ID CHDH_HUMAN Reviewed; 594 AA. AC Q8NE62; Q9NY17; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 16-JUN-2009, entry version 60. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-78. RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 113-594. RC TISSUE=Kidney; RA Bugert P., Hanke S., Chudek J., Kovacs G.; RT "Analysis of a putative tumor suppressor gene region of 100 kb at RT chromosome 3p21.1 in conventional renal cell carcinoma."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC012467; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034502; AAH34502.1; -; mRNA. DR EMBL; AJ272267; CAB75961.1; -; mRNA. DR IPI; IPI00168603; -. DR RefSeq; NP_060867.2; -. DR UniGene; Hs.126688; -. DR HSSP; Q945K2; 1JU2. DR PhosphoSite; Q8NE62; -. DR Ensembl; ENSG00000016391; Homo sapiens. DR GeneID; 55349; -. DR KEGG; hsa:55349; -. DR GeneCards; GC03M053826; -. DR HGNC; HGNC:24288; CHDH. DR PharmGKB; PA134873121; -. DR HOGENOM; Q8NE62; -. DR HOVERGEN; Q8NE62; -. DR BRENDA; 1.1.99.1; 247. DR DrugBank; DB00122; Choline. DR NextBio; 59691; -. DR ArrayExpress; Q8NE62; -. DR Bgee; Q8NE62; -. DR CleanEx; HS_CHDH; -. DR GermOnline; ENSG00000016391; Homo sapiens. 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW. 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 PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. PE 2: Evidence at transcript level; KW Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; KW Polymorphism; Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 594 Choline dehydrogenase, mitochondrial. FT /FTId=PRO_0000012329. FT NP_BIND 42 71 FAD (By similarity). FT ACT_SITE 511 511 By similarity. FT MOD_RES 496 496 N6-acetyllysine (By similarity). FT VARIANT 40 40 E -> A (in dbSNP:rs9001). FT /FTId=VAR_020421. FT VARIANT 78 78 L -> R (in dbSNP:rs12676). FT /FTId=VAR_055097. FT VARIANT 441 441 N -> S (in dbSNP:rs34974961). FT /FTId=VAR_049357. FT CONFLICT 113 113 R -> A (in Ref. 3; CAB75961). SQ SEQUENCE 594 AA; 65358 MW; E9764CD0F325A501 CRC64; MWCLLRGLGR PGALARGALG QQQSLGARAL ASAGSESRDE YSYVVVGAGS AGCVLAGRLT EDPAERVLLL EAGPKDVLAG SKRLSWKIHM PAALVANLCD DRYNWCYHTE VQRGLDGRVL YWPRGRVWGG SSSLNAMVYV RGHAEDYERW QRQGARGWDY AHCLPYFRKA QGHELGASRY RGADGPLRVS RGKTNHPLHC AFLEATQQAG YPLTEDMNGF QQEGFGWMDM TIHEGKRWSA ACAYLHPALS RTNLKAEAET LVSRVLFEGT RAVGVEYVKN GQSHRAYASK EVILSGGAIN SPQLLMLSGI GNADDLKKLG IPVVCHLPGV GQNLQDHLEI YIQQACTRPI TLHSAQKPLR KVCIGLEWLW KFTGEGATAH LETGGFIRSQ PGVPHPDIQF HFLPSQVIDH GRVPTQQEAY QVHVGPMRGT SVGWLKLRSA NPQDHPVIQP NYLSTETDIE DFRLCVKLTR EIFAQEALAP FRGKELQPGS HIQSDKEIDA FVRAKADSAY HPSCTCKMGQ PSDPTAVVDP QTRVLGVENL RVVDASIMPS MVSGNLNAPT IMIAEKAADI IKGQPALWDK DVPVYKPRTL ATQR //