ID   MIC27_BOVIN             Reviewed;         264 AA.
AC   Q3SZ27;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=MICOS complex subunit MIC27;
DE   AltName: Full=Apolipoprotein O-like;
DE   AltName: Full=Protein FAM121A;
DE   Flags: Precursor;
GN   Name=APOL; Synonyms=FAM121A, MIC27;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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 QIL1/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; BC103214; AAI03215.1; -; mRNA.
DR   RefSeq; NP_001030203.1; NM_001035031.1.
DR   AlphaFoldDB; Q3SZ27; -.
DR   STRING; 9913.ENSBTAP00000029044; -.
DR   PaxDb; Q3SZ27; -.
DR   PRIDE; Q3SZ27; -.
DR   Ensembl; ENSBTAT00000029044; ENSBTAP00000029044; ENSBTAG00000021790.
DR   GeneID; 506138; -.
DR   KEGG; bta:506138; -.
DR   CTD; 139322; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021790; -.
DR   VGNC; VGNC:26036; APOOL.
DR   eggNOG; KOG4798; Eukaryota.
DR   GeneTree; ENSGT00530000063666; -.
DR   HOGENOM; CLU_048383_0_0_1; -.
DR   InParanoid; Q3SZ27; -.
DR   OMA; EDMYSTR; -.
DR   OrthoDB; 1605767at2759; -.
DR   TreeFam; TF315313; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000021790; Expressed in tongue muscle and 105 other tissues.
DR   ExpressionAtlas; Q3SZ27; baseline and differential.
DR   GO; GO:0061617; C:MICOS complex; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..264
FT                   /note="MICOS complex subunit MIC27"
FT                   /id="PRO_0000254643"
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..264
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          189..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  29115 MW;  FFEBB65A2EF829CB CRC64;
     MAALRMGKLT TMPTGLIYAS ISVHVAKEEE SKKQLVKPEQ LPIYTAPPLQ SKYVEEQPGH
     LQMGFASIRT TTSRYIGWCK GVYVFVKNGI MDTVQFGKDA YVYLKNPPRD FLPKIGVITV
     SGLAGFISAR KGSRFKRIAY PLGLATLGAT VCYPVQSVII AKVAGKKAYA TSQQMYEAVK
     SLWTKNNKKL PEHKEKTKLG SADETETPAE TTHNLKHSVP LPAELSSETK TKSTSGATQF
     MPDPKLMDHG QSHPEDIDMY STRS