ID   MIC27_CHICK             Reviewed;         272 AA.
AC   Q5ZK55;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
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; ORFNames=RCJMB04_13b18;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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.
CC       {ECO:0000250|UniProtKB:Q6UXV4}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex (also known as MINOS or MitOS
CC       complex). {ECO:0000250|UniProtKB:Q6UXV4}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q6UXV4}; Multi-pass membrane protein
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; AJ720229; CAG31888.1; -; mRNA.
DR   RefSeq; NP_001006434.1; NM_001006434.2.
DR   AlphaFoldDB; Q5ZK55; -.
DR   STRING; 9031.ENSGALP00000011291; -.
DR   PaxDb; Q5ZK55; -.
DR   GeneID; 422271; -.
DR   KEGG; gga:422271; -.
DR   CTD; 139322; -.
DR   VEuPathDB; HostDB:geneid_422271; -.
DR   eggNOG; KOG4798; Eukaryota.
DR   InParanoid; Q5ZK55; -.
DR   OrthoDB; 1605767at2759; -.
DR   PhylomeDB; Q5ZK55; -.
DR   PRO; PR:Q5ZK55; -.
DR   Proteomes; UP000000539; Unplaced.
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..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..272
FT                   /note="MICOS complex subunit MIC27"
FT                   /id="PRO_0000254644"
FT   TOPO_DOM        28..107
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..134
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..272
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          187..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   272 AA;  30135 MW;  97BAE4BE3CDD68CD CRC64;
     MAAKVARLAA AASSLPFVCA VYAEEKESKS QLVKPKQLPI YCLPPLKSKY IEEQPGRLQK
     QFSSIRQTTG RYIGWCKDAF FFAKNGIVDS IQFGKDAYVY LKNPPPDFLP RVGIITISGL
     AGVVLARKDS RFKKIAYPLG LTTLGISVCY PAQAVVIAKI TGKKVISASH QTYEAVRSLW
     TKKEDASKLQ QESKSVTQEN KKNREISNVQ FESAIESRSS NRTESSPIES WSTKDPLPSS
     GTVKTTKFKP DPKLMDHGQS SPEDVDMYST RS