ID   MIC60_MESAU             Reviewed;          22 AA.
AC   P86248;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitochondrial inner membrane protein {ECO:0000250|UniProtKB:Q16891};
DE   AltName: Full=Mitofilin {ECO:0000250|UniProtKB:Q16891};
DE   Flags: Fragments;
GN   Name=IMMT {ECO:0000250|UniProtKB:Q16891}; Synonyms=MIC60;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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 an important
CC       role in the maintenance of the MICOS complex stability and the
CC       mitochondrial cristae morphology. {ECO:0000250|UniProtKB:Q16891}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC       CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC       and MICOS13/MIC13 (By similarity). This complex was also known under
CC       the names MINOS or MitOS complex. The MICOS complex associates with
CC       mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together
CC       described as components of the mitochondrial outer membrane sorting
CC       assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner
CC       membrane protein TMEM11 and with HSPA9 (By similarity). The MICOS and
CC       SAM complexes together with DNAJC11 are part of a large protein complex
CC       spanning both membranes termed the mitochondrial intermembrane space
CC       bridging (MIB) complex (By similarity). Interacts with HSPA1A/HSPA1B
CC       and OPA1, preferentially with the soluble OPA1 form (By similarity).
CC       Interacts with MICOS13/MIC13, MICOS10/MIC10, CHCHD3/MIC19,
CC       CHCHD6/MIC25, SAMM50 and TMEM11 (By similarity). Interacts with
CC       APOO/MIC23/MIC26 and APOOL/MIC27 (By similarity). Interacts with ARMC1
CC       (By similarity). Interacts with ARMC12 (By similarity).
CC       {ECO:0000250|UniProtKB:Q16891, ECO:0000250|UniProtKB:Q8CAQ8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q16891}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q16891}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P86248; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome.
FT   CHAIN           <1..>22
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000394417"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         22
SQ   SEQUENCE   22 AA;  2660 MW;  E7E1807F25859B0C CRC64;
     VVSQYHELVV QARLSEQELE FR