ID   CHDH_MOUSE              Reviewed;         596 AA.
AC   Q8BJ64; Q8CHT7;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Choline dehydrogenase, mitochondrial;
DE            Short=CHD;
DE            Short=CDH;
DE            EC=1.1.99.1;
DE   Flags: Precursor;
GN   Name=Chdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- CATALYTIC ACTIVITY: Choline + acceptor = betaine aldehyde +
CC       reduced acceptor.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- PTM: Acetylation of Lys-498 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
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DR   EMBL; AK030900; BAC27176.1; -; mRNA.
DR   EMBL; BC039186; AAH39186.1; -; mRNA.
DR   IPI; IPI00273146; -.
DR   RefSeq; NP_001129712.1; -.
DR   RefSeq; NP_758468.2; -.
DR   RefSeq; NP_780552.1; -.
DR   UniGene; Mm.259916; -.
DR   PhosphoSite; Q8BJ64; -.
DR   PRIDE; Q8BJ64; -.
DR   Ensembl; ENSMUSG00000015970; Mus musculus.
DR   GeneID; 218865; -.
DR   KEGG; mmu:218865; -.
DR   MGI; MGI:1860776; Chdh.
DR   HOGENOM; Q8BJ64; -.
DR   HOVERGEN; Q8BJ64; -.
DR   OMA; Q8BJ64; WREYKEN.
DR   BRENDA; 1.1.99.1; 244.
DR   NextBio; 376465; -.
DR   Bgee; Q8BJ64; -.
DR   CleanEx; MM_CHDH; -.
DR   GermOnline; ENSMUSG00000015970; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006066; P:cellular alcohol metabolic process; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from c...; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011533; Choline_dehydrogenase.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 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; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    596       Choline dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000012330.
FT   NP_BIND      44     73       FAD (By similarity).
FT   ACT_SITE    513    513       By similarity.
FT   MOD_RES     498    498       N6-acetyllysine.
FT   CONFLICT      4      4       V -> A (in Ref. 2; AAH39186).
FT   CONFLICT     12     12       W -> C (in Ref. 2; AAH39186).
FT   CONFLICT     24     24       Q -> R (in Ref. 2; AAH39186).
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
//