CHDH_RAT
ID CHDH_RAT Reviewed; 599 AA.
AC Q6UPE0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Choline dehydrogenase, mitochondrial;
DE Short=CDH;
DE Short=CHD;
DE EC=1.1.99.1 {ECO:0000305|PubMed:12951056};
DE Flags: Precursor;
GN Name=Chdh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-48, TRANSIT PEPTIDE
RP CLEAVAGE SITE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12951056; DOI=10.1016/j.bbrc.2003.08.010;
RA Huang S., Lin Q.;
RT "Functional expression and processing of rat choline dehydrogenase
RT precursor.";
RL Biochem. Biophys. Res. Commun. 309:344-350(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 -!- 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 Evidence={ECO:0000305|PubMed:12951056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17434;
CC Evidence={ECO:0000305|PubMed:12951056};
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:12951056}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12951056}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY365023; AAQ67365.1; -; mRNA.
DR EMBL; CH474046; EDL89007.1; -; Genomic_DNA.
DR EMBL; BC085787; AAH85787.1; -; mRNA.
DR RefSeq; NP_942026.1; NM_198731.2.
DR RefSeq; XP_006252640.1; XM_006252578.3.
DR RefSeq; XP_006252641.1; XM_006252579.3.
DR RefSeq; XP_006252642.1; XM_006252580.2.
DR RefSeq; XP_008769206.1; XM_008770984.2.
DR RefSeq; XP_008769207.1; XM_008770985.2.
DR AlphaFoldDB; Q6UPE0; -.
DR SMR; Q6UPE0; -.
DR STRING; 10116.ENSRNOP00000021407; -.
DR iPTMnet; Q6UPE0; -.
DR PhosphoSitePlus; Q6UPE0; -.
DR PaxDb; Q6UPE0; -.
DR PRIDE; Q6UPE0; -.
DR Ensembl; ENSRNOT00000021407; ENSRNOP00000021407; ENSRNOG00000015859.
DR GeneID; 290551; -.
DR KEGG; rno:290551; -.
DR UCSC; RGD:735166; rat.
DR CTD; 55349; -.
DR RGD; 735166; Chdh.
DR eggNOG; KOG1238; Eukaryota.
DR GeneTree; ENSGT00530000063260; -.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; Q6UPE0; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 798314at2759; -.
DR PhylomeDB; Q6UPE0; -.
DR TreeFam; TF313911; -.
DR BRENDA; 1.1.99.1; 5301.
DR Reactome; R-RNO-6798163; Choline catabolism.
DR UniPathway; UPA00529; UER00385.
DR PRO; PR:Q6UPE0; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Proteomes; UP000234681; Chromosome 16.
DR Bgee; ENSRNOG00000015859; Expressed in liver and 15 other tissues.
DR Genevisible; Q6UPE0; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0008812; F:choline dehydrogenase activity; IMP:RGD.
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; 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; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12951056"
FT CHAIN 35..599
FT /note="Choline dehydrogenase, mitochondrial"
FT /id="PRO_0000418439"
FT ACT_SITE 516
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 47..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 441
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 501
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
FT MOD_RES 501
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ64"
SQ SEQUENCE 599 AA; 66389 MW; 8ECDC1089B6236D0 CRC64;
MWQVLRSWSK RCLSPRGALA WAAQGQPRPP CSCAVASAAS GGKDEYTFIV VGAGSAGCVL
ANRLTEDPNH RVLLLEAGPK DLLMGSKRLQ WKIHMPAALV ANLCDDKYNW YYHTEAQPGL
DGRVLYWPRG RVWGGSSSLN AMVYIRGHAE DYNRWHRQGA EGWDYAHCLP YFRKAQKHEL
GANMYRGGDG PLHVSRGKTN HPLHQAFLQA ARQAGYPFTE DMNGFQQEGF GWMDMTIHQG
KRWSTASAYL RPALSRPNLR AEVQTLVSRV LFEGTRAVGV EYIKDGQSHK AYVSREVILS
GGAINSPQLL MLSGVGNADD LKKLGIPVVC HLPGVGQNLQ DHLEIYIQHA CTQPITLHSA
QKPLRKVCIG LEWLWRFTGD GATAHLETGG FIRSRPGVPH PDIQFHFLPS QVIDHGRKPT
QQEAYQVHVG TMRATSVGWL KLRSTNPQDH PMINPNYLST ETDVEDFRQC VKLTREIFAQ
EAFAPFRGKE LQPGSHVQSD KEIDAFVRAK ADSAYHPSCT CKMGQPSDPT AVVDQQTRVI
GVENLRVIDA SIMPSVVSGN LNAPTIMIAE KAADVIKGCP ALGDENVPVY KPQTLDTQR
