ID   MIC60_NEOFI             Reviewed;         624 AA.
AC   A1CXH2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=NFIA_108170;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027685; EAW25324.1; -; Genomic_DNA.
DR   RefSeq; XP_001267221.1; XM_001267220.1.
DR   AlphaFoldDB; A1CXH2; -.
DR   SMR; A1CXH2; -.
DR   STRING; 36630.CADNFIAP00009594; -.
DR   EnsemblFungi; EAW25324; EAW25324; NFIA_108170.
DR   GeneID; 4593322; -.
DR   KEGG; nfi:NFIA_108170; -.
DR   VEuPathDB; FungiDB:NFIA_108170; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000006702; 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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..624
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406661"
FT   TOPO_DOM        42..96
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..624
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          42..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          295..440
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        50..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  69370 MW;  0CA92951A13F9AD2 CRC64;
     MLRSSFTQSR QLLLSPARSR TAAQWLPKAG ASNRLAGQRF FADAKPPVTG APTPASPSSE
     SPIPPESVPK PSPAAEAPPP PPPPPAPARK TGRFRKFLLY LILTSGFAYG GGIFLALKSD
     NFHDFFTEYV PYGEDCVLYF EERDFYRRFP NTLRNQNRAP KDEGHTVTIP SKSGLSWKVA
     DEESGADVSQ KGPHMSALDN GEKAQLKPGA AKPEEKVAAV EKAKAESAAK EQSSDDKKKV
     QEEPKKPAAP AVTPIEFATV SEGDEEVVQE LVKTFNDIIT VIGADENAHK FSGAVNKAKE
     ELRTIGEKII AIRNEARNAA QEEIKQAHAT FDESARELIR RFEEARAHDA AQYREEFEVE
     RERLARAYQE KVNTELQRAQ EVAEQRLKNE LVEQAIELNR KYLHEVKDLV EREREGRLSK
     LNELTANVNL LEKLTTDWKE VIDTNLKTQQ LQVAVDAVRS VLERSTVPRP FVRELVAVKE
     LAAGDPVVEA AIASINPTAY QRGIPSTSQI IERFRRVADE VRKASLLPED AGIASHAASL
     VLSKVMFKKD AVAGSDDVES VLLRTEHLLE EGNLDDAARE MNTLKGWAKI LSKDWLSDVR
     RVLEVKQALE VIETEARLQC LRVE