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Q61425 (HCDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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

Names and origin

Protein namesRecommended name:
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Short name=HCDH
EC=1.1.1.35
Alternative name(s):
Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene names
Name:Hadh
Synonyms:Hadhsc, Mschad, Schad
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

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.

Post-translational modification

Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5. Ref.5

Sequence similarities

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence caution

The sequence BAA06122.1 differs from that shown. Reason: Erroneous initiation.

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 residue751N6-acetyllysine Ref.6
Modified residue801N6-succinyllysine Ref.5
Modified residue811N6-acetyllysine; alternate Ref.6
Modified residue811N6-succinyllysine; alternate Ref.5
Modified residue871N6-acetyllysine; alternate Ref.6
Modified residue871N6-succinyllysine; alternate Ref.5
Modified residue1251N6-acetyllysine Ref.6
Modified residue1361N6-acetyllysine; alternate Ref.6
Modified residue1361N6-succinyllysine; alternate Ref.5
Modified residue1791N6-acetyllysine Ref.6
Modified residue1851N6-acetyllysine; alternate Ref.6
Modified residue1851N6-succinyllysine; alternate Ref.5
Modified residue1921N6-acetyllysine; alternate Ref.6
Modified residue1921N6-succinyllysine; alternate Ref.5
Modified residue2021N6-acetyllysine; alternate Ref.6
Modified residue2021N6-succinyllysine; alternate Ref.5
Modified residue2061N6-succinyllysine Ref.5
Modified residue2121N6-acetyllysine; alternate Ref.6
Modified residue2121N6-succinyllysine; alternate Ref.5
Modified residue2411N6-acetyllysine; alternate Ref.5 Ref.6
Modified residue2411N6-succinyllysine; alternate Ref.5
Modified residue3121N6-acetyllysine; alternate By similarity
Modified residue3121N6-succinyllysine; alternate Ref.5

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

Sequences

Sequence LengthMass (Da)Tools
Q61425 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney and Liver.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-81, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-81; LYS-87; LYS-136; LYS-185; LYS-192; LYS-202; LYS-206; LYS-212; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-81; LYS-87; LYS-125; LYS-136; LYS-179; LYS-185; LYS-192; LYS-202; LYS-212 AND LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

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.
PIRJC4210.
RefSeqNP_032238.2. NM_008212.4.
UniGeneMm.260164.

3D structure databases

ProteinModelPortalQ61425.
SMRQ61425. Positions 23-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61425. 4 interactions.
MINTMINT-1859897.

PTM databases

PhosphoSiteQ61425.

2D gel databases

REPRODUCTION-2DPAGEQ61425.
SWISS-2DPAGEQ61425.

Proteomic databases

PaxDbQ61425.
PRIDEQ61425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984.
GeneID15107.
KEGGmmu:15107.
UCSCuc008rjl.1. mouse.

Organism-specific databases

CTD3033.
MGIMGI:96009. Hadh.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00720000108673.
HOGENOMHOG000141498.
HOVERGENHBG000832.
InParanoidQ61425.
KOK00022.
OMAAGFVTTR.
OrthoDBEOG7K3TMS.
PhylomeDBQ61425.
TreeFamTF300886.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

BgeeQ61425.
CleanExMM_HADH.
GenevestigatorQ61425.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR022694. 3-OHacyl-CoA_DH.
IPR006180. 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]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFPIRSF000105. HCDH. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHADH. mouse.
NextBio287498.
PROQ61425.
SOURCESearch...

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: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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