ID   MIC60_BLAGS             Reviewed;         689 AA.
AC   C5JIS0; A0A179UG41;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Formation of crista junctions protein 1;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; Synonyms=FCJ1; ORFNames=BDBG_02399;
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
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; GG657450; OAT06117.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5JIS0; -.
DR   SMR; C5JIS0; -.
DR   STRING; 559298.C5JIS0; -.
DR   EnsemblFungi; OAT06117; OAT06117; BDBG_02399.
DR   VEuPathDB; FungiDB:BDBG_02399; -.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   Proteomes; UP000002038; 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..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..689
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406641"
FT   TOPO_DOM        56..148
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..689
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          49..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          360..505
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        51..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..142
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  75756 MW;  9EBC8206AF39D965 CRC64;
     MLRTSIASSR QVLSSPICPN PSVQWLHTSR ARRVNAAASR RYYAVARKPN AGVRSSSTPN
     AAATPELSQK ATNSTSTKPP GPNDPDVRSP ASPSTGSTLH PETVSKPPQS PAVQGQTSPG
     SSVQPPEHEP SPPPPRPPPA PKTGLLRKLL YLFLTTGLAY AGGVWYSLRS DNFYDFFTEY
     IPYGEEAVLY LEERDFRSRF PSIARQINRR VSAPRDEGAQ VMIPGRSGLS WKVAEEQQEA
     SDVTKQGQHI SATDANELTE ETKVAEKAKE DVKSKPVAKK AEAAEPKSSP KVVEPHPAKA
     EENTSLEAPR QPVVPAAAAI EHLGLDNEDE PVVQDLVKVF NDIITVISAD ESASKFSVPI
     AKAKEELEKI GDRIVALKND AQESAKEEIR NAQAALDKSA AELVRHINEV RAQDAAEFRE
     EFESEREKIS KSYQEKVTTE LQRAHEVAEQ RLRNELVEQA IELNRKFLAD VKTLVENERE
     GRLSKLAELT ANVAELERLT AGWSDVIDIN LRTQQLQVAV DSVRTTLENS EVPRPFIREL
     AAVKELASND EVVAAAIASI SPTAYQRGIP SPAQLVDRFR RVASEVRKAS LLPENAGITS
     HAASLVLSKV MLKKQGTPVG NDVESILTRT ENLLEEGNFD EAAREMNSLQ GWAKLLSKDW
     LADVRRVLEV KQALEVIETE ARLRCLQVE