ID   MIC60_VANPO             Reviewed;         531 AA.
AC   A7TSS9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=Kpol_282p3;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480523; EDO14676.1; -; Genomic_DNA.
DR   RefSeq; XP_001642534.1; XM_001642484.1.
DR   AlphaFoldDB; A7TSS9; -.
DR   SMR; A7TSS9; -.
DR   STRING; 436907.A7TSS9; -.
DR   EnsemblFungi; EDO14676; EDO14676; Kpol_282p3.
DR   GeneID; 5542704; -.
DR   KEGG; vpo:Kpol_282p3; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   InParanoid; A7TSS9; -.
DR   OMA; NRWNLLE; -.
DR   OrthoDB; 1540241at2759; -.
DR   PhylomeDB; A7TSS9; -.
DR   Proteomes; UP000000267; 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; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..531
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406678"
FT   TOPO_DOM        16..34
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..531
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   COILED          210..267
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   531 AA;  59449 MW;  A6940F2076CEFD03 CRC64;
     MLRSSLNQNL AKRCLSTANN NGATLIKKRH PIRNFILKTA LGATVFYAGG VALSEYNEKF
     AEYFRTYVPL GDDLVHNYEV YRYGPDSKLG EGISVVGLRE MIQEVVYRNP TKFHPEGGEI
     EIIQEVVPPT RLLTLELITV DDERMDPKFS SLVKDLNSTI ETIINQNIYL TDSQIGYILE
     CYSTLTAAVT EYNQQLQNNM NLIIKEKTTK AVNELNSEYE KKFTDKESEL TGKFIQDFNN
     FKDQLEQKKA NELNTELRAN EQTLLAKHAN EVALLSITQV EEFTKIIKEK VDKERDGRLG
     QLQELDASVT SLSKSVDKMN NALMKNEVIT QMITLLSSMK QKLNEAGTTN EGLSLEKEID
     RIKLLSSIVP LATSSCKCSS KCKSNCKCSK SCGRKKTLMS VGISELDNAA SGKLILSNEQ
     LYNRWNLLEG DFKAASLLPA NPGILGHFTA KMFSLLLFTK RGVSVDGTDL DSVYAKVSEN
     IRLSKLDKAL ADVVSLKGWP HVVCQGWIDD AKRKLEVEAL IDVLDSEVRA L