MIC60_ASPNC
ID MIC60_ASPNC Reviewed; 631 AA.
AC A2QI68;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=MICOS complex subunit mic60;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=mic60; ORFNames=An04g02460;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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; AM270071; CAL00733.1; -; Genomic_DNA.
DR RefSeq; XP_001401614.1; XM_001401577.2.
DR AlphaFoldDB; A2QI68; -.
DR SMR; A2QI68; -.
DR PaxDb; A2QI68; -.
DR EnsemblFungi; CAL00733; CAL00733; An04g02460.
DR GeneID; 4990651; -.
DR KEGG; ang:ANI_1_500184; -.
DR VEuPathDB; FungiDB:An04g02460; -.
DR HOGENOM; CLU_008024_1_2_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..631
FT /note="MICOS complex subunit mic60"
FT /id="PRO_0000406647"
FT TOPO_DOM 48..103
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..631
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 50..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..447
FT /evidence="ECO:0000255"
FT COMPBIAS 70..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70199 MW; AD17AAF4625985C9 CRC64;
MVVRPMMLRS SVAPGRQLLL SSARQRTASQ WLSRAGASSR LSGQRFFADI KPPTTAAPTP
ATPSSESAVP PETVPKPSPA GQESTLPPST PPTPAPKGGR FRRFLLYLLL TSGFAYGGGV
FLALKFDNFH DFFTEYIPYG EESVLYFEER DFYRRFPNTL RNQNRLNPTP RDEGNKITIP
SKSGLTSKVA EEEISGADVS QKGPHMSATP AQKSSEAQTK PAAAKPEDKT TAVVKAKEDK
AAKEAEKKEE PRQPAIPAVT PLEFAQVNEG DEAIVQELVK TFNDMITVIS ADENSGKYSQ
PVAKAKEELQ KVGEKIIAVR EEARRAAQEE IQQAHATFDE SARELIRRFD EMRAADAAQY
REEFEAEREK LAHAYQEKIR TELQRAQEVA EQRLKNELVE QAIELNRKYL HEVKELVERE
REGRLSKLNE LTANVSELEK LTSGWREVID SNLRTQQLQV AVDAVRSVVD RSAVPRPFVR
ELVAVKELAA EDPVVEAAIS SINPAAYQRG IPSTSQIIER FRRVADEVRK ASLLPEDAGI
ASHAASVVLS KVMFKKDAVA GSDDVESVLY RTESLLEEGN LDAAAREMNS LSGWAKILSK
DWLVDVRRVL EVKQALEVIE TEARLQCLRV E
