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Q6UXV4

- APOOL_HUMAN

UniProt

Q6UXV4 - APOOL_HUMAN

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Protein
Apolipoprotein O-like
Gene
APOOL, CXorf33, FAM121A, UNQ8193/PRO23204
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the maintenance of mitochondrial cristae morphology. Specifically binds to cardiolipin (in vitro) but not to the precursor lipid phosphatidylglycerol.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein O-like
Alternative name(s):
Protein FAM121A
Gene namesi
Name:APOOL
Synonyms:CXorf33, FAM121A
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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 11083Mitochondrial intermembrane Reviewed prediction
Add
BLAST
Transmembranei111 – 12919Helical; Reviewed prediction
Add
BLAST
Topological domaini130 – 1378Mitochondrial matrix Reviewed prediction
Transmembranei138 – 15518Helical; Reviewed prediction
Add
BLAST
Topological domaini156 – 268113Mitochondrial intermembrane Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 – 2727Mitochondrion Reviewed prediction
Add
BLAST
Chaini28 – 268241Apolipoprotein O-like
PRO_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

Interacts with several subunits of the MINOS/MitOS complex, namely IMMT/Mitofilin, MINOS1, and SAMM50.1 Publication

Protein-protein interaction databases

BioGridi126558. 2 interactions.
DIPiDIP-47309N.
STRINGi9606.ENSP00000407202.

Structurei

3D structure databases

ProteinModelPortaliQ6UXV4.

Family & Domainsi

Sequence similaritiesi

Belongs to the apolipoprotein O family.

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.
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

« 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, SUBUNIT, MISCELLANEOUS.

Entry informationi

Entry nameiAPOOL_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 9, 2014
This is version 84 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.

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

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