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Q07417

- ACADS_MOUSE

UniProt

Q07417 - ACADS_MOUSE

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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

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 oxygen By similarity
Binding sitei297 – 2971FAD By similarity
Binding sitei297 – 2971FAD; shared with dimeric partner By similarity
Binding sitei308 – 3081FAD By similarity
Active sitei392 – 3921Proton acceptor By similarity
Binding sitei393 – 3931Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 16110FAD By similarity
Nucleotide bindingi185 – 1873FAD By similarity
Nucleotide bindingi365 – 3695FAD By similarity
Nucleotide bindingi365 – 3695FAD; shared with dimeric partner By similarity
Nucleotide bindingi394 – 3963FAD By 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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion By similarity
Add
BLAST
Chaini25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_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.

Family & Domainsi

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941D → G in AAA16714. 1 Publication
Sequence conflicti348 – 3481A → R in AAA16714. 1 Publication
Sequence conflicti369 – 3691G → S in AAA16714. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 128 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

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