CHCH2_MOUSE
ID CHCH2_MOUSE Reviewed; 153 AA.
AC Q9D1L0; Q3TUG8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 2;
GN Name=Chchd2;
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, and NOD; TISSUE=Egg, Head, Placenta, and Thymus;
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=129, and FVB/N; TISSUE=Colon, 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).
CC -!- FUNCTION: Transcription factor. Binds to the oxygen responsive element
CC of COX4I2 and activates its transcription under hypoxia conditions (4%
CC oxygen), as well as normoxia conditions (20% oxygen).
CC {ECO:0000250|UniProtKB:Q9Y6H1}.
CC -!- SUBUNIT: Interacts with RBPJ. {ECO:0000250|UniProtKB:Q9Y6H1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6H1}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9Y6H1}. Mitochondrion
CC intermembrane space {ECO:0000250|UniProtKB:Q9Y6H1}. Note=Mainly
CC localized in the intermembrane space. {ECO:0000250|UniProtKB:Q9Y6H1}.
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DR EMBL; AK003399; BAB22764.1; -; mRNA.
DR EMBL; AK088374; BAC40313.1; -; mRNA.
DR EMBL; AK145492; BAE26469.1; -; mRNA.
DR EMBL; AK160779; BAE36003.1; -; mRNA.
DR EMBL; AK162133; BAE36745.1; -; mRNA.
DR EMBL; AK166796; BAE39024.1; -; mRNA.
DR EMBL; AK167593; BAE39651.1; -; mRNA.
DR EMBL; BC042717; AAH42717.1; -; mRNA.
DR EMBL; BC082287; AAH82287.1; -; mRNA.
DR EMBL; BC084682; AAH84682.1; -; mRNA.
DR CCDS; CCDS19702.1; -.
DR RefSeq; NP_077128.2; NM_024166.6.
DR AlphaFoldDB; Q9D1L0; -.
DR SMR; Q9D1L0; -.
DR BioGRID; 199534; 4.
DR IntAct; Q9D1L0; 2.
DR MINT; Q9D1L0; -.
DR STRING; 10090.ENSMUSP00000091835; -.
DR iPTMnet; Q9D1L0; -.
DR PhosphoSitePlus; Q9D1L0; -.
DR EPD; Q9D1L0; -.
DR jPOST; Q9D1L0; -.
DR MaxQB; Q9D1L0; -.
DR PaxDb; Q9D1L0; -.
DR PeptideAtlas; Q9D1L0; -.
DR PRIDE; Q9D1L0; -.
DR ProteomicsDB; 281601; -.
DR Antibodypedia; 44807; 150 antibodies from 27 providers.
DR Ensembl; ENSMUST00000094280; ENSMUSP00000091835; ENSMUSG00000070493.
DR GeneID; 14004; -.
DR KEGG; mmu:14004; -.
DR UCSC; uc008ztn.1; mouse.
DR CTD; 51142; -.
DR MGI; MGI:1261428; Chchd2.
DR VEuPathDB; HostDB:ENSMUSG00000070493; -.
DR eggNOG; KOG4090; Eukaryota.
DR GeneTree; ENSGT00440000038159; -.
DR HOGENOM; CLU_093520_2_2_1; -.
DR InParanoid; Q9D1L0; -.
DR OMA; CDADARN; -.
DR OrthoDB; 1611117at2759; -.
DR PhylomeDB; Q9D1L0; -.
DR TreeFam; TF318060; -.
DR BioGRID-ORCS; 14004; 9 hits in 58 CRISPR screens.
DR ChiTaRS; Chchd2; mouse.
DR PRO; PR:Q9D1L0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D1L0; protein.
DR Bgee; ENSMUSG00000070493; Expressed in right kidney and 66 other tissues.
DR Genevisible; Q9D1L0; MM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; ISS:UniProtKB.
DR PROSITE; PS51808; CHCH; 1.
PE 2: Evidence at transcript level;
KW Activator; Disulfide bond; Mitochondrion; Nucleus; Reference proteome;
KW Transcription.
FT CHAIN 1..153
FT /note="Coiled-coil-helix-coiled-coil-helix domain-
FT containing protein 2"
FT /id="PRO_0000129161"
FT DOMAIN 113..153
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..126
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 136..146
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 116..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 126..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 153 AA; 15661 MW; 86D001C54F3354B4 CRC64;
MPRGSRSRTS RVTPPASRAP QMRAAPRRAP AAQPPAAAAP SAVGSPAAAP RQPGLMAQMA
TTAAGVAVGS AVGHTLGHAI TGGFSGGGSA EPAKPDITYQ EPQGAQLQNQ QSFGPCSLEI
KQFLECAQNQ SDVKLCEGFN EVLRQCRIAN GLM
