MIC19_MOUSE
ID MIC19_MOUSE Reviewed; 227 AA.
AC Q9CRB9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=MICOS complex subunit Mic19;
DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3;
GN Name=Chchd3; Synonyms=Mic19;
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=Kidney;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP PROTEIN SEQUENCE OF 2-8, FUNCTION, CLEAVAGE OF INITIATOR METHIONINE,
RP MYRISTOYLATION AT GLY-2, INTERACTION WITH HSPA1A/HSPA1B; IMMT; OPA1 AND
RP SAMM50, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=21081504; DOI=10.1074/jbc.m110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-50; SER-51 AND
RP SER-56, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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. Has also been shown
CC to function as a transcription factor which binds to the BAG1 promoter
CC and represses BAG1 transcription. Plays an important role in the
CC maintenance of the MICOS complex stability and the mitochondrial
CC cristae morphology. {ECO:0000250|UniProtKB:Q9NX63,
CC ECO:0000269|PubMed:21081504}.
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 (By similarity). Interacts with HSPA1A/HSPA1B and OPA1,
CC preferentially with the soluble OPA1 form.
CC {ECO:0000250|UniProtKB:Q9NX63, ECO:0000269|PubMed:21081504}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21081504}; Lipid-anchor
CC {ECO:0000269|PubMed:21081504}; Intermembrane side
CC {ECO:0000269|PubMed:21081504}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NX63}. Nucleus {ECO:0000250|UniProtKB:Q9NX63}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9NX63}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC Mic19 subfamily. {ECO:0000305}.
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DR EMBL; AK002263; BAB21974.1; -; mRNA.
DR EMBL; AK003519; BAB22832.1; -; mRNA.
DR EMBL; BC021941; AAH21941.1; -; mRNA.
DR CCDS; CCDS19986.1; -.
DR RefSeq; NP_079612.1; NM_025336.1.
DR AlphaFoldDB; Q9CRB9; -.
DR SMR; Q9CRB9; -.
DR BioGRID; 211197; 34.
DR IntAct; Q9CRB9; 13.
DR MINT; Q9CRB9; -.
DR STRING; 10090.ENSMUSP00000070149; -.
DR iPTMnet; Q9CRB9; -.
DR PhosphoSitePlus; Q9CRB9; -.
DR SwissPalm; Q9CRB9; -.
DR EPD; Q9CRB9; -.
DR jPOST; Q9CRB9; -.
DR MaxQB; Q9CRB9; -.
DR PaxDb; Q9CRB9; -.
DR PeptideAtlas; Q9CRB9; -.
DR PRIDE; Q9CRB9; -.
DR ProteomicsDB; 252553; -.
DR TopDownProteomics; Q9CRB9; -.
DR Antibodypedia; 32162; 307 antibodies from 33 providers.
DR Ensembl; ENSMUST00000066379; ENSMUSP00000070149; ENSMUSG00000053768.
DR GeneID; 66075; -.
DR KEGG; mmu:66075; -.
DR UCSC; uc009bgo.1; mouse.
DR CTD; 54927; -.
DR MGI; MGI:1913325; Chchd3.
DR VEuPathDB; HostDB:ENSMUSG00000053768; -.
DR eggNOG; KOG4083; Eukaryota.
DR GeneTree; ENSGT00390000000903; -.
DR HOGENOM; CLU_049040_2_1_1; -.
DR InParanoid; Q9CRB9; -.
DR OMA; QCYQQNP; -.
DR OrthoDB; 1509756at2759; -.
DR PhylomeDB; Q9CRB9; -.
DR TreeFam; TF326279; -.
DR BioGRID-ORCS; 66075; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Chchd3; mouse.
DR PRO; PR:Q9CRB9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CRB9; protein.
DR Bgee; ENSMUSG00000053768; Expressed in cardiac muscle of left ventricle and 264 other tissues.
DR ExpressionAtlas; Q9CRB9; baseline and differential.
DR Genevisible; Q9CRB9; MM.
DR GO; GO:0061617; C:MICOS complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0042407; P:cristae formation; ISO:MGI.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:MGI.
DR GO; GO:0008053; P:mitochondrial fusion; ISO:MGI.
DR InterPro; IPR007964; MIC19/MIC25.
DR Pfam; PF05300; MIC19_MIC25; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Myristate; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:21081504"
FT CHAIN 2..227
FT /note="MICOS complex subunit Mic19"
FT /id="PRO_0000129164"
FT DOMAIN 180..222
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..193
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 204..214
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 35..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:21081504"
FT DISULFID 183..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 193..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MUTAGEN 2
FT /note="G->A: Loss of SAMM50-binding. Reduced affinity
FT toward OPA1. No effect on IMMT-binding."
FT /evidence="ECO:0000269|PubMed:21081504"
SQ SEQUENCE 227 AA; 26335 MW; 055B1AF5A6DB808E CRC64;
MGGTASTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS SVYGASVSDE
DLKRRVAEEL ALEQAKKESE HQRRLKQARD LERERAAANE QLTRAVLRER ISSEEERMKA
KHLARQLEEK DRVMRKQDAF YKEQLARLEE RSSEFYKVTT EEYQKAAEEV EAKFKRYEYH
PVCADLQTKI LQCYRQNTQQ TLSCSALASQ YMHCVNHAKQ SMLEKGG
