ID   MIC60_SORMK             Reviewed;         684 AA.
AC   D1Z5G1; F7VR83;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=SMAC_01581;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000004; CCC08017.1; -; Genomic_DNA.
DR   RefSeq; XP_003352747.1; XM_003352699.1.
DR   AlphaFoldDB; D1Z5G1; -.
DR   SMR; D1Z5G1; -.
DR   STRING; 771870.D1Z5G1; -.
DR   EnsemblFungi; CCC08017; CCC08017; SMAC_01581.
DR   GeneID; 10810370; -.
DR   KEGG; smp:SMAC_01581; -.
DR   VEuPathDB; FungiDB:SMAC_01581; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   InParanoid; D1Z5G1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000001881; 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; 1.
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..684
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406674"
FT   TOPO_DOM        42..125
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..684
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          62..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          434..464
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        86..102
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  74528 MW;  57FE63D973CB17C8 CRC64;
     MLRTSLRSVR ALGSRPSAAV AGRQWQATVV RRAAVSGQRF FADDKKPVVP EPAQPAVLPA
     SETLTAPSTP PPASPQVEPT STIAPETTPL TPPAPEATVI PPVAEEPVVP PTLPTPRKKK
     GFFRRLRNFL LSLTILGAIA FGGGVYYSRI NDAFHDFFTE YIPYGEQAVL YLEELDFKKR
     FPDVVSRVTG RPRDSGEQVK VPAQSGASWR VADGGEPAGR QSSSIKKAAV AAKDAVTKSE
     PAVVAGANKD TAELPKAEST TTVTPVEPVP VAVAVADPAT AVAPADTAAA AAPAKKPFKA
     PEVDEPSRWP PASPIDPLKV NGATDPIVQD LVHMLNDIIT VINHDNANEK YAPTIGKAKN
     ELSKVAGRIN EMKAKVEAEA SKQVKARVDG FDKAANELVS RVESAMAAQE AAWRREFEEE
     MIRLKKSYDE KIHLIQDRER QIAEEKLNNR LLEQAIQLQR QFTDDIKKHV EEERDGRLGK
     LNELSSAVAD LEKLTSGWNE VVDTNLRTQQ LHVAVEAVRA SLQDAHHPRP FIKELVALKE
     IAAEDPVVDA AISSINPTAY QRGISTSAEL IDRFRRVATE VRKASLLPED AGVASHASSY
     VLSKLMFKKE GLAAGDDVES ILTRTQTYLE EGDLDNAARE INGLQGWAKT LSRDWLGEVR
     KVLEVQQALE VIQTEARLQS LRME