ID   MIC60_PICST             Reviewed;         548 AA.
AC   A3LQS0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=PICST_76840;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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}.
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DR   EMBL; CP000497; ABN65250.2; -; Genomic_DNA.
DR   RefSeq; XP_001383279.2; XM_001383242.1.
DR   AlphaFoldDB; A3LQS0; -.
DR   SMR; A3LQS0; -.
DR   STRING; 4924.XP_001383279.2; -.
DR   EnsemblFungi; ABN65250; ABN65250; PICST_76840.
DR   GeneID; 4838164; -.
DR   KEGG; pic:PICST_76840; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_2_0_1; -.
DR   InParanoid; A3LQS0; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
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; 2.
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..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..548
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406671"
FT   TOPO_DOM        14..42
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..548
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          14..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          265..370
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  60804 MW;  620E48954311D700 CRC64;
     MAVRPLSASA RVWSSSVSET GKSSQGQDQK HENYQNHQQS SLAGIVIKSA LFATVVYGAT
     MFIATKNDKV MDFVIDQQIP YYEETIDLIE NGSYDDLVSA IKAKISSIRL PSKDEITELS
     HKIEHTSEDL LKETKRKLES ARAEFGSHST AGSGTSASLP ANQLQKHPEI EHVKKEVEHL
     PAIKLNENVV SYVDASVKAT IDSFNDLINS IDVSKVTPTD EGLIKTINEK VSELASKVGA
     LSKKFDDELQ SKLKVSQTEL LSSYTKKELE LTENLLHQFN RERAQLESKL NERLKQEIAA
     TKETISQAAV NAVSMVRIEQ TKNFEKLVAD KINEERNGKL ANLEKLNSRL ESLEQFAESL
     ESQVVATQQK SVIQKSLSSL KAVLFVSNPE EKPQSIKPYV DDLFESSPDD EVIQLALGEL
     GPLLSKESTQ SILTTSQLLT RWEQLVPELR SASLLPPNAG LLGHLASIVF SKFLVSVKGD
     KPDGKDIESV IGRVEASLVR DELDVAVEEV ANLKGWTRKL ANDWVIEGRK RLEAEYLVEL
     IDAETRIL