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UniProtKB/Swiss-Prot entry P51174


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACADL_MOUSE
Primary accession number P51174
Secondary accession numbers O35302 Q8QZR6 Q9CU29 Q9DB83
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on June 16, 2003 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Long-chain specific acyl-CoA dehydrogenase, mitochondrial [Precursor]
Synonyms LCAD
EC 1.3.99.13
Gene name
Name: Acadl
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1006/geno.1995.1127; PubMed=8530022 [NCBI, ExPASy, EBI, Israel, Japan]
Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A., Tolwani R.J., Wood P.A.;
"RNA expression and chromosomal location of the mouse long-chain acyl-CoA dehydrogenase gene.";
Genomics 28:163-170(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
STRAIN=129/Sv;
DOI=10.1007/s003359900770; PubMed=9545492 [NCBI, ExPASy, EBI, Israel, Japan]
Kurtz D.M., Tolwani R.J., Wood P.A.;
"Structural characterization of the mouse long-chain acyl-CoA dehydrogenase gene and 5' regulatory region.";
Mamm. Genome 9:361-365(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U21489; AAC52329.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005140; BAB23838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK018319; BAB31161.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027412; AAH27412.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF018437; AAC23587.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF018433; AAC23587.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF018435; AAC23587.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF018436; AAC23587.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_031407.2; -.
UniGene Mm.2445
3D structure databases
HSSP Q06319; 1BUC. [HSSP ENTRY / PDB]
ModBase P51174.
Organism-specific databases
MGI MGI:87866; Acadl.
Gene expression databases
ArrayExpress P51174; -.
CleanEx MM_ACADL; -.
GermOnline ENSMUSG00000026003; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR006091; 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 of domain structure.
Gene3D G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.
Pfam PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00072; ACYL_COA_DH_1; 1.
PS00073; ACYL_COA_DH_2; 1.
BLOCKS P51174.
Genome annotation databases
Ensembl ENSMUSG00000026003; Mus musculus. [Contig view]
GeneID 11363; -.
KEGG mmu:11363; -.
Phylogenomic databases
HOGENOM P51174; -.
HOVERGEN P51174; -.
Other
SOURCE Acadl; Mus musculus.
ProtoNet P51174.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    30  30     Mitochondrion (By similarity). 
CHAIN   31   430  400     Long-chain specific acyl-CoA dehydrogenase, mitochondrial. PRO_0000000511
CONFLICT   14    15        KA -> RP (in Ref. 1 and 4). 
CONFLICT   14    14        K -> S (in Ref. 2; BAB23838). 
CONFLICT   19    20        PR -> TL (in Ref. 1). 
CONFLICT   22    22        P -> L (in Ref. 1 and 2; BAB23838). 
CONFLICT   25    25        A -> S (in Ref. 1). 
CONFLICT   32    32        A -> P (in Ref. 1; AAC52329). 
CONFLICT   35    35        R -> G (in Ref. 1; AAC52329). 
CONFLICT   47    47        V -> I (in Ref. 1; AAC52329 and 2; BAB23838). 
CONFLICT   58    58        D -> E (in Ref. 2; BAB31161). 
CONFLICT   131   132        GP -> RA (in Ref. 1; AAC52329). 
CONFLICT   135   135        S -> T (in Ref. 1; AAC52329). 
CONFLICT   225   225        S -> W (in Ref. 1; AAC52329). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 47908 Da [This is the MW of the unprocessed precursor] CRC64: 45CFED51640EAFFB [This is a checksum on the sequence]
        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 

P51174 in FASTA format

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