ID   MIC60_TALSN             Reviewed;         639 AA.
AC   B8MJK3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=TSTA_046570;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(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; EQ962657; EED15203.1; -; Genomic_DNA.
DR   RefSeq; XP_002485156.1; XM_002485111.1.
DR   AlphaFoldDB; B8MJK3; -.
DR   SMR; B8MJK3; -.
DR   STRING; 441959.B8MJK3; -.
DR   EnsemblFungi; EED15203; EED15203; TSTA_046570.
DR   GeneID; 8099568; -.
DR   VEuPathDB; FungiDB:TSTA_046570; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   InParanoid; B8MJK3; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   PhylomeDB; B8MJK3; -.
DR   Proteomes; UP000001745; 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..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..639
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406675"
FT   TOPO_DOM        39..112
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..639
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          34..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          309..447
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        43..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..104
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  70808 MW;  363C6D185688DAA4 CRC64;
     MLRYSVLSSQ TRLLSVSRQR TATQLLASNR ITTGKRYYAD PKNVQPTSPT PVSPESKSVI
     PPETVNSVTT TPTTQVQTSP PSSIQPPQPP VENPSTGSVP PPPPKRKGRF RRFLLYLILT
     SGIAYGGGVF AALKSDNFHD FFTEYVPYGE EAVLYFEERD FYRRFPNATR HSNRLPPIHK
     EESQRVTIPS KSGLSWKVAE EESDSGSLTQ KGPHNSAVSA SKDTTGAKAV TKAKEERAEK
     KAPAKKEAPA PAPQEETRTP AITPPTTLEL VKVEHADEPV VQEVVRIFND IITVISADEG
     AASKYAAPIS RVRTELESIG EKIVSLRAEA QKAAKEEIEK AHALFDESAK KLMQQIETAR
     AAEAAQFREE FEAEREKLSR AYQDKIQTEL ARAQELAEQR LKNELVEQAI ELNRKYLNDV
     KELVERERDG RLSKISELTA NVNQLEKLTT DWSDVIETNL KTQQLQVAVD AVRSVLENAA
     SAKPFVRELV AVKELAADDP VVAAAIASIN PTAYQRGIPT TSQIIDRFRR VAGEVRKASL
     LPEDAGIASH AASFVLSKVM FKRDAVTDGN DVESVLVRTE NLLEEGNLDA AAREMNTLQG
     WAKILSKDWL ADVRRVLEVK QALEVMETEA RLQCLRVES