ID   MIC60_ARTOC             Reviewed;         671 AA.
AC   C5FGB1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=MCYG_02615;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995702; EEQ29796.1; -; Genomic_DNA.
DR   RefSeq; XP_002849681.1; XM_002849635.1.
DR   AlphaFoldDB; C5FGB1; -.
DR   SMR; C5FGB1; -.
DR   STRING; 63405.XP_002849681.1; -.
DR   EnsemblFungi; EEQ29796; EEQ29796; MCYG_02615.
DR   GeneID; 9222731; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
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; 1.
DR   Pfam; PF09731; Mitofilin; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..671
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406659"
FT   TOPO_DOM        39..150
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        172..671
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          360..455
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        70..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..143
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  73463 MW;  B182772108E6D125 CRC64;
     MLRNSIAPSR GLGSLARQRA AGPWLTTSRR SLLGKRGYSK ARSAGWPYES SIRPGTAVLP
     TRKTSCATFT SSATLRENEP NVRSPPSPSS ASAITPEGVS KPPPSSPAAQ GLTSPGSSVN
     PPEPPKTQTG APPPPPPPPP ARKAKGKFTR FLLYLVLTTG VAYAGGVWFS LKSDNFHDFF
     TEYVPYGEEA VLYLEELDFR RRFPNATRHI NTRPAAPRDE GEKVTIPSKS GVSWKVAEKE
     GGSDVSQKGR HMSALDAETS RTTDKSKSAP KRPASEDKVV SETTGTKKDK SNERVPVTDT
     KKPAVSLDEP RKPAVPTVSS IEPLAALQDD ATIQELTKIV NGLITVINAD ESASKLAAPL
     TKAKEDFLKL GEQISRIKEE ALAAAKEEIN NAHLEFDRSA TELVRRIDEV RAEEAAQYRE
     EFEMEREKLA HSYQEKIKTE IERANAVAEQ RLRNELVEQA IEMNRKFLND VETLVEKERG
     GRLSKLSELT AQVAELEKLT AGWNEVIGAN LTTQQLQVAV DAVHTALESD SMPRPFINEL
     LAVKGLAGQD PIVNAAISSI NPTAYQRGIP STSQIIDRFR RVANEVRKAS LLPEDAGVAS
     HATSYLMSKV MFKKEVSSSG DDVESILTRT EKLLEEGNLD EAAREMNALR GWSKLLSKDW
     LADQWMLTQA L