MIC60_UNCRE
ID MIC60_UNCRE Reviewed; 668 AA.
AC C4JHS3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=MICOS complex subunit MIC60;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=MIC60; ORFNames=UREG_02759;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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; CH476615; EEP77910.1; -; Genomic_DNA.
DR RefSeq; XP_002543243.1; XM_002543197.1.
DR AlphaFoldDB; C4JHS3; -.
DR SMR; C4JHS3; -.
DR STRING; 33188.XP_002543243.1; -.
DR EnsemblFungi; EEP77910; EEP77910; UREG_02759.
DR GeneID; 8437546; -.
DR KEGG; ure:UREG_02759; -.
DR VEuPathDB; FungiDB:UREG_02759; -.
DR eggNOG; KOG1854; Eukaryota.
DR HOGENOM; CLU_008024_1_2_1; -.
DR InParanoid; C4JHS3; -.
DR OrthoDB; 1540241at2759; -.
DR Proteomes; UP000002058; 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..668
FT /note="MICOS complex subunit MIC60"
FT /id="PRO_0000406677"
FT TOPO_DOM 30..133
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..668
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..434
FT /evidence="ECO:0000255"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74143 MW; B86085E8EEFE610B CRC64;
MLRSSIAPSR QLLSPTVSRQ WLQASRRCYS RVRSPAAVSK GIPAFTPRGH AFTTSARLAN
DPNIRSPPSP SSESTIPPES VPRPPPSHPI QTSPGSTIEG RTQPPPPPPV TNTPPPPPPP
PPPAPKKGGR LRRLLIYLIL TTGLAYAGGV WLSLKSDNFH DFFTEYIPYG EEAVLYVEEQ
DFRRRFPNAT KQISRRAVEP RDEGQNVTIP GKSGVSWRVS EGQKETKEDG SDVSRRGKHM
SATEANTAKE ATKTSTVEET KAKKQVESAA PTTEKKSASE TVKPALEEPR APAIPTIDSV
EPLSMLVDEP TVQELTKIVN DLIAVINADE SSSRFTSTLS KAKADFQRLG EQIAVLRQDA
QDAARVEIEN ARAEMERTAN ELIRRIDEVR AEDAAQFREE YESERERLAN AYQEKIKTEL
QRVQEVAEQR LRNELVEQAI ELNRKFLSDV RSLVEKEREG RLSKLSELTA NVGELEKLTA
EWNSVVDTNL NTQQLQVAVD AVRSALENSD IPKPFINELV AVKELASDDQ VVDAAISSIS
PVAYQRGIPS PAQIVERFRR LATEVRKASL LPENAGIASH AASYMASKVM FKKQGSDDGD
DVESILTRTE NLLEEGRLDE AAREMNSLQG WSKILSKDWL ADVRRVLEVK QALEIIETEA
RLRCLQVE
