CHDH_HUMAN
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 03-AUG-2022, entry version 160.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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 project:
RT 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.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 -!- INTERACTION:
CC Q8NE62; Q92876: KLK6; NbExp=3; IntAct=EBI-7127986, EBI-2432309;
CC Q8NE62; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-7127986, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AC012467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034502; AAH34502.1; -; mRNA.
DR EMBL; AJ272267; CAB75961.1; -; mRNA.
DR CCDS; CCDS2873.1; -.
DR RefSeq; NP_060867.2; NM_018397.4.
DR RefSeq; XP_016862286.1; XM_017006797.1.
DR RefSeq; XP_016862287.1; XM_017006798.1.
DR AlphaFoldDB; Q8NE62; -.
DR SMR; Q8NE62; -.
DR BioGRID; 120629; 24.
DR CORUM; Q8NE62; -.
DR IntAct; Q8NE62; 16.
DR MINT; Q8NE62; -.
DR STRING; 9606.ENSP00000319851; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR iPTMnet; Q8NE62; -.
DR PhosphoSitePlus; Q8NE62; -.
DR BioMuta; CHDH; -.
DR DMDM; 229462828; -.
DR EPD; Q8NE62; -.
DR jPOST; Q8NE62; -.
DR MassIVE; Q8NE62; -.
DR MaxQB; Q8NE62; -.
DR PaxDb; Q8NE62; -.
DR PeptideAtlas; Q8NE62; -.
DR PRIDE; Q8NE62; -.
DR ProteomicsDB; 73126; -.
DR Antibodypedia; 31431; 144 antibodies from 22 providers.
DR DNASU; 55349; -.
DR Ensembl; ENST00000315251.11; ENSP00000319851.5; ENSG00000016391.11.
DR GeneID; 55349; -.
DR KEGG; hsa:55349; -.
DR MANE-Select; ENST00000315251.11; ENSP00000319851.5; NM_018397.5; NP_060867.2.
DR UCSC; uc003dgz.4; human.
DR CTD; 55349; -.
DR DisGeNET; 55349; -.
DR GeneCards; CHDH; -.
DR HGNC; HGNC:24288; CHDH.
DR HPA; ENSG00000016391; Tissue enhanced (kidney, liver).
DR neXtProt; NX_Q8NE62; -.
DR OpenTargets; ENSG00000016391; -.
DR PharmGKB; PA134873121; -.
DR VEuPathDB; HostDB:ENSG00000016391; -.
DR eggNOG; KOG1238; Eukaryota.
DR GeneTree; ENSGT00530000063260; -.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; Q8NE62; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 798314at2759; -.
DR PhylomeDB; Q8NE62; -.
DR TreeFam; TF313911; -.
DR BioCyc; MetaCyc:HS00375-MON; -.
DR BRENDA; 1.1.99.1; 2681.
DR PathwayCommons; Q8NE62; -.
DR Reactome; R-HSA-6798163; Choline catabolism.
DR SignaLink; Q8NE62; -.
DR UniPathway; UPA00529; UER00385.
DR BioGRID-ORCS; 55349; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; CHDH; human.
DR GenomeRNAi; 55349; -.
DR Pharos; Q8NE62; Tbio.
DR PRO; PR:Q8NE62; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NE62; protein.
DR Bgee; ENSG00000016391; Expressed in kidney epithelium and 185 other tissues.
DR ExpressionAtlas; Q8NE62; baseline and differential.
DR Genevisible; Q8NE62; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0008812; F:choline dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042426; P:choline catabolic process; TAS:Reactome.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
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 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..594
FT /note="Choline dehydrogenase, mitochondrial"
FT /id="PRO_0000012329"
FT ACT_SITE 511
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 42..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 436
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 484
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 484
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 496
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 496
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 580
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT VARIANT 40
FT /note="E -> A (in dbSNP:rs9001)"
FT /id="VAR_020421"
FT VARIANT 78
FT /note="L -> R (in dbSNP:rs12676)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055097"
FT VARIANT 441
FT /note="N -> S (in dbSNP:rs34974961)"
FT /id="VAR_049357"
FT CONFLICT 113
FT /note="R -> A (in Ref. 3; CAB75961)"
FT /evidence="ECO:0000305"
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
