MIC27_HUMAN
ID MIC27_HUMAN Reviewed; 268 AA.
AC Q6UXV4; Q3KNU7; Q5H9D1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=MICOS complex subunit MIC27;
DE AltName: Full=Apolipoprotein O-like;
DE AltName: Full=Protein FAM121A;
DE Flags: Precursor;
GN Name=APOOL; Synonyms=CXorf33, FAM121A, MIC27; ORFNames=UNQ8193/PRO23204;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND IDENTIFICATION IN THE MICOS
RP COMPLEX.
RX PubMed=23704930; DOI=10.1371/journal.pone.0063683;
RA Weber T.A., Koob S., Heide H., Wittig I., Head B., van der Bliek A.,
RA Brandt U., Mittelbronn M., Reichert A.S.;
RT "APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein
RT complex determining cristae morphology in mammalian mitochondria.";
RL PLoS ONE 8:E63683-E63683(2013).
RN [6]
RP NOMENCLATURE.
RX PubMed=24687277; DOI=10.1083/jcb.201401006;
RA Pfanner N., van der Laan M., Amati P., Capaldi R.A., Caudy A.A.,
RA Chacinska A., Darshi M., Deckers M., Hoppins S., Icho T., Jakobs S., Ji J.,
RA Kozjak-Pavlovic V., Meisinger C., Odgren P.R., Park S.K., Rehling P.,
RA Reichert A.S., Sheikh M.S., Taylor S.S., Tsuchida N., van der Bliek A.M.,
RA van der Klei I.J., Weissman J.S., Westermann B., Zha J., Neupert W.,
RA Nunnari J.;
RT "Uniform nomenclature for the mitochondrial contact site and cristae
RT organizing system.";
RL J. Cell Biol. 204:1083-1086(2014).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MICOS10; APOO AND
RP IMMT.
RX PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
RA Koob S., Barrera M., Anand R., Reichert A.S.;
RT "The non-glycosylated isoform of MIC26 is a constituent of the mammalian
RT MICOS complex and promotes formation of crista junctions.";
RL Biochim. Biophys. Acta 1853:1551-1563(2015).
RN [9]
RP IDENTIFICATION IN THE MICOS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [10]
RP IDENTIFICATION IN THE MICOS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25781180; DOI=10.1371/journal.pone.0120213;
RA Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.;
RT "Detailed analysis of the human mitochondrial contact site complex indicate
RT a hierarchy of subunits.";
RL PLoS ONE 10:E0120213-E0120213(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC the mitochondrial inner membrane that plays crucial roles in the
CC maintenance of crista junctions, inner membrane architecture, and
CC formation of contact sites to the outer membrane. Specifically binds to
CC cardiolipin (in vitro) but not to the precursor lipid
CC phosphatidylglycerol. Plays a crucial role in crista junction formation
CC and mitochondrial function (PubMed:23704930), (PubMed:25764979).
CC {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and MICOS13/MIC13. This complex was also known under the names MINOS or
CC MitOS complex (PubMed:25764979, PubMed:25781180, PubMed:23704930,
CC PubMed:25764979, PubMed:25781180, PubMed:25997101).The MICOS complex
CC associates with mitochondrial outer membrane proteins SAMM50, MTX1 and
CC MTX2 (together described as components of the mitochondrial outer
CC membrane sorting assembly machinery (SAM) complex) and DNAJC11,
CC mitochondrial inner membrane protein TMEM11 and with HSPA9. The MICOS
CC and SAM complexes together with DNAJC11 are part of a large protein
CC complex spanning both membranes termed the mitochondrial intermembrane
CC space bridging (MIB) complex. Interacts with MICOS10/MIC10, IMMT/MIC60
CC and APOO/MIC23/MIC26 (PubMed:25764979, PubMed:25781180,
CC PubMed:23704930, PubMed:25764979, PubMed:25781180, PubMed:25997101).
CC {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979,
CC ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:23704930, ECO:0000269|PubMed:25764979}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:23704930}. Mitochondrion
CC {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.
CC -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC family. {ECO:0000305}.
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DR EMBL; AY358193; AAQ88560.1; -; mRNA.
DR EMBL; Z83820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107096; AAI07097.1; -; mRNA.
DR CCDS; CCDS48138.1; -.
DR RefSeq; NP_940852.3; NM_198450.5.
DR AlphaFoldDB; Q6UXV4; -.
DR BioGRID; 126558; 87.
DR ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex.
DR CORUM; Q6UXV4; -.
DR DIP; DIP-47309N; -.
DR IntAct; Q6UXV4; 46.
DR MINT; Q6UXV4; -.
DR STRING; 9606.ENSP00000362268; -.
DR iPTMnet; Q6UXV4; -.
DR MetOSite; Q6UXV4; -.
DR PhosphoSitePlus; Q6UXV4; -.
DR BioMuta; APOOL; -.
DR DMDM; 74749432; -.
DR EPD; Q6UXV4; -.
DR jPOST; Q6UXV4; -.
DR MassIVE; Q6UXV4; -.
DR MaxQB; Q6UXV4; -.
DR PaxDb; Q6UXV4; -.
DR PeptideAtlas; Q6UXV4; -.
DR PRIDE; Q6UXV4; -.
DR ProteomicsDB; 67669; -.
DR TopDownProteomics; Q6UXV4; -.
DR Antibodypedia; 390; 142 antibodies from 24 providers.
DR DNASU; 139322; -.
DR Ensembl; ENST00000373173.7; ENSP00000362268.2; ENSG00000155008.16.
DR GeneID; 139322; -.
DR KEGG; hsa:139322; -.
DR MANE-Select; ENST00000373173.7; ENSP00000362268.2; NM_198450.6; NP_940852.3.
DR UCSC; uc004eem.4; human.
DR CTD; 139322; -.
DR GeneCards; APOOL; -.
DR HGNC; HGNC:24009; APOOL.
DR HPA; ENSG00000155008; Low tissue specificity.
DR MIM; 300955; gene.
DR neXtProt; NX_Q6UXV4; -.
DR OpenTargets; ENSG00000155008; -.
DR PharmGKB; PA162376732; -.
DR VEuPathDB; HostDB:ENSG00000155008; -.
DR eggNOG; KOG4798; Eukaryota.
DR GeneTree; ENSGT00530000063666; -.
DR HOGENOM; CLU_048383_0_0_1; -.
DR InParanoid; Q6UXV4; -.
DR OrthoDB; 1605767at2759; -.
DR PhylomeDB; Q6UXV4; -.
DR TreeFam; TF315313; -.
DR PathwayCommons; Q6UXV4; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q6UXV4; -.
DR BioGRID-ORCS; 139322; 27 hits in 701 CRISPR screens.
DR ChiTaRS; APOOL; human.
DR GenomeRNAi; 139322; -.
DR Pharos; Q6UXV4; Tbio.
DR PRO; PR:Q6UXV4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6UXV4; protein.
DR Bgee; ENSG00000155008; Expressed in skeletal muscle tissue of biceps brachii and 202 other tissues.
DR ExpressionAtlas; Q6UXV4; baseline and differential.
DR Genevisible; Q6UXV4; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0061617; C:MICOS complex; IDA:UniProtKB.
DR GO; GO:0044284; C:mitochondrial crista junction; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IBA:GO_Central.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR InterPro; IPR019166; MIC26/MIC27.
DR InterPro; IPR033182; MIC26/MIC27_animal.
DR PANTHER; PTHR14564; PTHR14564; 1.
DR Pfam; PF09769; ApoO; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..268
FT /note="MICOS complex subunit MIC27"
FT /id="PRO_0000042052"
FT TOPO_DOM 28..110
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..137
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..268
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 187..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 268 AA; 29159 MW; 2BA4B3AACFBDA298 CRC64;
MAAIRMGKLT TMPAGLIYAS VSVHAAKQEE SKKQLVKPEQ LPIYTAPPLQ SKYVEEQPGH
LQMGFASIRT ATGCYIGWCK GVYVFVKNGI MDTVQFGKDA YVYLKNPPRD FLPKMGVITV
SGLAGLVSAR KGSKFKKITY PLGLATLGAT VCYPVQSVII AKVTAKKVYA TSQQIFGAVK
SLWTKSSKEE SLPKPKEKTK LGSSSEIEVP AKTTHVLKHS VPLPTELSSE AKTKSESTSG
ATQFMPDPKL MDHGQSHPED IDMYSTRS
