV4 - MIC27_HUMAN

Protein

MICOS complex subunit MIC27

Gene

APOOL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol.1 Publication

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MICOS complex subunit MIC27
    Alternative name(s):
    Apolipoprotein O-like
    Protein FAM121A
    Gene namesi
    Name:APOOL
    Synonyms:CXorf33, FAM121A, MIC27
    ORF Names:UNQ8193/PRO23204
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:24009. APOOL.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162376732.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 268241MICOS complex subunit MIC27PRO_0000042052Add
    BLAST

    Proteomic databases

    MaxQBiQ6UXV4.
    PaxDbiQ6UXV4.
    PRIDEiQ6UXV4.

    PTM databases

    PhosphoSiteiQ6UXV4.

    Expressioni

    Gene expression databases

    BgeeiQ6UXV4.
    CleanExiHS_APOOL.
    GenevestigatoriQ6UXV4.

    Organism-specific databases

    HPAiHPA000612.

    Interactioni

    Subunit structurei

    Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27 and IMMT/MIC60. The complex associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2, and with HSPA9.1 Publication

    Protein-protein interaction databases

    BioGridi126558. 2 interactions.
    DIPiDIP-47309N.
    IntActiQ6UXV4. 1 interaction.
    STRINGi9606.ENSP00000407202.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UXV4.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 11083Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini130 – 1378Mitochondrial matrixSequence Analysis
    Topological domaini156 – 268113Mitochondrial intermembraneSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei111 – 12919HelicalSequence AnalysisAdd
    BLAST
    Transmembranei138 – 15518HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG240513.
    HOGENOMiHOG000034010.
    HOVERGENiHBG055885.
    OMAiNTSEWEE.
    OrthoDBiEOG7CG70V.
    PhylomeDBiQ6UXV4.
    TreeFamiTF315313.

    Family and domain databases

    InterProiIPR019166. Apolipoprotein_O.
    [Graphical view]
    PfamiPF09769. ApoO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q6UXV4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAIRMGKLT TMPAGLIYAS VSVHAAKQEE SKKQLVKPEQ LPIYTAPPLQ    50
    SKYVEEQPGH LQMGFASIRT ATGCYIGWCK GVYVFVKNGI MDTVQFGKDA 100
    YVYLKNPPRD FLPKMGVITV SGLAGLVSAR KGSKFKKITY PLGLATLGAT 150
    VCYPVQSVII AKVTAKKVYA TSQQIFGAVK SLWTKSSKEE SLPKPKEKTK 200
    LGSSSEIEVP AKTTHVLKHS VPLPTELSSE AKTKSESTSG ATQFMPDPKL 250
    MDHGQSHPED IDMYSTRS 268
    Length:268
    Mass (Da):29,159
    Last modified:July 5, 2004 - v1
    Checksum:i2BA4B3AACFBDA298
    GO

    Sequence cautioni

    The sequence CAI42458.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358193 mRNA. Translation: AAQ88560.1.
    Z83820 Genomic DNA. Translation: CAI42458.1. Different initiation.
    BC107096 mRNA. Translation: AAI07097.1.
    CCDSiCCDS48138.1.
    RefSeqiNP_940852.3. NM_198450.5.
    UniGeneiHs.512181.
    Hs.729014.

    Genome annotation databases

    EnsembliENST00000373173; ENSP00000362268; ENSG00000155008.
    GeneIDi139322.
    KEGGihsa:139322.
    UCSCiuc004eem.3. human.

    Polymorphism databases

    DMDMi74749432.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358193 mRNA. Translation: AAQ88560.1 .
    Z83820 Genomic DNA. Translation: CAI42458.1 . Different initiation.
    BC107096 mRNA. Translation: AAI07097.1 .
    CCDSi CCDS48138.1.
    RefSeqi NP_940852.3. NM_198450.5.
    UniGenei Hs.512181.
    Hs.729014.

    3D structure databases

    ProteinModelPortali Q6UXV4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126558. 2 interactions.
    DIPi DIP-47309N.
    IntActi Q6UXV4. 1 interaction.
    STRINGi 9606.ENSP00000407202.

    PTM databases

    PhosphoSitei Q6UXV4.

    Polymorphism databases

    DMDMi 74749432.

    Proteomic databases

    MaxQBi Q6UXV4.
    PaxDbi Q6UXV4.
    PRIDEi Q6UXV4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373173 ; ENSP00000362268 ; ENSG00000155008 .
    GeneIDi 139322.
    KEGGi hsa:139322.
    UCSCi uc004eem.3. human.

    Organism-specific databases

    CTDi 139322.
    GeneCardsi GC0XP084258.
    HGNCi HGNC:24009. APOOL.
    HPAi HPA000612.
    neXtProti NX_Q6UXV4.
    PharmGKBi PA162376732.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240513.
    HOGENOMi HOG000034010.
    HOVERGENi HBG055885.
    OMAi NTSEWEE.
    OrthoDBi EOG7CG70V.
    PhylomeDBi Q6UXV4.
    TreeFami TF315313.

    Miscellaneous databases

    GenomeRNAii 139322.
    NextBioi 83938.
    PROi Q6UXV4.

    Gene expression databases

    Bgeei Q6UXV4.
    CleanExi HS_APOOL.
    Genevestigatori Q6UXV4.

    Family and domain databases

    InterProi IPR019166. Apolipoprotein_O.
    [Graphical view ]
    Pfami PF09769. ApoO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria."
      Weber T.A., Koob S., Heide H., Wittig I., Head B., van der Bliek A., Brandt U., Mittelbronn M., Reichert A.S.
      PLoS ONE 8:E63683-E63683(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT.
    6. Cited for: NOMENCLATURE.

    Entry informationi

    Entry nameiMIC27_HUMAN
    AccessioniPrimary (citable) accession number: Q6UXV4
    Secondary accession number(s): Q3KNU7, Q5H9D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [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

    Miscellaneous

    Overexpression of APOOL results in mitochondrial fragmentation, reduced oxygen consumption, and altered cristae morphology. Down-regulation impairs mitochondrial function and also alters cristae morphology (PubMed:23704930).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3