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Q07417 (ACADS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Short name=SCAD
EC=1.3.8.1
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene names
Name:Acads
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Miscellaneous

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

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion By similarity
Chain25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000499

Regions

Nucleotide binding152 – 16110FAD By similarity
Nucleotide binding185 – 1873FAD By similarity
Nucleotide binding365 – 3695FAD By similarity
Nucleotide binding365 – 3695FAD; shared with dimeric partner By similarity
Nucleotide binding394 – 3963FAD By similarity
Region269 – 2724Substrate binding By similarity

Sites

Active site3921Proton acceptor By similarity
Binding site1611Substrate; via carbonyl oxygen By similarity
Binding site2971FAD By similarity
Binding site2971FAD; shared with dimeric partner By similarity
Binding site3081FAD By similarity
Binding site3931Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict941D → G in AAA16714. Ref.1
Sequence conflict3481A → R in AAA16714. Ref.1
Sequence conflict3691G → S in AAA16714. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07417 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 53DDE98661DF6333

FASTA41244,890
        10         20         30         40         50         60 
MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL 

        70         80         90        100        110        120 
DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRACA STGVIMSVNN 

       130        140        150        160        170        180 
SLYLGPILKF GSAQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN 

       190        200        210        220        230        240 
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN 

       250        260        270        280        290        300 
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF 

       310        320        330        340        350        360 
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS 

       370        380        390        400        410 
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00116591.
PIRI49605.
RefSeqNP_031409.2. NM_007383.3.
UniGeneMm.18759.

3D structure databases

ProteinModelPortalQ07417.
SMRQ07417. Positions 28-411.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031524.

PTM databases

PhosphoSiteQ07417.

2D gel databases

REPRODUCTION-2DPAGEQ07417.

Proteomic databases

PaxDbQ07417.
PRIDEQ07417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031524; ENSMUSP00000031524; ENSMUSG00000029545.
GeneID11409.
KEGGmmu:11409.

Organism-specific databases

CTD35.
MGIMGI:87868. Acads.

Phylogenomic databases

eggNOGCOG1960.
GeneTreeENSGT00680000099623.
HOGENOMHOG000131659.
HOVERGENHBG000224.
InParanoidQ91W85.
KOK00248.
OMAYRDAKLN.
OrthoDBEOG4ZPDVH.

Enzyme and pathway databases

UniPathwayUPA00660.

Gene expression databases

BgeeQ07417.
CleanExMM_ACADS.
GenevestigatorQ07417.
GermOnlineENSMUSG00000029545. Mus musculus.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278650.
SOURCESearch...

Entry information

Entry nameACADS_MOUSE
AccessionPrimary (citable) accession number: Q07417
Secondary accession number(s): Q91W85
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents