MIC60_AJECG
ID MIC60_AJECG Reviewed; 685 AA.
AC C0NUJ9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=MICOS complex subunit MIC60;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=MIC60; ORFNames=HCBG_07030;
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; GG663372; EEH05079.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NUJ9; -.
DR SMR; C0NUJ9; -.
DR STRING; 447093.C0NUJ9; -.
DR EnsemblFungi; EEH05079; EEH05079; HCBG_07030.
DR VEuPathDB; FungiDB:HCBG_07030; -.
DR HOGENOM; CLU_008024_1_2_1; -.
DR InParanoid; C0NUJ9; -.
DR OrthoDB; 1540241at2759; -.
DR Proteomes; UP000001631; 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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..685
FT /note="MICOS complex subunit MIC60"
FT /id="PRO_0000406637"
FT TOPO_DOM 43..145
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..685
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 66..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..494
FT /evidence="ECO:0000255"
FT COMPBIAS 66..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75882 MW; BFF0AE625EB9ED9C CRC64;
MLRTSIASSR PLLPSSVCPK APAQWLCTSR ARRVNTATRR YHALARKSNA GRRCSLTPNT
ATTSQFFQKA ASSTSTKPPG PSDADVRSPA SPSSRSSLRP ESIPKPPQSP PVQGQTSPGS
EVLPPDHESS TPPPPPGPKS SRLRKLLYLF LTAGLAYAGG VWYSLRSDNF YDFFTEYIPY
GEEAVLYLEE RDFRNRFPHV TKQINRRVTV PKDEGAQVTI PSGSGLSWKV AEEQQEATDM
TKKGRRMGTA HANEPTKDIK VAEKAKEEVK SKSAAKKEDV AANIPIQEAL EPQPAKTEEK
NLEAPRQPAV PAVTAIERLV QDKADEPVVQ DLVKVFNDVI SVISADESAS KFAGPIAKAK
EELQRIGDRI VALKKDAQES AQEEIRNAHA AFDKSAAELI RRIDEVRTQD AAEFREEFES
EREKIARSYQ EKVNTELQRA HEVAEQRLRN ELVEQAIELN RKFLSDVKTL VENEREGRLS
KLAELSANVA ELERLTAGWS DVVDINLKTQ QLQVAVDAVR TTLENSDVPR PFVRELAAVK
ELASNDEVVA AAIASISPAA YQRGIPSAAQ LVDRFRRVAS EVRKARLLPE NAGITSHAAS
LVLSKVMLKK QGLPTSDDVE SILTRTENFL EEGNFDEAAR EMNSLQGWAK LLSKDWLADV
RRVLEVKQAL EIIETEARLR CLQVE