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Q61425

- HCDH_MOUSE

UniProt

Q61425 - HCDH_MOUSE

Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

Hadh

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    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 – 571NADBy similarity
    Binding sitei73 – 731Coenzyme ABy similarity
    Binding sitei80 – 801Coenzyme ABy similarity
    Binding sitei122 – 1221NADBy similarity
    Binding sitei127 – 1271NADBy similarity
    Binding sitei149 – 1491Coenzyme ABy similarity
    Binding sitei149 – 1491NADBy similarity
    Sitei170 – 1701Important for catalytic activityBy similarity
    Binding sitei173 – 1731NADBy similarity
    Binding sitei305 – 3051NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 396NADBy 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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1212MitochondrionBy similarityAdd
    BLAST
    Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialPRO_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; alternateBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111S → Y in BAE40188. (PubMed:16141072)Curated
    Sequence conflicti56 – 561V → M in BAE41023. (PubMed:16141072)Curated
    Sequence conflicti111 – 1111H → D in BAA06122. (PubMed:7642117)Curated
    Sequence conflicti146 – 1461S → G in BAE40188. (PubMed:16141072)Curated
    Sequence conflicti211 – 2111C → S in BAA06122. (PubMed:7642117)Curated

    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

    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: October 1, 2014
    This is version 130 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