MIC25_MOUSE
ID MIC25_MOUSE Reviewed; 273 AA.
AC Q91VN4; Q3UNQ1; Q9D5I5; Q9DAM8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-31 AND SER-33, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24193.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005696; BAB24193.1; ALT_FRAME; mRNA.
DR EMBL; AK015314; BAB29792.1; -; mRNA.
DR EMBL; AK144093; BAE25696.1; -; mRNA.
DR EMBL; AC122387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011331; AAH11331.1; -; mRNA.
DR EMBL; BC052929; AAH52929.1; -; mRNA.
DR CCDS; CCDS39557.1; -.
DR RefSeq; NP_001161208.1; NM_001167736.1.
DR RefSeq; NP_079627.3; NM_025351.3.
DR AlphaFoldDB; Q91VN4; -.
DR SMR; Q91VN4; -.
DR BioGRID; 211212; 11.
DR IntAct; Q91VN4; 3.
DR MINT; Q91VN4; -.
DR STRING; 10090.ENSMUSP00000032172; -.
DR iPTMnet; Q91VN4; -.
DR PhosphoSitePlus; Q91VN4; -.
DR EPD; Q91VN4; -.
DR jPOST; Q91VN4; -.
DR MaxQB; Q91VN4; -.
DR PaxDb; Q91VN4; -.
DR PRIDE; Q91VN4; -.
DR ProteomicsDB; 293478; -.
DR Antibodypedia; 46643; 218 antibodies from 27 providers.
DR Ensembl; ENSMUST00000032172; ENSMUSP00000032172; ENSMUSG00000030086.
DR GeneID; 66098; -.
DR KEGG; mmu:66098; -.
DR UCSC; uc009cwh.2; mouse.
DR CTD; 84303; -.
DR MGI; MGI:1913348; Chchd6.
DR VEuPathDB; HostDB:ENSMUSG00000030086; -.
DR eggNOG; KOG4083; Eukaryota.
DR GeneTree; ENSGT00390000000903; -.
DR HOGENOM; CLU_049040_0_0_1; -.
DR InParanoid; Q91VN4; -.
DR OMA; LRCYRDN; -.
DR OrthoDB; 1234703at2759; -.
DR PhylomeDB; Q91VN4; -.
DR TreeFam; TF326279; -.
DR BioGRID-ORCS; 66098; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Chchd6; mouse.
DR PRO; PR:Q91VN4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91VN4; protein.
DR Bgee; ENSMUSG00000030086; Expressed in seminiferous tubule of testis and 256 other tissues.
DR ExpressionAtlas; Q91VN4; baseline and differential.
DR Genevisible; Q91VN4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0061617; C:MICOS complex; ISO:MGI.
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 1: Evidence at protein 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..273
FT /note="MICOS complex subunit Mic25"
FT /id="PRO_0000129170"
FT DOMAIN 232..273
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..189
FT /evidence="ECO:0000255"
FT MOTIF 235..245
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 256..266
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT DISULFID 235..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 245..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT CONFLICT 11
FT /note="R -> S (in Ref. 1; BAB24193)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..14
FT /note="VSF -> WSL (in Ref. 1; BAB29792)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="R -> C (in Ref. 3; AAH11331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29852 MW; 4A6345E4B17B0DDE CRC64;
MGSAESAEAR RVSFEMDEEE RVRVLQGIRL SESVVNRMKD CSQPSAGEQL VPGFGPSSSA
PVPTVPLPAI SVPTVPAPTT PVPTAPSSSV RGLPGGTCKG PLTDVKVPSA ESGGGLQSSA
VKEDLKKFQQ EQLAVQDEMV RVAKKEKEAA EKHLKASLPK KKASLTHEQQ QSARLARELE
DREAELSRRD TFYKEQQGRI QEKNAELYKL SSQQFHEAAS KAESTIKPRR VEPVCSGLQA
QILRCYRDHL HEVLLCSDLV KAYQHCVSTA RKG
