MIC25_BOVIN
ID MIC25_BOVIN Reviewed; 236 AA.
AC Q32L35;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=MICOS complex subunit MIC25;
DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6;
GN Name=CHCHD6; Synonyms=MIC25;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and MICOS13/MIC13. This complex was also known under the names MINOS or
CC MitOS complex. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC components of the mitochondrial outer membrane sorting assembly
CC machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC with DNAJC11 are part of a large protein complex spanning both
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex. Interacts with DISC1. Interacts with IMMT/MIC60.
CC {ECO:0000250|UniProtKB:Q9BRQ6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BRQ6}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9BRQ6}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9BRQ6}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC Mic25 subfamily. {ECO:0000305}.
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DR EMBL; DAAA02054713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02054714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02054715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109788; AAI09789.1; -; mRNA.
DR RefSeq; NP_001069870.1; NM_001076402.2.
DR AlphaFoldDB; Q32L35; -.
DR SMR; Q32L35; -.
DR STRING; 9913.ENSBTAP00000041190; -.
DR PaxDb; Q32L35; -.
DR PRIDE; Q32L35; -.
DR GeneID; 615934; -.
DR KEGG; bta:615934; -.
DR CTD; 84303; -.
DR eggNOG; KOG4083; Eukaryota.
DR HOGENOM; CLU_049040_0_0_1; -.
DR InParanoid; Q32L35; -.
DR OrthoDB; 1234703at2759; -.
DR TreeFam; TF326279; -.
DR Proteomes; UP000009136; Unplaced.
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 InterPro; IPR042860; MIC25.
DR PANTHER; PTHR47609; PTHR47609; 1.
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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..236
FT /note="MICOS complex subunit MIC25"
FT /id="PRO_0000416908"
FT DOMAIN 195..236
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..167
FT /evidence="ECO:0000255"
FT MOTIF 198..208
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 219..229
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRQ6"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91VN4"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT DISULFID 198..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 208..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 236 AA; 26439 MW; 8CFB1B72BBF5E4CC CRC64;
MGSAESREGR RASFGMDEEE RVRVLQGIRL SENVVNRMKE PGQPSRVGLL APPAAALGPS
GGREKDSKPP RPDCGSGRGP PRVQVDPLER CDWEQAVLQD ELVRVATTER EAAASPRSVT
LRRGEGGVDQ EKQRLAQRAR ELESQEEELR CRDAFYKEQL GRLERQNLEA YRLSSQQFHE
AATKIEGAIK PRRVEPVCSG LQAQILRCYR DRLQEVLLCA DLVRAYQHCV SSAHKG
