MIC60_SCLS1
ID MIC60_SCLS1 Reviewed; 659 AA.
AC A7F6C1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=MICOS complex subunit mic60;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=mic60; ORFNames=SS1G_13150;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476643; EDN98292.1; -; Genomic_DNA.
DR RefSeq; XP_001586057.1; XM_001586007.1.
DR AlphaFoldDB; A7F6C1; -.
DR SMR; A7F6C1; -.
DR STRING; 665079.A7F6C1; -.
DR EnsemblFungi; EDN98292; EDN98292; SS1G_13150.
DR GeneID; 5482053; -.
DR KEGG; ssl:SS1G_13150; -.
DR eggNOG; KOG1854; Eukaryota.
DR HOGENOM; CLU_008024_1_2_1; -.
DR InParanoid; A7F6C1; -.
DR OMA; LQGWAKV; -.
DR Proteomes; UP000001312; 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..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..659
FT /note="MICOS complex subunit mic60"
FT /id="PRO_0000406673"
FT TOPO_DOM 41..129
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..659
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 41..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..458
FT /evidence="ECO:0000255"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 72575 MW; 97C6BCB0F9C15FE5 CRC64;
MLRAGLRSSR ALGLRPNVVS PGRQWRAQNA RVISDTMRTF ADKSSISDSR PPVLPGSASE
ATSEPLPPGA VATPNSAAPT PATPTSSTIP AENVPLTPPP PGVQSPGPPP PSSSPPPPAP
KPKRRFFRKF FTTLFLLTTL GFGGGVYYSR INDNFHDFFT EYVPFGEDAV LYFEEQEFRK
RFPLISSRAS RPPRDTGEQV KIPSQSGVSW RVANENKDST GRHTSSAKDK VKPSEAVQTP
HDSKPADRVK AVEQVKSGNS PVKNSPAPPA TPESKPSNVQ KDPEVNEPSR AYKKIERIDP
INIPNGNEPV VQELVKIMND IIAVVNADNA NARFTSTMDK AKAELNRVGA KILDMKDAAL
KQADEKIKSS DAEFDRAAMQ LMQNFKNQQA EQEAQFRAEY EAERKRIHEN YEQKLKSELD
RANEVNEKTL QNNLTEQALE LKRAFLADVK NRVEQEREGR LGKLSELTST VNDLEKLTGD
FNTVVDQNLK TQHLHVAVEA VRANLEKSQI PRPFTRELAA LKEIASDDPV VNAAIASINP
VAYQKGVPSS AALIDRFRRV ASEVRKASLL PEEAGVASHA SSYVLSKLLF KKKGLATGDD
VESILTRTET FLEEGDLDGA AREMNGLKGW AKTLSKDWLG EVRKVLEVQQ ALDKPDYKV
