MIC27_MOUSE
ID MIC27_MOUSE Reviewed; 265 AA.
AC Q78IK4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Fam121a, Mic27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250|UniProtKB:Q6UXV4}.
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. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC components of the mitochondrial outer membrane sorting assembly
CC machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC with DNAJC11 are part of a large protein complex spanning both
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex. Interacts with MICOS10/MIC10, IMMT/MIC60 and APOO/MIC23/MIC26.
CC {ECO:0000250|UniProtKB:Q6UXV4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q6UXV4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6UXV4}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q6UXV4}.
CC -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC family. {ECO:0000305}.
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DR EMBL; BC024334; AAH24334.1; -; mRNA.
DR CCDS; CCDS30359.1; -.
DR RefSeq; NP_080841.1; NM_026565.3.
DR AlphaFoldDB; Q78IK4; -.
DR BioGRID; 212664; 3.
DR IntAct; Q78IK4; 4.
DR STRING; 10090.ENSMUSP00000026599; -.
DR iPTMnet; Q78IK4; -.
DR PhosphoSitePlus; Q78IK4; -.
DR SwissPalm; Q78IK4; -.
DR EPD; Q78IK4; -.
DR jPOST; Q78IK4; -.
DR MaxQB; Q78IK4; -.
DR PaxDb; Q78IK4; -.
DR PeptideAtlas; Q78IK4; -.
DR PRIDE; Q78IK4; -.
DR ProteomicsDB; 252554; -.
DR Antibodypedia; 390; 142 antibodies from 24 providers.
DR DNASU; 68117; -.
DR Ensembl; ENSMUST00000026599; ENSMUSP00000026599; ENSMUSG00000025525.
DR GeneID; 68117; -.
DR KEGG; mmu:68117; -.
DR UCSC; uc009udh.1; mouse.
DR CTD; 139322; -.
DR MGI; MGI:1915367; Apool.
DR VEuPathDB; HostDB:ENSMUSG00000025525; -.
DR eggNOG; KOG4798; Eukaryota.
DR GeneTree; ENSGT00530000063666; -.
DR InParanoid; Q78IK4; -.
DR OMA; EDMYSTR; -.
DR OrthoDB; 1605767at2759; -.
DR PhylomeDB; Q78IK4; -.
DR TreeFam; TF315313; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 68117; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q78IK4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q78IK4; protein.
DR Bgee; ENSMUSG00000025525; Expressed in interventricular septum and 211 other tissues.
DR ExpressionAtlas; Q78IK4; baseline and differential.
DR Genevisible; Q78IK4; MM.
DR GO; GO:0061617; C:MICOS complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042407; P:cristae formation; IBA:GO_Central.
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..265
FT /note="MICOS complex subunit Mic27"
FT /id="PRO_0000042054"
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..265
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UXV4"
SQ SEQUENCE 265 AA; 29261 MW; 3DBAFD5D0AA3DC78 CRC64;
MAAFRMGKLT TIPAGLIYAS INVRLAKEEE PKKQLVRPDQ LPIYTAPPLH SKYVEEQPGN
LQRGFASIRT TTVYYIGWCK SIYLFMKNGV MDTVQFGKDA YVYLKNPPQD FLPKMGVITA
SGLAGLLSAR KGSRFKKIAY PLGLATLGAT VCYPAQSVII AKITGKKAYA TSQQIFQAIK
SLWTQKSENE SLPEPKEESK EGRSDEIHAS LPDLKHSVSL PKELASATVI KSESTSGTTQ
FIPDPKLMDH GQSHPDDKDM YSTRS
