ID   MIC60_PENRW             Reviewed;         646 AA.
AC   B6H457;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=MICOS complex subunit mic60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=mic60; ORFNames=Pc13g07690;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(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; AM920428; CAP91838.1; -; Genomic_DNA.
DR   RefSeq; XP_002559198.1; XM_002559152.1.
DR   AlphaFoldDB; B6H457; -.
DR   SMR; B6H457; -.
DR   STRING; 1108849.XP_002559198.1; -.
DR   EnsemblFungi; CAP91838; CAP91838; PCH_Pc13g07690.
DR   GeneID; 8309930; -.
DR   KEGG; pcs:Pc13g07690; -.
DR   VEuPathDB; FungiDB:PCH_Pc13g07690; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   BioCyc; PCHR:PC13G07690-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
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..61
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..646
FT                   /note="MICOS complex subunit mic60"
FT                   /id="PRO_0000406666"
FT   TOPO_DOM        62..115
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..646
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          61..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          317..455
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        74..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  71907 MW;  596EE5CB2B9FDD8C CRC64;
     MLRSSIAPGR QLLSNPVRQR IPSQWLSRAG ASNRLAGQVK RTISPSFLFL YTHNRHAQRF
     FADSKPPTTG GPTPVSPSSE SSVPPETISK AAEQESKLPP SPPAAAPRKS GRFRRFLIYL
     ILTSGFAYGG SIFLALKFDN FHDFFTEYIP YGEESVLYFE ERDFYRRFPN ALRHPNRLPA
     APREEGKPVT IPSKSGLSWK VAEEQKADAD SKKAEAAHEG QIKPAAAKPE ERNAAVVKAK
     EDTASKHSTK EAKPESEAKS PVSLDEPRKP AVSASTIELL QLQDGDDTVV QDLVKTFNDI
     VTVISADENS NKYSAPVAKA KGELEKIAEK IAAIRSEARN TAQEELNKLH ATFDESAREL
     MRQFEEVRST DLASFREEFE AEREKLALAY QQKVNTELRH AQELAEQRLQ NELVEQAIEL
     NRKYVHEVKS LVEREREGRL SKLTELTADV NELEKLTAGW SDVIDANLKT QQLQVALDAV
     RTVVERAETP RPFIRELVAV KELAAGDAVV EAAIASINPT AYQRGIPSTT QIFERFRRVA
     SEVRKASLLP EDAGVASHAA SLVLSKVMFK KDALSEGDDV ESVLVRTENL LQQGDVDAAA
     REMNTLQGWA KILSKDWLGD VRKVLEVRQA LEVIEAEARL QCLRVE