ID   MIC60_FUSV7             Reviewed;         633 AA.
AC   C7YIH6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=NECHADRAFT_75325;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(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; GG698896; EEU48806.1; -; Genomic_DNA.
DR   RefSeq; XP_003054519.1; XM_003054473.1.
DR   AlphaFoldDB; C7YIH6; -.
DR   SMR; C7YIH6; -.
DR   STRING; 140110.NechaP75325; -.
DR   EnsemblFungi; NechaT75325; NechaP75325; NechaG75325.
DR   GeneID; 9676440; -.
DR   KEGG; nhe:NECHADRAFT_75325; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   InParanoid; C7YIH6; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000005206; 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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..633
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406660"
FT   TOPO_DOM        42..109
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..633
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          40..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          304..421
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        50..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..100
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  69945 MW;  ABBB0F57D548F4CF CRC64;
     MLRTSLRSVR VLGGRPSVAA AARQWPVAAS RRAALVGQRH YAVDKKPESA SSPSLPNTQS
     VASDKIHETT IDDVGETKAA TVDAPKTTPP PPPPPPAPKK KGFFRRLRNF VFTLFVLGAV
     GFAGGVWYSC FSDNFHDFFT GYVPFGEQAV LYLEEMEYKK RFPNSATNAK SRDADGAVRI
     PAQSGASWRV ADGTRRSSAG PVPAKQEEPK AEAPKPKAAE PKPTAKVVEK PAPTPAPAPT
     PRSESGFKAP EVNEPSRYPP LKPIDLLSLD DAREPVIQDL VHMVNDLILV INADGAHGRY
     GSSVNKAKNE ITKVGGKLKG MKEQFEKKAA GQVRDKIDEF DKAATDLIDR VESAMITQES
     QWRHEFEEEM KKVRENYEDR VKVLLERERK LNEEKLQNQL LEQALALKKE FVKDVENQVE
     QERESRLGKL TALSSAVADL EKLTTGWNEV LDTNLQTQQL HVAVEAVRAS LEDDHHPRPF
     IRELVALREI ASDDPVVNAA IASVNPTAYQ RGISTSSQLI DRFRRVANEV RKASLLPDEA
     GVASHASSWV LSHVMFKKQG LAEGNDVESV LTRTQTYLEE GDLDSAAREM NGLEGWAKTL
     SKDWLGEVRK VLEVQQALDV IATEARLQSL RVD