MIC27_PONAB
ID MIC27_PONAB Reviewed; 266 AA.
AC Q5NVS6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR925925; CAI29587.1; -; mRNA.
DR RefSeq; NP_001127062.1; NM_001133590.1.
DR AlphaFoldDB; Q5NVS6; -.
DR GeneID; 100174091; -.
DR KEGG; pon:100174091; -.
DR CTD; 139322; -.
DR InParanoid; Q5NVS6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0061617; C:MICOS complex; IEA:InterPro.
DR GO; GO:0042407; P:cristae formation; IEA:InterPro.
DR InterPro; IPR019166; MIC26/MIC27.
DR InterPro; IPR033182; MIC26/MIC27_animal.
DR PANTHER; PTHR14564; PTHR14564; 1.
DR Pfam; PF09769; ApoO; 1.
PE 2: Evidence at transcript 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..266
FT /note="MICOS complex subunit MIC27"
FT /id="PRO_0000042053"
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..266
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UXV4"
SQ SEQUENCE 266 AA; 28710 MW; DC7345789053F8A1 CRC64;
MAAIRMGKLT TMPAGLIYAS VSVHAAKEEE SKKQLVKPEQ LPIYTAPPLQ SKYVEEQPGH
LQMGFASIRT ATGCYIGWCK GVYVFVKNGI MDTVQFGKDA YVYMKNPPRD FLPKMGVITV
SGLAGLVSAR KGSKFKKITY PLGLATLGAT VCYPVQSVII AKVTAKKIYA TSQQIFGAVK
SLWTKSSKEE SLPKPKEKTK LGSSSEIEVP AKTTHVLKHS VPLPTELSSE AKTKSESTSD
VQISEVGGKI IGTWGPNVTN SGVLRI