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Q07417

- ACADS_MOUSE

UniProt

Q07417 - ACADS_MOUSE

Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei161 – 1611Substrate; via carbonyl oxygenBy similarity
    Binding sitei297 – 2971FADBy similarity
    Binding sitei297 – 2971FAD; shared with dimeric partnerBy similarity
    Binding sitei308 – 3081FADBy similarity
    Active sitei392 – 3921Proton acceptorBy similarity
    Binding sitei393 – 3931Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi152 – 16110FADBy similarity
    Nucleotide bindingi185 – 1873FADBy similarity
    Nucleotide bindingi365 – 3695FADBy similarity
    Nucleotide bindingi365 – 3695FAD; shared with dimeric partnerBy similarity
    Nucleotide bindingi394 – 3963FADBy similarity

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: InterPro
    2. butyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    3. fatty-acyl-CoA binding Source: Ensembl
    4. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. butyrate catabolic process Source: Ensembl
    2. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
    3. protein homotetramerization Source: Ensembl
    4. response to glucocorticoid Source: Ensembl
    5. response to starvation Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.1)
    Short name:
    SCAD
    Alternative name(s):
    Butyryl-CoA dehydrogenase
    Gene namesi
    Name:Acads
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:87868. Acads.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrial membrane Source: Ensembl
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424MitochondrionBy similarityAdd
    BLAST
    Chaini25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysine; alternate1 Publication
    Modified residuei51 – 511N6-succinyllysine; alternate1 Publication
    Modified residuei72 – 721N6-acetyllysine1 Publication
    Modified residuei129 – 1291N6-acetyllysine; alternate1 Publication
    Modified residuei129 – 1291N6-succinyllysine; alternate1 Publication
    Modified residuei208 – 2081N6-acetyllysine1 Publication
    Modified residuei262 – 2621N6-acetyllysine; alternate1 Publication
    Modified residuei262 – 2621N6-succinyllysine; alternate1 Publication
    Modified residuei292 – 2921N6-acetyllysine1 Publication
    Modified residuei306 – 3061N6-acetyllysine; alternate1 Publication
    Modified residuei306 – 3061N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ07417.
    PaxDbiQ07417.
    PRIDEiQ07417.

    2D gel databases

    REPRODUCTION-2DPAGEQ07417.

    PTM databases

    PhosphoSiteiQ07417.

    Expressioni

    Gene expression databases

    BgeeiQ07417.
    CleanExiMM_ACADS.
    GenevestigatoriQ07417.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiQ07417. 5 interactions.
    MINTiMINT-4086625.
    STRINGi10090.ENSMUSP00000031524.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07417.
    SMRiQ07417. Positions 28-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2724Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    GeneTreeiENSGT00750000117417.
    HOGENOMiHOG000131659.
    HOVERGENiHBG000224.
    InParanoidiQ91W85.
    KOiK00248.
    OMAiMAVAIES.
    OrthoDBiEOG74FF0S.
    TreeFamiTF105019.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q07417-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE    50
    KELVPIAAQL DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI 100
    ALEEISRACA STGVIMSVNN SLYLGPILKF GSAQQKQQWI TPFTNGDKIG 150
    CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS 200
    TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK 250
    ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF 300
    GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL 350
    AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL 400
    VIAGHLLRSY RS 412
    Length:412
    Mass (Da):44,890
    Last modified:July 27, 2011 - v2
    Checksum:i53DDE98661DF6333
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941D → G in AAA16714. (PubMed:8276399)Curated
    Sequence conflicti348 – 3481A → R in AAA16714. (PubMed:8276399)Curated
    Sequence conflicti369 – 3691G → S in AAA16714. (PubMed:8276399)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11163 mRNA. Translation: AAA16714.1.
    AK155361 mRNA. Translation: BAE33217.1.
    AK169428 mRNA. Translation: BAE41170.1.
    CH466529 Genomic DNA. Translation: EDL19883.1.
    BC016259 mRNA. Translation: AAH16259.1.
    CCDSiCCDS19579.1.
    PIRiI49605.
    RefSeqiNP_031409.2. NM_007383.3.
    UniGeneiMm.18759.

    Genome annotation databases

    EnsembliENSMUST00000031524; ENSMUSP00000031524; ENSMUSG00000029545.
    GeneIDi11409.
    KEGGimmu:11409.
    UCSCiuc008zdb.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11163 mRNA. Translation: AAA16714.1 .
    AK155361 mRNA. Translation: BAE33217.1 .
    AK169428 mRNA. Translation: BAE41170.1 .
    CH466529 Genomic DNA. Translation: EDL19883.1 .
    BC016259 mRNA. Translation: AAH16259.1 .
    CCDSi CCDS19579.1.
    PIRi I49605.
    RefSeqi NP_031409.2. NM_007383.3.
    UniGenei Mm.18759.

    3D structure databases

    ProteinModelPortali Q07417.
    SMRi Q07417. Positions 28-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q07417. 5 interactions.
    MINTi MINT-4086625.
    STRINGi 10090.ENSMUSP00000031524.

    PTM databases

    PhosphoSitei Q07417.

    2D gel databases

    REPRODUCTION-2DPAGE Q07417.

    Proteomic databases

    MaxQBi Q07417.
    PaxDbi Q07417.
    PRIDEi Q07417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031524 ; ENSMUSP00000031524 ; ENSMUSG00000029545 .
    GeneIDi 11409.
    KEGGi mmu:11409.
    UCSCi uc008zdb.1. mouse.

    Organism-specific databases

    CTDi 35.
    MGIi MGI:87868. Acads.

    Phylogenomic databases

    eggNOGi COG1960.
    GeneTreei ENSGT00750000117417.
    HOGENOMi HOG000131659.
    HOVERGENi HBG000224.
    InParanoidi Q91W85.
    KOi K00248.
    OMAi MAVAIES.
    OrthoDBi EOG74FF0S.
    TreeFami TF105019.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .

    Miscellaneous databases

    NextBioi 278650.
    PROi Q07417.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q07417.
    CleanExi MM_ACADS.
    Genevestigatori Q07417.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase cDNA."
      Kelly C.L., Hinsdale M.E., Wood P.A.
      Genomics 18:137-140(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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 and NOD.
      Tissue: Heart.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Strain: FVB/N.
      Tissue: Salivary gland.
    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 [LARGE SCALE ANALYSIS] AT LYS-51; LYS-129; LYS-262 AND LYS-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: 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-51; LYS-72; LYS-129; LYS-208; LYS-262; LYS-292 AND LYS-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiACADS_MOUSE
    AccessioniPrimary (citable) accession number: Q07417
    Secondary accession number(s): Q91W85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 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

    Miscellaneous

    A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

    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