CHDH_MOUSE
ID CHDH_MOUSE Reviewed; 596 AA.
AC Q8BJ64; Q3TPY4; Q8CHT7;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Choline dehydrogenase, mitochondrial;
DE Short=CDH;
DE Short=CHD;
DE EC=1.1.99.1;
DE Flags: Precursor;
GN Name=Chdh;
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=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=FVB/N;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Pancreas, 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).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20371614; DOI=10.1096/fj.09-153718;
RA Johnson A.R., Craciunescu C.N., Guo Z., Teng Y.W., Thresher R.J.,
RA Blusztajn J.K., Zeisel S.H.;
RT "Deletion of murine choline dehydrogenase results in diminished sperm
RT motility.";
RL FASEB J. 24:2752-2761(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-486 AND LYS-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486; LYS-498 AND LYS-582, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC ChEBI:CHEBI:17499; EC=1.1.99.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:20371614}.
CC -!- PTM: Acetylation of Lys-498 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- DISRUPTION PHENOTYPE: Decreased testicular betaine and increased
CC choline and phosphatidylcholine concentrations. Only one of eleven
CC males was able to reproduce, impaired fertility was due to diminished
CC sperm motility. {ECO:0000269|PubMed:20371614}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AK030900; BAC27176.1; -; mRNA.
DR EMBL; AK164042; BAE37601.1; -; mRNA.
DR EMBL; BC039186; AAH39186.1; -; mRNA.
DR CCDS; CCDS26892.1; -.
DR RefSeq; NP_001129712.1; NM_001136240.1.
DR RefSeq; NP_758468.2; NM_172264.2.
DR RefSeq; NP_780552.1; NM_175343.5.
DR AlphaFoldDB; Q8BJ64; -.
DR SMR; Q8BJ64; -.
DR STRING; 10090.ENSMUSP00000065542; -.
DR iPTMnet; Q8BJ64; -.
DR PhosphoSitePlus; Q8BJ64; -.
DR SwissPalm; Q8BJ64; -.
DR EPD; Q8BJ64; -.
DR jPOST; Q8BJ64; -.
DR MaxQB; Q8BJ64; -.
DR PaxDb; Q8BJ64; -.
DR PeptideAtlas; Q8BJ64; -.
DR PRIDE; Q8BJ64; -.
DR ProteomicsDB; 281611; -.
DR Antibodypedia; 31431; 144 antibodies from 22 providers.
DR DNASU; 218865; -.
DR Ensembl; ENSMUST00000067620; ENSMUSP00000065542; ENSMUSG00000015970.
DR Ensembl; ENSMUST00000118917; ENSMUSP00000112916; ENSMUSG00000015970.
DR GeneID; 218865; -.
DR KEGG; mmu:218865; -.
DR UCSC; uc007sup.2; mouse.
DR CTD; 55349; -.
DR MGI; MGI:1860776; Chdh.
DR VEuPathDB; HostDB:ENSMUSG00000015970; -.
DR eggNOG; KOG1238; Eukaryota.
DR GeneTree; ENSGT00530000063260; -.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; Q8BJ64; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 798314at2759; -.
DR PhylomeDB; Q8BJ64; -.
DR TreeFam; TF313911; -.
DR BRENDA; 1.1.99.1; 3474.
DR Reactome; R-MMU-6798163; Choline catabolism.
DR UniPathway; UPA00529; UER00385.
DR BioGRID-ORCS; 218865; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Chdh; mouse.
DR PRO; PR:Q8BJ64; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BJ64; protein.
DR Bgee; ENSMUSG00000015970; Expressed in vestibular membrane of cochlear duct and 201 other tissues.
DR Genevisible; Q8BJ64; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008812; F:choline dehydrogenase activity; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR011533; BetA.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01810; betA; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..596
FT /note="Choline dehydrogenase, mitochondrial"
FT /id="PRO_0000012330"
FT ACT_SITE 513
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 44..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 438
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 486
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 486
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 498
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 498
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 582
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 4
FT /note="V -> A (in Ref. 2; AAH39186)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="W -> C (in Ref. 2; AAH39186)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Q -> R (in Ref. 2; AAH39186)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> A (in Ref. 1; BAE37601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66415 MW; D31F19A0E0DB9587 CRC64;
MWQVLRGWRK GWQSPRGALA WAVQGQPCPP CSRAVASVGK DEYTFVVVGA GSAGCVLASR
LTEDPNHRVL LLEAGPKDLL MGSKRLQWKI HMPAALVSNL CDDKYNWYYH TEPQPGMDSR
VLYWPRGRVW GGSSSLNAMV YIRGHAEDYN RWHREGAEGW DYAHCLPYFR KAQRHELGAN
MYRGGDGPLH VSRGKTNHPL HQAFLQAARQ AGYPFTEDMN GFQQEGFGWM DMTVHQGKRW
STACAYLHPV LSRPNLRAEV QTLVSRVLFE GTRAVGVEYI KDGQRHKAYV SREVILSGGA
INSPQLLMLS GVGNADDLRK LDIPVVCHLP GVGQNLQDHL EVYVQQACTQ PITLHSAQKP
LRKVCIGLEW LWSYTGDGAT AHLETGGFIR SRPGVPHPDI QFHFLPSQVI DHGRKPTQQE
AYQVHVGTMR ATSVGWLKLR SANPRDHPVI HPNYLSTETD VEDFRQCVRL SREIFAQEAL
APFRGKELQP GSHVQSDKEI DAFVRAKADS AYHPSCTCKM GRSSDPTAVV DAQTKVIGVE
NLRVVDASIM PSVVSGNLNA PTVMIAEKAA DIIKGHPALE DKNVPVYKPQ TLDTQR
