MIC25_HUMAN
ID MIC25_HUMAN Reviewed; 235 AA.
AC Q9BRQ6; D6R9U0; D6RIB4; H8Y0Y7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=MICOS complex subunit MIC25;
DE AltName: Full=Coiled-coil-helix cristae morphology protein 1;
DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6;
GN Name=CHCHD6; Synonyms=CHCM1, MIC25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND
RP INTERACTION WITH CHCHD3; DISC1 AND IMMT.
RX PubMed=22228767; DOI=10.1074/jbc.m111.277103;
RA An J., Shi J., He Q., Lui K., Liu Y., Huang Y., Sheikh M.S.;
RT "CHCM1/CHCHD6, a novel mitochondrial protein linked to regulation of
RT mitofilin and mitochondrial cristae morphology.";
RL J. Biol. Chem. 287:7411-7426(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP IDENTIFICATION IN A COMPLEX WITH IMMT.
RX PubMed=17624330; DOI=10.1016/j.febslet.2007.06.052;
RA Xie J., Marusich M.F., Souda P., Whitelegge J., Capaldi R.A.;
RT "The mitochondrial inner membrane protein mitofilin exists as a complex
RT with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-
RT containing protein 3 and 6 and DnaJC11.";
RL FEBS Lett. 581:3545-3549(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP NOMENCLATURE.
RX PubMed=24687277; DOI=10.1083/jcb.201401006;
RA Pfanner N., van der Laan M., Amati P., Capaldi R.A., Caudy A.A.,
RA Chacinska A., Darshi M., Deckers M., Hoppins S., Icho T., Jakobs S., Ji J.,
RA Kozjak-Pavlovic V., Meisinger C., Odgren P.R., Park S.K., Rehling P.,
RA Reichert A.S., Sheikh M.S., Taylor S.S., Tsuchida N., van der Bliek A.M.,
RA van der Klei I.J., Weissman J.S., Westermann B., Zha J., Neupert W.,
RA Nunnari J.;
RT "Uniform nomenclature for the mitochondrial contact site and cristae
RT organizing system.";
RL J. Cell Biol. 204:1083-1086(2014).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION IN THE MICOS COMPLEX, INTERACTION WITH IMMT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [11]
RP IDENTIFICATION IN THE MICOS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25781180; DOI=10.1371/journal.pone.0120213;
RA Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.;
RT "Detailed analysis of the human mitochondrial contact site complex indicate
RT a hierarchy of subunits.";
RL PLoS ONE 10:E0120213-E0120213(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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:0000269|PubMed:22228767}.
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 (PubMed:17624330, PubMed:22228767,
CC PubMed:25781180, PubMed:25997101). 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 (PubMed:22228767). Interacts with DISC1
CC (PubMed:22228767). Interacts with IMMT/MIC60 (PubMed:22228767,
CC PubMed:25997101). {ECO:0000269|PubMed:17624330,
CC ECO:0000269|PubMed:22228767, ECO:0000269|PubMed:25781180,
CC ECO:0000269|PubMed:25997101, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BRQ6; Q9Y512: SAMM50; NbExp=3; IntAct=EBI-2557895, EBI-748409;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:22228767}; Lipid-anchor
CC {ECO:0000305|PubMed:22228767}. Mitochondrion
CC {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.
CC -!- INDUCTION: Down-regulated following genotoxic stress.
CC {ECO:0000269|PubMed:22228767}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC Mic25 subfamily. {ECO:0000305}.
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DR EMBL; JF264889; AEA95848.1; -; mRNA.
DR EMBL; AC078867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79352.1; -; Genomic_DNA.
DR EMBL; BC006123; AAH06123.1; -; mRNA.
DR CCDS; CCDS3041.1; -.
DR RefSeq; NP_001307539.1; NM_001320610.1.
DR RefSeq; NP_115719.1; NM_032343.2.
DR AlphaFoldDB; Q9BRQ6; -.
DR SMR; Q9BRQ6; -.
DR BioGRID; 124029; 107.
DR ComplexPortal; CPX-6141; MICOS mitochondrial contact site and cristae organizing system complex.
DR CORUM; Q9BRQ6; -.
DR IntAct; Q9BRQ6; 33.
DR MINT; Q9BRQ6; -.
DR STRING; 9606.ENSP00000290913; -.
DR ChEMBL; CHEMBL4105993; -.
DR GlyGen; Q9BRQ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRQ6; -.
DR PhosphoSitePlus; Q9BRQ6; -.
DR BioMuta; CHCHD6; -.
DR DMDM; 62510505; -.
DR EPD; Q9BRQ6; -.
DR jPOST; Q9BRQ6; -.
DR MassIVE; Q9BRQ6; -.
DR MaxQB; Q9BRQ6; -.
DR PaxDb; Q9BRQ6; -.
DR PeptideAtlas; Q9BRQ6; -.
DR PRIDE; Q9BRQ6; -.
DR ProteomicsDB; 78807; -.
DR Antibodypedia; 46643; 218 antibodies from 27 providers.
DR DNASU; 84303; -.
DR Ensembl; ENST00000290913.8; ENSP00000290913.3; ENSG00000159685.11.
DR GeneID; 84303; -.
DR KEGG; hsa:84303; -.
DR MANE-Select; ENST00000290913.8; ENSP00000290913.3; NM_032343.3; NP_115719.1.
DR UCSC; uc003ejf.3; human.
DR CTD; 84303; -.
DR DisGeNET; 84303; -.
DR GeneCards; CHCHD6; -.
DR HGNC; HGNC:28184; CHCHD6.
DR HPA; ENSG00000159685; Tissue enhanced (testis).
DR MIM; 615634; gene.
DR neXtProt; NX_Q9BRQ6; -.
DR OpenTargets; ENSG00000159685; -.
DR PharmGKB; PA134899331; -.
DR VEuPathDB; HostDB:ENSG00000159685; -.
DR eggNOG; KOG4083; Eukaryota.
DR GeneTree; ENSGT00390000000903; -.
DR HOGENOM; CLU_049040_0_0_1; -.
DR InParanoid; Q9BRQ6; -.
DR OMA; LRCYRDN; -.
DR OrthoDB; 1234703at2759; -.
DR PhylomeDB; Q9BRQ6; -.
DR TreeFam; TF326279; -.
DR PathwayCommons; Q9BRQ6; -.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q9BRQ6; -.
DR BioGRID-ORCS; 84303; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; CHCHD6; human.
DR GenomeRNAi; 84303; -.
DR Pharos; Q9BRQ6; Tbio.
DR PRO; PR:Q9BRQ6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BRQ6; protein.
DR Bgee; ENSG00000159685; Expressed in left testis and 139 other tissues.
DR ExpressionAtlas; Q9BRQ6; baseline and differential.
DR Genevisible; Q9BRQ6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0061617; C:MICOS complex; IDA:UniProtKB.
DR GO; GO:0044284; C:mitochondrial crista junction; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC: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..235
FT /note="MICOS complex subunit MIC25"
FT /id="PRO_0000129169"
FT DOMAIN 194..235
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 31..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..176
FT /evidence="ECO:0000255"
FT MOTIF 197..207
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 218..228
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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 197..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 207..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT VARIANT 95
FT /note="A -> S (in dbSNP:rs2272487)"
FT /id="VAR_024412"
SQ SEQUENCE 235 AA; 26458 MW; 674DE387557AF4F0 CRC64;
MGSTESSEGR RVSFGVDEEE RVRVLQGVRL SENVVNRMKE PSSPPPAPTS STFGLQDGNL
RAPHKESTLP RSGSSGGQQP SGMKEGVKRY EQEHAAIQDK LFQVAKRERE AATKHSKASL
PTGEGSISHE EQKSVRLARE LESREAELRR RDTFYKEQLE RIERKNAEMY KLSSEQFHEA
ASKMESTIKP RRVEPVCSGL QAQILHCYRD RPHEVLLCSD LVKAYQRCVS AAHKG
