Q9CRB9 (CHCH3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial

Gene names

Name:

Chchd3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for maintenance of mitochondrial crista integrity and mitochondrial function. May act as a scaffolding protein that stabilizes protein complexes involved in crista architecture and protein import. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Ref.3
Subunit structure	Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the soluble OPA1 form. Component of the MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2. Interacts with CHCHD6. Ref.3
Subcellular location	Mitochondrion inner membrane; Lipid-anchor; Intermembrane side. Cytoplasm By similarity. Nucleus By similarity Ref.3.
Sequence similarities	Contains 1 CHCH domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Molecular function	Repressor
PTM	Acetylation Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	inner mitochondrial membrane organization Inferred from electronic annotation. Source: Compara mitochondrial fusion Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from direct assay Ref.3. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from sequence or structural similarity. Source: UniProtKB phosphatase binding Inferred from sequence or structural similarity. Source: UniProtKB protein complex scaffold Inferred from mutant phenotype Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 227	226	Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial		PRO_0000129164
Regions
	Domain	176 – 217	42	CHCH
Amino acid modifications
	Modified residue	49	1	Phosphotyrosine By similarity
	Modified residue	50	1	Phosphoserine By similarity
	Modified residue	58	1	Phosphoserine Ref.5
	Modified residue	142	1	N6-acetyllysine By similarity
	Lipidation	2	1	N-myristoyl glycine Ref.3
Experimental info
	Mutagenesis	2	1	G → A: Loss of SAMM50-binding. Reduced affinity toward OPA1. No effect on IMMT-binding. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9CRB9 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 055B1AF5A6DB808E	FASTA	227	26,335
	10 20 30 40 50 60 MGGTASTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS SVYGASVSDE 70 80 90 100 110 120 DLKRRVAEEL ALEQAKKESE HQRRLKQARD LERERAAANE QLTRAVLRER ISSEEERMKA 130 140 150 160 170 180 KHLARQLEEK DRVMRKQDAF YKEQLARLEE RSSEFYKVTT EEYQKAAEEV EAKFKRYEYH 190 200 210 220 PVCADLQTKI LQCYRQNTQQ TLSCSALASQ YMHCVNHAKQ SMLEKGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[3]	"ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function." Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S. J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION, CLEAVAGE OF INITIATOR METHIONINE, MYRISTOYLATION AT GLY-2, INTERACTION WITH HSPA1A/HSPA1B; IMMT; OPA1 AND SAMM50, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2, MASS SPECTROMETRY.
[4]	"Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria." Mootha V.K., Bunkenborg J., Olsen J.V., Hjerrild M., Wisniewski J.R., Stahl E., Bolouri M.S., Ray H.N., Sihag S., Kamal M., Patterson N., Lander E.S., Mann M. Cell 115:629-640(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION. Strain: C57BL/6J.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002263 mRNA. Translation: BAB21974.1. AK003519 mRNA. Translation: BAB22832.1. BC021941 mRNA. Translation: AAH21941.1.
IPI	IPI00133562.
RefSeq	NP_079612.1. NM_025336.1.
UniGene	Mm.21501.
3D structure databases
ProteinModelPortal	Q9CRB9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CRB9. 3 interactions.
PTM databases
PhosphoSite	Q9CRB9.
Proteomic databases
PaxDb	Q9CRB9.
PRIDE	Q9CRB9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000066379; ENSMUSP00000070149; ENSMUSG00000053768.
GeneID	66075.
KEGG	mmu:66075.
UCSC	uc009bgo.1. mouse.
Organism-specific databases
CTD	54927.
MGI	MGI:1913325. Chchd3.
Phylogenomic databases
eggNOG	NOG284774.
GeneTree	ENSGT00390000000903.
HOGENOM	HOG000252969.
HOVERGEN	HBG050936.
InParanoid	Q9CRB9.
OMA	SALANQY.
OrthoDB	EOG46MBKQ.
Gene expression databases
ArrayExpress	Q9CRB9.
Bgee	Q9CRB9.
Genevestigator	Q9CRB9.
GermOnline	ENSMUSG00000053768. Mus musculus.
Family and domain databases
InterPro	IPR007964. DUF737. [Graphical view]
Pfam	PF05300. DUF737. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CHCHD3. mouse.
NextBio	320556.
SOURCE	Search...

Entry information

Entry name

CHCH3_MOUSE

Accession

Primary (citable) accession number: Q9CRB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program