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Protein

MICOS complex subunit MIC27

Gene

APOOL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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. Plays a crucial role in crista junction formation and mitochondrial function (PubMed:23704930), (PubMed:25764979).2 Publications

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:24009. APOOL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 11083Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei111 – 12919HelicalSequence AnalysisAdd
BLAST
Topological domaini130 – 1378Mitochondrial matrixSequence Analysis
Transmembranei138 – 15518HelicalSequence AnalysisAdd
BLAST
Topological domaini156 – 268113Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376732.

Polymorphism and mutation databases

BioMutaiAPOOL.
DMDMi74749432.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6UXV4.
PaxDbiQ6UXV4.
PRIDEiQ6UXV4.

PTM databases

PhosphoSiteiQ6UXV4.

Expressioni

Gene expression databases

BgeeiQ6UXV4.
CleanExiHS_APOOL.
ExpressionAtlasiQ6UXV4. baseline and differential.
GenevisibleiQ6UXV4. HS.

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, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex (PubMed:25764979, PubMed:25781180, PubMed:23704930, PubMed:25764979, PubMed:25781180, PubMed:25997101). The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with MINOS1/MIC10, IMMT/MIC60 and APOO/MIC23/MIC26 (PubMed:25764979, PubMed:25781180, PubMed:23704930, PubMed:25764979, PubMed:25781180, PubMed:25997101).

Protein-protein interaction databases

BioGridi126558. 3 interactions.
DIPiDIP-47309N.
IntActiQ6UXV4. 2 interactions.
STRINGi9606.ENSP00000362268.

Structurei

3D structure databases

ProteinModelPortaliQ6UXV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG240513.
GeneTreeiENSGT00530000063666.
HOGENOMiHOG000034010.
HOVERGENiHBG055885.
InParanoidiQ6UXV4.
OMAiRFKRIAY.
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

        10         20         30         40         50
MAAIRMGKLT TMPAGLIYAS VSVHAAKQEE SKKQLVKPEQ LPIYTAPPLQ
60 70 80 90 100
SKYVEEQPGH LQMGFASIRT ATGCYIGWCK GVYVFVKNGI MDTVQFGKDA
110 120 130 140 150
YVYLKNPPRD FLPKMGVITV SGLAGLVSAR KGSKFKKITY PLGLATLGAT
160 170 180 190 200
VCYPVQSVII AKVTAKKVYA TSQQIFGAVK SLWTKSSKEE SLPKPKEKTK
210 220 230 240 250
LGSSSEIEVP AKTTHVLKHS VPLPTELSSE AKTKSESTSG ATQFMPDPKL
260
MDHGQSHPED IDMYSTRS
Length:268
Mass (Da):29,159
Last modified:July 5, 2004 - v1
Checksum:i2BA4B3AACFBDA298
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358193 mRNA. Translation: AAQ88560.1.
Z83820 Genomic DNA. No translation available.
Z99571 Genomic DNA. No translation available.
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358193 mRNA. Translation: AAQ88560.1.
Z83820 Genomic DNA. No translation available.
Z99571 Genomic DNA. No translation available.
BC107096 mRNA. Translation: AAI07097.1.
CCDSiCCDS48138.1.
RefSeqiNP_940852.3. NM_198450.5.
UniGeneiHs.512181.
Hs.729014.

3D structure databases

ProteinModelPortaliQ6UXV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126558. 3 interactions.
DIPiDIP-47309N.
IntActiQ6UXV4. 2 interactions.
STRINGi9606.ENSP00000362268.

PTM databases

PhosphoSiteiQ6UXV4.

Polymorphism and mutation databases

BioMutaiAPOOL.
DMDMi74749432.

Proteomic databases

MaxQBiQ6UXV4.
PaxDbiQ6UXV4.
PRIDEiQ6UXV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi139322.
GeneCardsiGC0XP084258.
HGNCiHGNC:24009. APOOL.
HPAiHPA000612.
neXtProtiNX_Q6UXV4.
PharmGKBiPA162376732.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG240513.
GeneTreeiENSGT00530000063666.
HOGENOMiHOG000034010.
HOVERGENiHBG055885.
InParanoidiQ6UXV4.
OMAiRFKRIAY.
OrthoDBiEOG7CG70V.
PhylomeDBiQ6UXV4.
TreeFamiTF315313.

Miscellaneous databases

ChiTaRSiAPOOL. human.
GenomeRNAii139322.
NextBioi83938.
PROiQ6UXV4.

Gene expression databases

BgeeiQ6UXV4.
CleanExiHS_APOOL.
ExpressionAtlasiQ6UXV4. baseline and differential.
GenevisibleiQ6UXV4. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION IN THE MICOS COMPLEX.
  6. Cited for: NOMENCLATURE.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The non-glycosylated isoform of MIC26 is a constituent of the mammalian MICOS complex and promotes formation of crista junctions."
    Koob S., Barrera M., Anand R., Reichert A.S.
    Biochim. Biophys. Acta 1853:1551-1563(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MINOS1; APOO AND IMMT.
  9. "QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology."
    Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F., Gygi S.P., Van Vactor D., Harper J.W.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MICOS COMPLEX, SUBCELLULAR LOCATION.
  10. "Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits."
    Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.
    PLoS ONE 10:E0120213-E0120213(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MICOS COMPLEX, SUBCELLULAR LOCATION.

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: July 22, 2015
This is version 93 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

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

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.