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Q61425

- HCDH_MOUSE

UniProt

Q61425 - HCDH_MOUSE

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Protein
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Gene
Hadh, Hadhsc, Mschad, Schad
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD By similarity
Binding sitei73 – 731Coenzyme A By similarity
Binding sitei80 – 801Coenzyme A By similarity
Binding sitei122 – 1221NAD By similarity
Binding sitei127 – 1271NAD By similarity
Binding sitei149 – 1491Coenzyme A By similarity
Binding sitei149 – 1491NAD By similarity
Sitei170 – 1701Important for catalytic activity By similarity
Binding sitei173 – 1731NAD By similarity
Binding sitei305 – 3051NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: MGI
  2. NAD+ binding Source: InterPro

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
  2. negative regulation of insulin secretion Source: Ensembl
  3. response to activity Source: Ensembl
  4. response to drug Source: Ensembl
  5. response to insulin Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (EC:1.1.1.35)
Short name:
HCDH
Alternative name(s):
Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene namesi
Name:Hadh
Synonyms:Hadhsc, Mschad, Schad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:96009. Hadh.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1212Mitochondrion By similarity
Add
BLAST
Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
PRO_0000007407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysine1 Publication
Modified residuei80 – 801N6-succinyllysine1 Publication
Modified residuei81 – 811N6-acetyllysine; alternate1 Publication
Modified residuei81 – 811N6-succinyllysine; alternate1 Publication
Modified residuei87 – 871N6-acetyllysine; alternate1 Publication
Modified residuei87 – 871N6-succinyllysine; alternate1 Publication
Modified residuei125 – 1251N6-acetyllysine1 Publication
Modified residuei136 – 1361N6-acetyllysine; alternate1 Publication
Modified residuei136 – 1361N6-succinyllysine; alternate1 Publication
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternate1 Publication
Modified residuei192 – 1921N6-acetyllysine; alternate1 Publication
Modified residuei192 – 1921N6-succinyllysine; alternate1 Publication
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Modified residuei202 – 2021N6-succinyllysine; alternate1 Publication
Modified residuei206 – 2061N6-succinyllysine1 Publication
Modified residuei212 – 2121N6-acetyllysine; alternate1 Publication
Modified residuei212 – 2121N6-succinyllysine; alternate1 Publication
Modified residuei241 – 2411N6-acetyllysine; alternate2 Publications
Modified residuei241 – 2411N6-succinyllysine; alternate1 Publication
Modified residuei312 – 3121N6-acetyllysine; alternate By similarity
Modified residuei312 – 3121N6-succinyllysine; alternate1 Publication

Post-translational modificationi

Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ61425.
PaxDbiQ61425.
PRIDEiQ61425.

2D gel databases

REPRODUCTION-2DPAGEQ61425.
SWISS-2DPAGEQ61425.

PTM databases

PhosphoSiteiQ61425.

Expressioni

Gene expression databases

BgeeiQ61425.
CleanExiMM_HADH.
GenevestigatoriQ61425.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiQ61425. 4 interactions.
MINTiMINT-1859897.

Structurei

3D structure databases

ProteinModelPortaliQ61425.
SMRiQ61425. Positions 23-314.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ61425.
KOiK00022.
OMAiDTKYRAC.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ61425.
TreeFamiTF300886.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR022694. 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]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000105. HCDH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61425-1 [UniParc]FASTAAdd to Basket

« Hide

MAFVTRQFLR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG    50
HTVVLVDQTE DILAKSKKGI EESLKRMAKK KFTENPKAGD EFVEKTLSCL 100
STSTDAASVV HSTDLVVEAI VENLKLKNEL FQRLDKFAAE HTIFASNTSS 150
LQITNIANAT TRQDRFAGLH FFNPVPMMKL VEVIKTPMTS QKTFESLVDF 200
CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLHERGDAS KEDIDTAMKL 250
GAGYPMGPFE LLDYVGLDTT KFILDGWHEM EPENPLFQPS PSMNNLVAQK 300
KLGKKTGEGF YKYK 314
Length:314
Mass (Da):34,464
Last modified:June 6, 2002 - v2
Checksum:i366A4C075F708BC1
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → Y in BAE40188. 1 Publication
Sequence conflicti56 – 561V → M in BAE41023. 1 Publication
Sequence conflicti111 – 1111H → D in BAA06122. 1 Publication
Sequence conflicti146 – 1461S → G in BAE40188. 1 Publication
Sequence conflicti211 – 2111C → S in BAA06122. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS38640.1.
PIRiJC4210.
RefSeqiNP_032238.2. NM_008212.4.
UniGeneiMm.260164.

Genome annotation databases

EnsembliENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984.
GeneIDi15107.
KEGGimmu:15107.
UCSCiuc008rjl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS38640.1.
PIRi JC4210.
RefSeqi NP_032238.2. NM_008212.4.
UniGenei Mm.260164.

3D structure databases

ProteinModelPortali Q61425.
SMRi Q61425. Positions 23-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61425. 4 interactions.
MINTi MINT-1859897.

PTM databases

PhosphoSitei Q61425.

2D gel databases

REPRODUCTION-2DPAGE Q61425.
SWISS-2DPAGE Q61425.

Proteomic databases

MaxQBi Q61425.
PaxDbi Q61425.
PRIDEi Q61425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029610 ; ENSMUSP00000029610 ; ENSMUSG00000027984 .
GeneIDi 15107.
KEGGi mmu:15107.
UCSCi uc008rjl.1. mouse.

Organism-specific databases

CTDi 3033.
MGIi MGI:96009. Hadh.

Phylogenomic databases

eggNOGi COG1250.
GeneTreei ENSGT00720000108673.
HOGENOMi HOG000141498.
HOVERGENi HBG000832.
InParanoidi Q61425.
KOi K00022.
OMAi DTKYRAC.
OrthoDBi EOG7K3TMS.
PhylomeDBi Q61425.
TreeFami TF300886.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

ChiTaRSi HADH. mouse.
NextBioi 287498.
PROi Q61425.
SOURCEi Search...

Gene expression databases

Bgeei Q61425.
CleanExi MM_HADH.
Genevestigatori Q61425.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR022694. 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 ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000105. HCDH. 1 hit.
SUPFAMi SSF48179. SSF48179. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHCDH_MOUSE
AccessioniPrimary (citable) accession number: Q61425
Secondary accession number(s): Q3TF75
, Q3THK8, Q3UFI0, Q8K149, Q925U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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