ID   MIC60_KLULA             Reviewed;         535 AA.
AC   Q6CSB8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; OrderedLocusNames=KLLA0D02310g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382124; CAH00267.1; -; Genomic_DNA.
DR   RefSeq; XP_453171.1; XM_453171.1.
DR   AlphaFoldDB; Q6CSB8; -.
DR   SMR; Q6CSB8; -.
DR   STRING; 28985.XP_453171.1; -.
DR   EnsemblFungi; CAH00267; CAH00267; KLLA0_D02310g.
DR   GeneID; 2893040; -.
DR   KEGG; kla:KLLA0_D02310g; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   InParanoid; Q6CSB8; -.
DR   OMA; NRWNLLE; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0061617; C:MICOS complex; IEA:EnsemblFungi.
DR   GO; GO:0030061; C:mitochondrial crista; IEA:EnsemblFungi.
DR   GO; GO:0044284; C:mitochondrial crista junction; IEA:EnsemblFungi.
DR   GO; GO:0042407; P:cristae formation; IEA:EnsemblFungi.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   PANTHER; PTHR15415; PTHR15415; 2.
DR   Pfam; PF09731; Mitofilin; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..535
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406656"
FT   TOPO_DOM        13..26
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..535
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          106..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          191..342
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   535 AA;  59391 MW;  4C0FC94D71BA304B CRC64;
     MFRASKALGQ RFASTNVPVK TARPFRNFLW KLGAATTVFY VGGVALSTYN YQFAELFTDN
     VPLAEELVQL VESYNDGTLN APQLSLDEIR KKFGSITRKV QSVPHLGSTS STVTESQSIA
     SGSGSTAAAA TTGTDSNSVV LSSVPPVGSV LLRLPHLKLD DDSNSFNNKS FVESFNKQVD
     SLNEKEFILP ENAVESFLES YHGLSSQLNE LNRDLADQLN SQLGQLSAEL KQSVESDKVK
     EIESNKLQLM QQFEKDLSNL KVEFEQKFDS QLQSSLKANE QAMLAKHKNE LAMLSIKQVQ
     EFNKIISNKI ENERNGRLKN LDELNGSVKT VSDSLAALEE TLLRSECVNQ LTNLVSSIKF
     KLNLDNTPSL DISKDLQKLT TLVNILPGKP NKCDAKEPQL IDVVVNELNS LTSAKENKQI
     LSNEQLLNRW GLLQDKIREA SLLPPNAGFL GHVSAKFFSL FLFNKSGISN ENDIDSVISR
     VTENIKLNRL DKAVEDVVQL QGWSRLEADD WLQAARSKLE LETLVDVVDH EIKTL