ID   MIC60_DEBHA             Reviewed;         578 AA.
AC   Q6BXM9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; OrderedLocusNames=DEHA2B01716g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382134; CAG85026.2; -; Genomic_DNA.
DR   RefSeq; XP_457040.2; XM_457040.1.
DR   AlphaFoldDB; Q6BXM9; -.
DR   SMR; Q6BXM9; -.
DR   STRING; 4959.XP_457040.2; -.
DR   EnsemblFungi; CAG85026; CAG85026; DEHA2B01716g.
DR   GeneID; 2913729; -.
DR   KEGG; dha:DEHA2B01716g; -.
DR   VEuPathDB; FungiDB:DEHA2B01716g; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   InParanoid; Q6BXM9; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..578
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406654"
FT   TOPO_DOM        29..68
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..578
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          169..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          248..317
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   578 AA;  64554 MW;  49E0FA85E9BA0BFC CRC64;
     MIRTSVRRVV VNSNKFDVRS ISNSSIRFNV PNNQRTPPPA VRPPTSPIIV TEGGPKGGSQ
     KQKKKFSFAG FLFKTAFWAS VVYGGTLFVA TKNDKVMDFI MDKQPPYYEE LLNVIEHGSI
     EDLKRQLRDT QHKISNFDFK LPSKAKIDEF THELESRGEN LIEETKRKLG TSTGAKPRQA
     IPEGNSAPTP AEQLQKPVET IHKTVDHLPL IQLDKGIASS VDSSIKSTIK SFNDLILSID
     AGSQSGNESL MREITENVSK LSSKLNKLTS SFDEELSSKL KISQSELLSS YTKKELELTE
     NLLHQFHHEK AQMEKKLGSR LDQEIEATKQ TISQAAVNAV SMMRVEQTKN FEKLIKGKID
     QERDGRLANL DKLNSRITEL ENFSTSLESQ LVANHQKSLI QQSLTKLKSL LLGASSEQEK
     PRLISPYVDN LAKVSHESKD ELIALALQDL QPLLSRESTQ SILSTPQLLT RWEQLVPELR
     SASLLPPNAG LLGHLSSMLF SKLLFPVKGA KPDGKDIESV IGRVESSLAR GELDVAVEEA
     ANLKGWSRKL ADDWVKEGRK KLEIEFLMKI IDAESKIL