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Reviewed, UniProtKB/Swiss-Prot P51174 (ACADL_MOUSE)

Last modified November 25, 2008. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Long-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=LCAD
    EC=1.3.99.13
Gene names
Name: Acadl
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

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.

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Ontologies

Keywords

   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

long-chain-acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 430400Long-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000511

Experimental info

Sequence conflict14 – 152KA → RP Ref.1 Ref.4
Sequence conflict141K → S in BAB23838. Ref.2
Sequence conflict19 – 202PR → TL Ref.1
Sequence conflict221P → L in BAB23838. Ref.1 Ref.2
Sequence conflict251A → S Ref.1
Sequence conflict321A → P in AAC52329. Ref.1
Sequence conflict351R → G in AAC52329. Ref.1
Sequence conflict471V → I in AAC52329. Ref.1
Sequence conflict471V → I in BAB23838. Ref.2
Sequence conflict581D → E in BAB31161. Ref.2
Sequence conflict131 – 1322GP → RA in AAC52329. Ref.1
Sequence conflict1351S → T in AAC52329. Ref.1
Sequence conflict2251S → W in AAC52329. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P51174-1 [UniParc].

Last modified June 16, 2003. Version 2.
Checksum: 45CFED51640EAFFB

FASTA43047,908
        10         20         30         40         50         60 
MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR RIFSSEHDIF 

        70         80         90        100        110        120 
RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT 

       130        140        150        160        170        180 
WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD 

       190        200        210        220        230        240 
LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK 

       250        260        270        280        290        300 
GFIKGRKLHK MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI 

       310        320        330        340        350        360 
SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS CLQLHETKRL 

       370        380        390        400        410        420 
DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE 

       430 
LIARQIVSDS

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References

« Hide 'large scale' references
[1]"RNA expression and chromosomal location of the mouse long-chain acyl-CoA dehydrogenase gene."
Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A., Tolwani R.J., Wood P.A.
Genomics 28:163-170(1995) [PubMed: 8530022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Structural characterization of the mouse long-chain acyl-CoA dehydrogenase gene and 5' regulatory region."
Kurtz D.M., Tolwani R.J., Wood P.A.
Mamm. Genome 9:361-365(1998) [PubMed: 9545492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
Strain: 129/Sv.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U21489 mRNA. Translation: AAC52329.1.
AK005140 mRNA. Translation: BAB23838.1.
AK018319 mRNA. Translation: BAB31161.1.
BC027412 mRNA. Translation: AAH27412.1.
AF018437 expand/collapse EMBL AC list , AF018433, AF018435, AF018436 Genomic DNA. Translation: AAC23587.1.
RefSeqNP_031407.2.
UniGeneMm.2445

3D structure databases

HSSPHSSP built from PDB template 1BUC based on UniProtKB Q06319.
ModBaseSearch...

PTM databases

PhosphoSiteP51174.

Genome annotation databases

EnsemblENSMUSG00000026003. Mus musculus. [Contig view]
GeneID11363.
KEGGmmu:11363.

Organism-specific databases

MGIMGI:87866. Acadl.

Phylogenomic databases

HOGENOMP51174.
HOVERGENP51174.

Gene expression databases

ArrayExpressP51174.
CleanExMM_ACADL.
GermOnlineENSMUSG00000026003. Mus musculus.

Family and domain databases

InterProIPR006091. Acyl-CoA_DHase/Oxase_M.
IPR006089. Acyl-CoA_DHase_CS.
IPR006092. Acyl-CoA_DHase_N.
IPR006090. Acyl-CoA_Oxase/DHase_1.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio278636.
SOURCESearch...

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Entry information

Entry nameACADL_MOUSE
AccessionPrimary (citable) accession number: P51174
Secondary accession number(s): O35302 expand/collapse secondary AC list , Q8QZR6, Q9CU29, Q9DB83
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 16, 2003
Last modified: November 25, 2008
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents