MIC60_EMENI
ID MIC60_EMENI Reviewed; 618 AA.
AC Q5B6I7; C8V6J0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, 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; ORFNames=AN3843;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(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; AACD01000062; EAA59108.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75260.1; -; Genomic_DNA.
DR RefSeq; XP_661447.1; XM_656355.1.
DR AlphaFoldDB; Q5B6I7; -.
DR SMR; Q5B6I7; -.
DR STRING; 162425.CADANIAP00004863; -.
DR EnsemblFungi; CBF75260; CBF75260; ANIA_03843.
DR EnsemblFungi; EAA59108; EAA59108; AN3843.2.
DR GeneID; 2873261; -.
DR KEGG; ani:AN3843.2; -.
DR VEuPathDB; FungiDB:AN3843; -.
DR eggNOG; KOG1854; Eukaryota.
DR HOGENOM; CLU_008024_1_2_1; -.
DR InParanoid; Q5B6I7; -.
DR OMA; LQGWAKV; -.
DR OrthoDB; 1540241at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; 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; 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..618
FT /note="MICOS complex subunit mic60"
FT /id="PRO_0000406655"
FT TOPO_DOM 42..89
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..618
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 44..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..403
FT /evidence="ECO:0000255"
FT COMPBIAS 47..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 68634 MW; EA928A6DE3077846 CRC64;
MLRSSVLQGR HILSSSARPR PAPQWLARAG ASSRLAGQRF FADAKSPTPV TPSSATPVPA
ETAAKSTAGP SATETPTPAP TRKTGRFRKF LIYLILTSGL AYGGGVFLAL KSDNFHDFFT
EYVPYGEESV LYFEERDFYR RFPNTLRNKN RLSPASRDEG SRVTIPSKSG LSSKEVEETG
TDVSQPGPHM SAVTPAKADE ATIKPAAAKP EEKTAAVKEA KKQAQEPEKP REEPKQEPKL
PGSAPITTLE FANVSEGDEP IVQELVKTFN DIITVISADE DSAKYSKPVA KAKEELQKIG
EQILSVRDEA RRAAQEEIEK AHATFDESAR ELIRRFEEVR ANDAAQYREE FEAERERLAL
AYQQKIQTEL QRAQEIAEQR LQNELVEQAI ELNRKYIHEV KDLVEREREG RLSKLSELTS
SVSELETLVT GWREVIDTNL KTQQLQVAVD AVRSALERST VPRPFVRELV AVKELAGDDP
VVEAAIASIN PAAYQRGIPS TSQIIERFRR VADEVRKASL LPEDAGIASH AASLVLSKVM
FKKDAEAGSD DVESVLLRTE NLLEQGNLDD AAREMNSLKG WAKILSKDWL ADVRRVLEVK
QALEVIETEA RLQCLRVE
