ID   MC25A_XENLA             Reviewed;         260 AA.
AC   Q6AX41;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=MICOS complex subunit mic25-a;
DE   AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6A;
GN   Name=chchd6-a; Synonyms=mic25-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000250|UniProtKB:Q9BRQ6}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex (also known as MINOS or MitOS
CC       complex). {ECO:0000250|UniProtKB:Q9BRQ6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9BRQ6}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9BRQ6}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC       Mic25 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH79771.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC079771; AAH79771.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6AX41; -.
DR   SMR; Q6AX41; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0061617; C:MICOS complex; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0042407; P:cristae formation; ISS:UniProtKB.
DR   InterPro; IPR007964; MIC19/MIC25.
DR   Pfam; PF05300; MIC19_MIC25; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Lipoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..260
FT                   /note="MICOS complex subunit mic25-a"
FT                   /id="PRO_0000416911"
FT   DOMAIN          213..255
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          94..187
FT                   /evidence="ECO:0000255"
FT   MOTIF           216..226
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           237..247
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COMPBIAS        11..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        216..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        226..237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   260 AA;  29367 MW;  B112340BF3EC1418 CRC64;
     MGGSESTGRK VSFGMDEEER VRVLRGVRLS DEVVNRMKDS NLPSKDQSTS TASGTTSGPT
     TFPSKAGPSA SHSASTSKDG AHKPTARGVG HQYAEEDLYR RYEKEQALIQ EELARLAKRE
     REAAHERLSS SVLREKNITS QERRKAEHLP ADLDEWAKEL EQKEAELQRL NTFYREQLNS
     IEKKNLEIYK LTAEQFHTAA SNAELRVKQR SYDPVCMDLQ SNILKCYAEN KQERLNCSDL
     AKEYGKCVSA AQKNLLFNHG