ID   MIC60_AJEDR             Reviewed;         653 AA.
AC   C5GFG7;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=BDCG_03160;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999975; EEQ88040.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GFG7; -.
DR   SMR; C5GFG7; -.
DR   STRING; 559297.C5GFG7; -.
DR   EnsemblFungi; EEQ88040; EEQ88040; BDCG_03160.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   Proteomes; UP000002039; 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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..653
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406640"
FT   TOPO_DOM        20..112
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..653
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          9..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          324..469
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..106
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  71826 MW;  A1F90C2E7CAF4929 CRC64;
     MQVVRYYAVA RKPNAGVRSS STPNAAATPE LSQKATNSTS TKPPGPNDPD VRSPASPSTG
     STLHPETVSK PPQSPAVQGQ TSPGSSVQPP EHEPSPPPPR PPPAPKTGLL RKLLYLFLTT
     GLAYAGGVWY SLRSDNFYDF FTEYIPYGEE AVLYLEERDF RSRFPSIARQ INRRVSAPRD
     EGAQVMIPGR SGLSWKVAEE QQEASDVTKQ GQHISATDAN ELTEETKVAE KAKEDVKSKP
     VAKKAEAAEP KSSPKVVEPH PAKAEENTSL EAPRQPVVPA AAAIEHLGLD NEDEPVVQDL
     VKVFNDIITV ISADESASKF SVPIAKAKEE LEKIGDRIVA LKNDAQESAK EEIRNAQAAL
     DKSAAELVRH INEVRAQDAA EFREEFESER EKISKSYQEK VTTELQRAHE VAEQRLRNEL
     VEQAIELNRK FLADVKTLVE NEREGRLSKL AELTANVAEL ERLTAGWSDV IDINLRTQQL
     QVAVDSVRTT LENSEVPRPF IRELAAVKEL ASNDEVVAAA IASISPTAYQ RGIPSPAQLV
     DRFRRVASEV RKASLLPENA GITSHAASLV LSKVMLKKQG TPVGNDVESI LTRTENLLEE
     GNFDEAAREM NSLQGWAKLL SKDWLADVRR VLEVKQALEV IETEARLRCL QVE