Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07417

- ACADS_MOUSE

UniProt

Q07417 - ACADS_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 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
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 membrane Source: Ensembl
  2. mitochondrion Source: MGI
  3. nucleus Source: Ensembl
Complete GO annotation...

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.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiQ07417.
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

        10         20         30         40         50
MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE
60 70 80 90 100
KELVPIAAQL DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI
110 120 130 140 150
ALEEISRACA STGVIMSVNN SLYLGPILKF GSAQQKQQWI TPFTNGDKIG
160 170 180 190 200
CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS
210 220 230 240 250
TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK
260 270 280 290 300
ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF
310 320 330 340 350
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL
360 370 380 390 400
AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL
410
VIAGHLLRSY RS
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 ENSGT00760000119007.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi Q07417.
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: October 29, 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

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