ID   MIC60_ARTBC             Reviewed;         684 AA.
AC   D4ANR0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=ARB_05877;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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; ABSU01000004; EFE34921.1; -; Genomic_DNA.
DR   RefSeq; XP_003015566.1; XM_003015520.1.
DR   AlphaFoldDB; D4ANR0; -.
DR   SMR; D4ANR0; -.
DR   STRING; 663331.D4ANR0; -.
DR   EnsemblFungi; EFE34921; EFE34921; ARB_05877.
DR   GeneID; 9526252; -.
DR   KEGG; abe:ARB_05877; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   Proteomes; UP000008866; 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..11
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           12..684
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406642"
FT   TOPO_DOM        12..140
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..684
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          61..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          367..445
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        61..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  74743 MW;  BBC59D723D60B263 CRC64;
     MLRNSIAPSR GLGSLARQRL TTSGRNLITK RSYVKGKSAA WPPGRSIASV LPARKTSCAT
     FTTSATRGNE QNIRSPPSPS SASAISPEGI SKPASSSPAG QTSPGSSVNS PEPPKAQTSA
     PPPPPPPPPP APKAKGRFGR SLLYLVLTAG VAYAGGVWFS LRSDNFHDFF TEYVPYGEEA
     VLYFEELDFR RRFPNATRHI NTRPAAPRDE GEKVTIPSKS GVSWKVAENE GTSDVTHKGR
     HMSAVDAEVP RTGGDAKSAP NKPTTEDKKD SEKTGSKKDE SKERVPVTDT KKSTVSLDEP
     RKPAVATVAS IEPLASLQDD PIIQELTKIV NGLIAVINAD ESASKLAAPI AKAKDDFLKL
     GEQISSIKKE AHAAAQEEIK NAHKEFERSA TELVRRIDEV RSEEAAEYRE EFETEREKLA
     NSYQEKIKTE VERANAVAEQ RLRNELVEQA IELNRKFLSD VDTLVEKERQ GRFSKLSELS
     AQVAELEKLT AGWNEVIGAN LTTQQLQVAV DAVHSALESE SMPRPFINEL LAVKSLAGQD
     PIVNAAISSI NPTAYQRGIP STAQIIDRFR RVANEVRKAS LLPEDAGVAS HATSYLMSKV
     MFKKEASSSG DDVESILTRT EKLLEQGNLD DAAREMNALR GWSKLLSKDW LADVRRVLEV
     RQALEVCFLS LLPTLSLLIY YNEC