ID   MIC60_LODEL             Reviewed;         578 AA.
AC   A5DSD2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=LELG_00268;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH981524; EDK42090.1; -; Genomic_DNA.
DR   RefSeq; XP_001527748.1; XM_001527698.1.
DR   AlphaFoldDB; A5DSD2; -.
DR   SMR; A5DSD2; -.
DR   STRING; 379508.A5DSD2; -.
DR   EnsemblFungi; EDK42090; EDK42090; LELG_00268.
DR   GeneID; 5235638; -.
DR   KEGG; lel:LELG_00268; -.
DR   VEuPathDB; FungiDB:LELG_00268; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   InParanoid; A5DSD2; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000001996; 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; 2.
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..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..578
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406658"
FT   TOPO_DOM        30..74
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..578
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          174..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          294..392
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   578 AA;  64123 MW;  00E1E33BD2791788 CRC64;
     MLRVVGSSVK LPVVNLTSSR GISAGIVKLN KKVAGPPPVI TVKKDEPLVT PPSIEPIPIT
     EEIVIEEKPK KKFSLFGFLF KSTLLLAAVY GGTLYVATKN DKVMDFVVDN QLPYHEELLD
     VIENTTKEDL EDAWYNLKGK ASNVKLPTKD DIEQMTTKLE HKGEDLLKET KKKFTEATEK
     GRKGTELTPG EQLQRPVEVE SITRNVTRLP LIELSSDVAN SVDSSVRQTI ASLNNFIQSI
     DATPLASSNT ALVKSIDASL NQLAKKLNSL TTSFDEEVKN KLKKSQTELF SAYTKKELDL
     TENLLHQYNA EKAQLEKKLN QRLEQEVKAT RDAVSQAATN AVSMVRIEQT KSFEKLVAEK
     INEERNGRLA NLQKLNDKIT ELEKFAVSFE NLIVKTHERN LIQRSVAALK NALLATPDVD
     ATPKSITPYL ETLAQISTND EVLNLALRDL APLVSQESTH SILTNAQLLS RFEQLAPELR
     SSSLLPPNAG LLGHLSSLVF SKLLLPVKGV KADGKDIESV IARIESSLVR GNLDVAVEEA
     ANLKGWTRRL ANDWVVDARK RLEVEFLLNL IESESRLL