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Reviewed, UniProtKB/Swiss-Prot Q61425 (HCDH_MOUSE)

Last modified January 19, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
      Short name=HCDH
    EC=1.1.1.35
Alternative name(s):
    Short chain 3-hydroxyacyl-CoA dehydrogenase
    Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Gene names
Name: Hadh
Synonyms: Hadhsc, Mschad, Schad
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from direct assay. Source: MGI

coenzyme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1212Mitochondrion By similarity
Chain13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
PRO_0000007407

Regions

Nucleotide binding34 – 396NAD By similarity

Sites

Binding site571NAD By similarity
Binding site731Coenzyme A By similarity
Binding site801Coenzyme A By similarity
Binding site1221NAD By similarity
Binding site1271NAD By similarity
Binding site1491Coenzyme A By similarity
Binding site1491NAD By similarity
Binding site1731NAD By similarity
Binding site3051NAD By similarity
Site1701Important for catalytic activity By similarity

Amino acid modifications

Modified residue1791N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine Ref.5
Modified residue2411N6-acetyllysine By similarity
Modified residue3121N6-acetyllysine By similarity

Experimental info

Sequence conflict111S → Y in BAE40188. Ref.3
Sequence conflict561V → M in BAE41023. Ref.3
Sequence conflict1111H → D in BAA06122. Ref.1
Sequence conflict1461S → G in BAE40188. Ref.3
Sequence conflict2111C → S in BAA06122. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q61425-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 366A4C075F708BC1

FASTA31434,464
        10         20         30         40         50         60 
MAFVTRQFLR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE 

        70         80         90        100        110        120 
DILAKSKKGI EESLKRMAKK KFTENPKAGD EFVEKTLSCL STSTDAASVV HSTDLVVEAI 

       130        140        150        160        170        180 
VENLKLKNEL FQRLDKFAAE HTIFASNTSS LQITNIANAT TRQDRFAGLH FFNPVPMMKL 

       190        200        210        220        230        240 
VEVIKTPMTS QKTFESLVDF CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLHERGDAS 

       250        260        270        280        290        300 
KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFILDGWHEM EPENPLFQPS PSMNNLVAQK 

       310 
KLGKKTGEGF YKYK

« Hide

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References

« Hide 'large scale' references
[1]"Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA dehydrogenase."
Nomura M., Takihara Y., Shimada K.
Gene 160:309-310(1995) [PubMed: 7642117] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mouse medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase gene."
O'Brien L.K., Sims H.F., Strauss A.W.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Amnion, Extraembryonic tissue, Pancreas and Placenta.
[4]"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].
Tissue: Kidney and Liver.
[5]"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-202, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D29639 mRNA. Translation: BAA06122.1. Different initiation.
AF375597, AF375596 Genomic DNA. Translation: AAK54642.1.
AK132260 mRNA. Translation: BAE21064.1.
AK148486 mRNA. Translation: BAE28581.1.
AK167024 mRNA. Translation: BAE39197.1.
AK168238 mRNA. Translation: BAE40188.1.
AK168877 mRNA. Translation: BAE40695.1.
AK169261 mRNA. Translation: BAE41023.1.
BC028833 mRNA. Translation: AAH28833.1.
BC064712 mRNA. Translation: AAH64712.1.
IPIIPI00121105.
PIRJC4210.
RefSeqNP_032238.2.
UniGeneMm.260164

3D structure databases

SMRQ61425. Positions 24-314.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ61425.

PTM databases

PhosphoSiteQ61425.

2-D gel databases

SWISS-2DPAGEQ61425.
REPRODUCTION-2DPAGEQ61425.

Proteomic databases

PRIDEQ61425.

Genome annotation databases

EnsemblENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984; Mus musculus. [Genome view]
GeneID15107.
KEGGmmu:15107.
NMPDRfig|10090.3.peg.9008.
UCSCuc008rjl.1. mouse.

Organism-specific databases

CTD15107.
MGIMGI:96009. Hadh.

Phylogenomic databases

eggNOGroNOG15739.
HOGENOMHBG691737.
HOVERGENQ61425.
InParanoidQ61425.
OMADTTKFIM.
OrthoDBEOG9G7FJB.
PhylomeDBQ61425.

Enzyme and pathway databases

BRENDA1.1.1.35. 244.

Gene expression databases

ArrayExpressQ61425.
BgeeQ61425.
CleanExMM_HADH.
GenevestigatorQ61425.
GermOnlineENSMUSG00000027984. Mus musculus.

Family and domain databases

InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio287498.
SOURCESearch...

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Entry information

Entry nameHCDH_MOUSE
AccessionPrimary (citable) accession number: Q61425
Secondary accession number(s): Q3TF75 expand/collapse secondary AC list , Q3THK8, Q3UFI0, Q8K149, Q925U9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: January 19, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents