ID   MIC60_PHANO             Reviewed;         621 AA.
AC   Q0V4H8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=SNOG_01086;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445325; EAT92581.2; -; Genomic_DNA.
DR   RefSeq; XP_001791743.1; XM_001791691.1.
DR   AlphaFoldDB; Q0V4H8; -.
DR   SMR; Q0V4H8; -.
DR   STRING; 13684.SNOT_01086; -.
DR   EnsemblFungi; SNOT_01086; SNOT_01086; SNOG_01086.
DR   GeneID; 5967970; -.
DR   KEGG; pno:SNOG_01086; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   InParanoid; Q0V4H8; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0061617; C:MICOS complex; IBA:GO_Central.
DR   GO; GO:0042407; P:cristae formation; IBA:GO_Central.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   PANTHER; PTHR15415; PTHR15415; 2.
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..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..621
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406668"
FT   TOPO_DOM        32..116
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..621
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          34..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          311..388
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        41..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68438 MW;  A9025E520F5C3EA0 CRC64;
     MLRASILRAS PAVRPLARQT RPQWRVVQRC YADNKNLGET AVPNPAPTVT PSSTEKATIP
     SSDIPKPPPA PETAGASRSA PTIQPATTPP TGPGSASIAP DPKQPKPKKK GRIRRLLFWL
     TILSGLGYAG GVWYSLVSDN FHDFFTEYVP YGEDAVAYFE EREFRKRVPW PCWDSPRLQP
     QNLVRRTSSS ILRPQWAEWR VLPTRATATS GTKGPHTIAN VQEKKQEAAQ TATVVKEEAA
     APAPAKPVNH LDHLAVPDAN DAVVQDVVKI VNDIITVINA DSAHDGKYNS ALDKAKSELG
     RVVSDINLMK ANLRKESEEK VKSAHDEFEQ AAKELVQRLD HQMQAQEAHW KEEFENERER
     LSQTYKDRLR SELEAAEKVY EQKTKNELLQ QSIHLQKSFT ASVRERVEAE RDGRLGKLNE
     LSSSVHELEK LTAEWNSVVD ANLKTQHLVV AVEAVKSALE TQATPKPFVT ELAALKEIAA
     DDPVVSAAIA SINPAAYQRG IPSPALLIDR FRRVAAEVRK AALLPEDAGV ASHIASLAMS
     KVLFKKSGLA VGQDVEAVLA RTEVLLEEGD LDAAAREMNG LQGWAKVLSK DWLGECRRVL
     EVRQALDVIA TEARLNSLLV D