ID   MIC60_YEAS6             Reviewed;         539 AA.
AC   B5VMG3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=AWRI1631_112380;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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; ABSV01001492; EDZ70881.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VMG3; -.
DR   SMR; B5VMG3; -.
DR   Proteomes; UP000008988; 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; 2.
DR   Pfam; PF09731; Mitofilin; 3.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..539
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406681"
FT   TOPO_DOM        17..36
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..539
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   COILED          172..267
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   539 AA;  61063 MW;  BAFB92C0D0955FAE CRC64;
     MLRTTASRKI VLRRGLASIN TGTTVASKKA SHKFRNTFWT IALSATAFYA GGIIYSQKND
     KFGDFFSNNV PFAEDLLETY EHYHDRPTLF LEDSWDGLKA KSNDLLSGLT GSSQTRRSNR
     ENIEVKKILS LEPLNIETEN SDPQLKEIIG SLNDLINSLN DSNLSIPESE FNSIKKSNQN
     MLTNLSQLNE TLKEALSNYM IQRTSEVITE LNTQYENSKR EFEKNLQKNL LQEVDEFKEN
     LTKQKDKELE EKLKANEELL QAKHANEVGL LSITQVKEFN KIIKDKIEKE RNGRLAHLEE
     INSEVNDLSK SIDRSSKILS KNEALVQLTF QVDEIKSRIN NNNLPDVNID KELSRLKLLS
     NLLSTFNKKS CCDDGDCCSC KKGNKNEGKE GKISCKCKPK TNPPSLLSVV YDELESTCSG
     KKILSNEQIY NRWNLLADDF KTASLLPPNS GILGQLTAKV FSLFLFTKTG NPSNATDFDS
     VYARVGDNLR VSNLNDAVEE VVSLKGWPHK VCESWIEDAR RKLEVQRLVE ILDCEIRTL