ID   MIC60_TRIVH             Reviewed;         683 AA.
AC   D4DHX2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=TRV_06779;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
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; ACYE01000389; EFE38528.1; -; Genomic_DNA.
DR   RefSeq; XP_003019173.1; XM_003019127.1.
DR   AlphaFoldDB; D4DHX2; -.
DR   SMR; D4DHX2; -.
DR   EnsemblFungi; EFE38528; EFE38528; TRV_06779.
DR   GeneID; 9577170; -.
DR   KEGG; tve:TRV_06779; -.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   Proteomes; UP000008383; 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   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..11
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           12..683
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406676"
FT   TOPO_DOM        12..139
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..683
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          61..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          367..444
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        61..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..133
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   683 AA;  74802 MW;  F9FD57BD85FA89AA CRC64;
     MLRNSIAPSR GLGSLARQRL TTSGRNLITK RSYIEGKSAA WPSGRSIASV LPARKTSCAT
     FTTSATRGNE QNIRSPPSPS SASAISPEGI SRPASSSPAG QTSPGSSVNP PEPPKAQTGA
     PPPPPPPPPA PKAKGRFGRS LLYLVLTAGV AYAGGVWFSL RSDNFHDFFT EYVPYGEEAV
     LYFEELDFRR RFPNATRHIN TRPAAPRDEG EKVTIPSKSG VSWKVAENEG TSDVTHKGRH
     MSAVDAEVFR TGGDAKSASN KPTTEDKKGS EKTGSKKDES KERVPVTDTK KSTVSLDEPR
     KPAVATVSSI EPLAALQDDP IIQELTKIVN GLIAVINADE SASKLAAPIA KAKDDFLKLG
     EQISSIKKEA HIAAQEEIKN AHKEFERSAT ELVRRIDEVR SEEAAEYREE FETEREKLAN
     SYQEKIKTEV ERANAVAEQR LRNELVEQAI QLNRKFLSDV DTLVEKERQG RFSKLSELSA
     QVAELEKLTA GWNEVIGANL TTQQLQVAVD AVHSALESES MPRPFINELL AVKSLAGQDP
     IVNAAISSIN PTAYQRGIPS TAQIIDRFRR VANEVRKASL LPEDAGVASH ATSYLMSKVM
     FKKEASSSGD DVESILTRTE KLLEQGNLDD AAREMNALRG WSKLLSKDWL ADVRRVLEVR
     QALEVCFLFL LPTLSLLIYY NEY