ID   MIC60_PARBA             Reviewed;         685 AA.
AC   C1GYK6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=PAAG_03160;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293999; EEH41597.1; -; Genomic_DNA.
DR   RefSeq; XP_002794615.1; XM_002794569.2.
DR   AlphaFoldDB; C1GYK6; -.
DR   STRING; 502779.C1GYK6; -.
DR   EnsemblFungi; EEH41597; EEH41597; PAAG_03160.
DR   GeneID; 9097969; -.
DR   KEGG; pbl:PAAG_03160; -.
DR   VEuPathDB; FungiDB:PAAG_03160; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..685
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406663"
FT   TOPO_DOM        43..149
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..685
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          47..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          356..379
FT                   /evidence="ECO:0000255"
FT   COILED          405..451
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        47..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..143
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  75036 MW;  D6B093CCD0F6090D CRC64;
     MLRTSIATSR QVLSSPVCPK ASAQWLRSSS AGRANTTTRR HYAILQEPNG ALRSSSSPSV
     AAVSDVSQRA SNSTNTKRPN TSDLNLRSAA SPSTGSTLKP ETVLVAPVSP PRQGQTSPGS
     AASAPEPTAA PPPSPPPTPP TPKTGRLRRF LLYLFLTTGL AYAGGVWYSL RSDNFYDFFT
     EYAPYGEDAV LYLEERDFRN RFPNATKKNN RRAVTPIDGG AQVTIPGGSG LSWKVAEEQQ
     EGSDISKKGP HMSAVDKNKA TKDTKRVEKT KGGVTSKSPA QREEAVKTKP ATEGVKTQPA
     KVEETPREPA IPAVTTIDHL VLNTEDEPVV QDLLKVFNDI ITVISADAPS SFSGPVAKAK
     EELEKIGKRI LALKSDAQAS AQKEINDAHA SFDKSAAKLI RRIDEMRAED ATKFREEFEA
     ERERIAQSYQ EKINTELQRV HEVAEQRLRN ELVEQAIELN RKFLSDVKNL VEHERESRLS
     KLAELVSSVA ELERLTAGWS DVIDINLKTQ QLQVAVDAVR TTLENSNVPR PFIRELAAVK
     KLASNDEVVS AAIDSISPVA YQRGIPSSAQ LVDRFRRVAS EVRKASLLPE NAGITSHAAS
     FVLSKVMLKK HGSPAGNDVE STLTRAENFL EEGNLDEAAR EMNSLKGWAK LLSKDWLADV
     RRVLEVKQAL EVIETEARLR CLQVE