ID   MIC60_CANDC             Reviewed;         564 AA.
AC   B9WLF1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=CD36_28660;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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. Plays a role in
CC       keeping cristae membranes connected to the inner boundary membrane.
CC       Also promotes protein import via the mitochondrial intermembrane space
CC       assembly (MIA) pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC       {ECO:0000305}.
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DR   EMBL; FM992695; CAX39912.1; -; Genomic_DNA.
DR   RefSeq; XP_002421912.1; XM_002421867.1.
DR   AlphaFoldDB; B9WLF1; -.
DR   SMR; B9WLF1; -.
DR   STRING; 42374.XP_002421912.1; -.
DR   EnsemblFungi; CAX39912; CAX39912; CD36_28660.
DR   GeneID; 8050225; -.
DR   KEGG; cdu:CD36_28660; -.
DR   CGD; CAL0000169710; Cd36_28660.
DR   VEuPathDB; FungiDB:CD36_28660; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000002605; Chromosome R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   PANTHER; PTHR15415; PTHR15415; 2.
DR   Pfam; PF09731; Mitofilin; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..564
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406650"
FT   TOPO_DOM        18..61
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..564
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          27..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          281..380
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..55
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  62720 MW;  B540DF636A7F4533 CRC64;
     MIRITSRSVK GAVNIRSVST STVRFNNAPK VVSPPVPPTV KPQGSEIPPP PPPPPKTKKF
     SLFGFLFKTT LLATVVYGGT LYAATKNDKV MDFVIDKQLP FHEELIDFIE NGSTEDLEEA
     WENLKSKFTN VKLPTKDDID ELTQKLEHRG EDIIKETKKK IASTHIGHKS GTDLTPAEQL
     QRGVEIESVK KDFAHLPLIE LNSDLGKSVD DTVKQTITSF NNFIQSIDAS SLANKDDKLV
     ASVNTSVNQL ASRLNSLTKD FDNELQKKLK VSQTELFSSF TRKELELTEN LLHQFSTEKQ
     QLESKLNQKL NQEIQAARAA ISQAASNAVA MVRIEQTKNF EKLVSEKLNE ERTGRLANLE
     KLNDRIIELE KFAEGFETQI VSNHKKAIIH QTVSKLKSLL LAPTAGDKPQ PIKPYLDELT
     KIASDDEVLK LAIKDLSPLV TNESTHSILT NAQLLSRWEQ LAPELRSASL LPPNAGLLGH
     LASIVFSKLL LPVKGIKEDG KDIESVIGRV ESSLARGELD IAVEEAANLK GWSRKLANDW
     VVEGRKRLEI EFLLGLIESE SRII