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Q8BJ64 (CHDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline dehydrogenase, mitochondrial
Short name=CDH
Short name=CHD
EC=1.1.99.1
Gene names
Name:Chdh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Choline + acceptor = betaine aldehyde + reduced acceptor.

Cofactor

FAD By similarity.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1.

Subcellular location

Mitochondrion Potential.

Post-translational modification

Acetylation of Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: MGI

   Molecular functioncholine dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 596Choline dehydrogenase, mitochondrialPRO_0000012330

Regions

Nucleotide binding44 – 7330FAD By similarity

Sites

Active site5131 By similarity

Amino acid modifications

Modified residue4981N6-acetyllysine Ref.3

Experimental info

Sequence conflict41V → A in AAH39186. Ref.2
Sequence conflict121W → C in AAH39186. Ref.2
Sequence conflict241Q → R in AAH39186. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BJ64 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D31F19A0E0DB9587

FASTA59666,415
        10         20         30         40         50         60 
MWQVLRGWRK GWQSPRGALA WAVQGQPCPP CSRAVASVGK DEYTFVVVGA GSAGCVLASR 

        70         80         90        100        110        120 
LTEDPNHRVL LLEAGPKDLL MGSKRLQWKI HMPAALVSNL CDDKYNWYYH TEPQPGMDSR 

       130        140        150        160        170        180 
VLYWPRGRVW GGSSSLNAMV YIRGHAEDYN RWHREGAEGW DYAHCLPYFR KAQRHELGAN 

       190        200        210        220        230        240 
MYRGGDGPLH VSRGKTNHPL HQAFLQAARQ AGYPFTEDMN GFQQEGFGWM DMTVHQGKRW 

       250        260        270        280        290        300 
STACAYLHPV LSRPNLRAEV QTLVSRVLFE GTRAVGVEYI KDGQRHKAYV SREVILSGGA 

       310        320        330        340        350        360 
INSPQLLMLS GVGNADDLRK LDIPVVCHLP GVGQNLQDHL EVYVQQACTQ PITLHSAQKP 

       370        380        390        400        410        420 
LRKVCIGLEW LWSYTGDGAT AHLETGGFIR SRPGVPHPDI QFHFLPSQVI DHGRKPTQQE 

       430        440        450        460        470        480 
AYQVHVGTMR ATSVGWLKLR SANPRDHPVI HPNYLSTETD VEDFRQCVRL SREIFAQEAL 

       490        500        510        520        530        540 
APFRGKELQP GSHVQSDKEI DAFVRAKADS AYHPSCTCKM GRSSDPTAVV DAQTKVIGVE 

       550        560        570        580        590 
NLRVVDASIM PSVVSGNLNA PTVMIAEKAA DIIKGHPALE DKNVPVYKPQ TLDTQR

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
[3]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK030900 mRNA. Translation: BAC27176.1.
BC039186 mRNA. Translation: AAH39186.1.
IPIIPI00273146.
RefSeqNP_001129712.1. NM_001136240.1.
NP_758468.2. NM_172264.2.
NP_780552.1. NM_175343.5.
UniGeneMm.259916.

3D structure databases

ProteinModelPortalQ8BJ64.
SMRQ8BJ64. Positions 12-577.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BJ64.

PTM databases

PhosphoSiteQ8BJ64.

Proteomic databases

PRIDEQ8BJ64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067620; ENSMUSP00000065542; ENSMUSG00000015970.
ENSMUST00000118917; ENSMUSP00000112916; ENSMUSG00000015970.
ENSMUST00000167454; ENSMUSP00000130457; ENSMUSG00000015970.
GeneID218865.
KEGGmmu:218865.
UCSCuc007sup.2. mouse.

Organism-specific databases

CTD55349.
MGIMGI:1860776. Chdh.

Phylogenomic databases

GeneTreeENSGT00530000063260.
HOGENOMHBG734713.
HOVERGENHBG023639.
InParanoidQ8BJ64.
OMAERCADFI.
OrthoDBEOG4PK27G.
PhylomeDBQ8BJ64.

Gene expression databases

ArrayExpressQ8BJ64.
BgeeQ8BJ64.
CleanExMM_CHDH.
GenevestigatorQ8BJ64.
GermOnlineENSMUSG00000015970. Mus musculus.

Family and domain databases

InterProIPR011533. Choline_dehydrogenase.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
KOK00108.
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
TIGRFAMsTIGR01810. BetA. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio376465.
SOURCESearch...

Entry information

Entry nameCHDH_MOUSE
AccessionPrimary (citable) accession number: Q8BJ64
Secondary accession number(s): Q8CHT7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents