ID   MIC60_COCP7             Reviewed;         671 AA.
AC   C5P436;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=CPC735_063270;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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}.
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DR   EMBL; ACFW01000015; EER28454.1; -; Genomic_DNA.
DR   RefSeq; XP_003070599.1; XM_003070553.1.
DR   AlphaFoldDB; C5P436; -.
DR   SMR; C5P436; -.
DR   EnsemblFungi; EER28454; EER28454; CPC735_063270.
DR   GeneID; 9696094; -.
DR   KEGG; cpw:CPC735_063270; -.
DR   VEuPathDB; FungiDB:CPC735_063270; -.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   Proteomes; UP000009084; 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..671
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406653"
FT   TOPO_DOM        12..141
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..671
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          75..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          342..433
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        104..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..135
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  74398 MW;  D8C5ECA9C1950418 CRC64;
     MIRSSIAPSR QLLSPTTGRQ WLQSSRVRGG LVGKKHYSRT RKAPVISKAI PTLDGVVLPV
     RGNNAFTTSA ILANDSHVRS PPSPSSESAI APEGVPRPPQ SHPVQTSPGS SVDGRAQPPP
     ETNTPPPPPP PAPKKGGRFR RFLIYLIFTT GLAYAGGIWL SLTSDNFHDF FTEYVPYGEE
     AVLYVEEQDF RRRFPNAARQ ITRRVTGPRE EGQNVTIPGK SGLSWKVSEE ESEAKEAGSD
     VSRKGKHMSA TEVNKEKTAA VEQVKAKKEA APAIKKETTP AESKKPALEE ARSPALPTAS
     PVQPLSIAIE DEPTVQELMR IVNDLISVVN ADESSSRFTS TLSKAKADFE KLGERIIAAK
     QESYKFAQEE IEKARADMEK SANELIRRID EVRADDAAQF REEYEAERER LARAYQEKIK
     IELQRVQEVS EQRLRNELVE QAIELNRKFL SDVRSLVENE REGRLSKLSE LTANVGELER
     LTAEWNSVVD TNLTTQQLQV AVDAVRSALE NSDIPRPFIN ELVAVKELAA GDPVVDAAIS
     SISPVAYQRG IPSSAQIIER FRRLATEVRK ASLLPENAGI ASHAASYMMS KVMFKKQGSE
     EGDDVESILT RTETLLEEGR LDDAAREMNS LQGWSKILSK DWLADVRRVL EVNQALELIE
     TEARLRCLQV E