ver.2
Home
|
Help
|
Advanced search
Previous release (v1)
2024-04-27 01:54:03, GGRNA.v2 : RefSeq release 222 (Jan, 2024)
LOCUS NM_012819 1453 bp mRNA linear ROD 21-NOV-2023
DEFINITION Rattus norvegicus acyl-CoA dehydrogenase, long chain (Acadl), mRNA;
nuclear gene for mitochondrial product.
ACCESSION NM_012819
VERSION NM_012819.2
KEYWORDS RefSeq; RefSeq Select.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (bases 1 to 1453)
AUTHORS Martin J, Balmer ML, Rajendran S, Maurhofer O, Dufour JF and
St-Pierre MV.
TITLE Nutritional stress exacerbates hepatic steatosis induced by
deletion of the histidine nucleotide-binding (Hint2) mitochondrial
protein
JOURNAL Am J Physiol Gastrointest Liver Physiol 310 (7), G497-G509 (2016)
PUBMED 26767982
REFERENCE 2 (bases 1 to 1453)
AUTHORS Exil VJ, Silva Avila D, Benedetto A, Exil EA, Adams MR, Au C and
Aschner M.
TITLE Stressed-induced TMEM135 protein is part of a conserved genetic
network involved in fat storage and longevity regulation in
Caenorhabditis elegans
JOURNAL PLoS One 5 (12), e14228 (2010)
PUBMED 21151927
REMARK Publication Status: Online-Only
REFERENCE 3 (bases 1 to 1453)
AUTHORS Goetzman ES, Tian L and Wood PA.
TITLE Differential induction of genes in liver and brown adipose tissue
regulated by peroxisome proliferator-activated receptor-alpha
during fasting and cold exposure in acyl-CoA
dehydrogenase-deficient mice
JOURNAL Mol Genet Metab 84 (1), 39-47 (2005)
PUBMED 15639194
REFERENCE 4 (bases 1 to 1453)
AUTHORS Kwitek AE, Gullings-Handley J, Yu J, Carlos DC, Orlebeke K, Nie J,
Eckert J, Lemke A, Andrae JW, Bromberg S, Pasko D, Chen D, Scheetz
TE, Casavant TL, Soares MB, Sheffield VC, Tonellato PJ and Jacob
HJ.
TITLE High-density rat radiation hybrid maps containing over 24,000
SSLPs, genes, and ESTs provide a direct link to the rat genome
sequence
JOURNAL Genome Res 14 (4), 750-757 (2004)
PUBMED 15060019
REFERENCE 5 (bases 1 to 1453)
AUTHORS Ghisla S and Thorpe C.
TITLE Acyl-CoA dehydrogenases. A mechanistic overview
JOURNAL Eur J Biochem 271 (3), 494-508 (2004)
PUBMED 14728676
REMARK Review article
REFERENCE 6 (bases 1 to 1453)
AUTHORS Willard J, Vicanek C, Battaile KP, Van Veldhoven PP, Fauq AH, Rozen
R and Vockley J.
TITLE Cloning of a cDNA for short/branched chain acyl-Coenzyme A
dehydrogenase from rat and characterization of its tissue
expression and substrate specificity
JOURNAL Arch Biochem Biophys 331 (1), 127-133 (1996)
PUBMED 8660691
REFERENCE 7 (bases 1 to 1453)
AUTHORS Hainline BE, Kahlenbeck DJ, Grant J and Strauss AW.
TITLE Tissue specific and developmental expression of rat long-and
medium-chain acyl-CoA dehydrogenases
JOURNAL Biochim Biophys Acta 1216 (3), 460-468 (1993)
PUBMED 8268228
REFERENCE 8 (bases 1 to 1453)
AUTHORS Matsubara Y, Indo Y, Naito E, Ozasa H, Glassberg R, Vockley J,
Ikeda Y, Kraus J and Tanaka K.
TITLE Molecular cloning and nucleotide sequence of cDNAs encoding the
precursors of rat long chain acyl-coenzyme A, short chain
acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence
homology of four enzymes of the acyl-CoA dehydrogenase family
JOURNAL J Biol Chem 264 (27), 16321-16331 (1989)
PUBMED 2777793
REFERENCE 9 (bases 1 to 1453)
AUTHORS Ikeda,Y., Keese,S.M., Fenton,W.A. and Tanaka,K.
TITLE Biosynthesis of four rat liver mitochondrial acyl-CoA
dehydrogenases: in vitro synthesis, import into mitochondria, and
processing of their precursors in a cell-free system and in
cultured cells
JOURNAL Arch Biochem Biophys 252 (2), 662-674 (1987)
PUBMED 3813556
REFERENCE 10 (bases 1 to 1453)
AUTHORS Ikeda,Y., Okamura-Ikeda,K. and Tanaka,K.
TITLE Purification and characterization of short-chain, medium-chain, and
long-chain acyl-CoA dehydrogenases from rat liver mitochondria.
Isolation of the holo- and apoenzymes and conversion of the
apoenzyme to the holoenzyme
JOURNAL J Biol Chem 260 (2), 1311-1325 (1985)
PUBMED 3968063
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from
JACYVU010000215.1.
On Nov 27, 2020 this sequence version replaced NM_012819.1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: L11276.1, BC062006.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA5760400, SAMN06621351
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
gene product(s) localized to mito. :: inferred from homology
RefSeq Select criteria :: based on single
protein-coding transcript
##RefSeq-Attributes-END##
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-83 JACYVU010000215.1 1441758-1441840 c
84-239 JACYVU010000215.1 1437106-1437261 c
240-377 JACYVU010000215.1 1433929-1434066 c
378-542 JACYVU010000215.1 1432304-1432468 c
543-609 JACYVU010000215.1 1424014-1424080 c
610-774 JACYVU010000215.1 1419836-1420000 c
775-876 JACYVU010000215.1 1419212-1419313 c
877-990 JACYVU010000215.1 1418168-1418281 c
991-1118 JACYVU010000215.1 1410695-1410822 c
1119-1205 JACYVU010000215.1 1409200-1409286 c
1206-1453 JACYVU010000215.1 1403672-1403919 c
FEATURES Location/Qualifiers
source 1..1453
/organism="Rattus norvegicus"
/mol_type="mRNA"
/strain="BN"
/db_xref="taxon:10116"
/chromosome="9"
/map="9q32"
gene 1..1453
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="acyl-CoA dehydrogenase, long chain"
/db_xref="GeneID:25287"
/db_xref="RGD:2011"
exon 1..83
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
CDS 7..1299
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/EC_number="1.3.8.8"
/note="long-chain specific acyl-CoA dehydrogenase,
mitochondrial; Acyl Coenzyme A dehydrogenase, long chain;
acetyl-Coenzyme A dehydrogenase, long-chain; long-chain
acyl-CoA dehydrogenase; LCAD long chain acyl-CoA
dehydrogenase; acyl-Coenzyme A dehydrogenase, long-chain"
/codon_start=1
/product="long-chain specific acyl-CoA dehydrogenase,
mitochondrial precursor"
/protein_id="NP_036951.1"
/db_xref="GeneID:25287"
/db_xref="RGD:2011"
/translation="
MAARLLLRSLRVLSARSATLPPPSARCSHSGAEARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPYHEEWEKAGEVSRELWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEQFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGKKLHKMGMKAQDTAELFFEDVRLPASALLGEENKGFYYLMQELPQERLLIADLAISACEFMFEETRNYVRQRKAFGKTVAHIQTVQHKLAELKTNICVTRAFVDSCLQLHETKRLDSASASMAKYWASELQNTVAYQCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS"
transit_peptide 7..96
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Mitochondrion.
/evidence=ECO:0000269|PubMed:2777793; propagated from
UniProtKB/Swiss-Prot (P15650.1)"
mat_peptide 97..1296
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/product="Long-chain specific acyl-CoA dehydrogenase,
mitochondrial. /id=PRO_0000000513"
/note="propagated from UniProtKB/Swiss-Prot (P15650.1)"
misc_feature 130..132
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 166..168
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (P15650.1); phosphorylation site"
misc_feature 169..171
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (P15650.1); phosphorylation site"
misc_feature 172..1287
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Long chain acyl-CoA dehydrogenase; Region: LCAD;
cd01160"
/db_xref="CDD:173849"
misc_feature 202..204
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 247..249
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 280..282
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 289..291
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature order(514..516,520..525,538..543,613..615,619..621,
1222..1224,1243..1245,1249..1251)
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="FAD binding site [chemical binding]; other site"
/db_xref="CDD:173849"
misc_feature order(541..543,847..849,868..870,880..882,1234..1239)
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="substrate binding pocket [chemical binding]; other
site"
/db_xref="CDD:173849"
misc_feature 577..579
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); phosphorylation site"
misc_feature 766..768
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 841..843
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 877..879
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="catalytic base [active]"
/db_xref="CDD:173849"
misc_feature 958..960
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 970..972
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 1078..1080
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); acetylation site"
misc_feature 1090..1092
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P51174; propagated from
UniProtKB/Swiss-Prot (P15650.1); phosphorylation site"
exon 84..239
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 240..377
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 378..542
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 543..609
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 610..774
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 775..876
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 877..990
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 991..1118
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 1119..1205
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
exon 1206..1453
/gene="Acadl"
/gene_synonym="ACOADA; LCAD"
/inference="alignment:Splign:2.1.0"
ORIGIN
cccgccatggctgcgcgcctgctcctccgctcccttcgtgtcctgagcgcccgctcggcgacactcccgccgccctccgcccgatgttctcattctggagcagaagcacgtctagaaactccttctgctaaaaaattaactgatattggaatcagaagaatcttttcctcagagcatgacattttccgggagagtgtaaggaagttttttcaagaagaagtgattccctaccacgaagaatgggagaaagccggagaagtgagtagagagctctgggaaaaagctggcaagcaaggcctgcttggcatcaacattgcagagaaacatggcggcatcggtggggacttgttgtcaacagcagttacttgggaagagcaagcatactcaaattgcacaggccctggtttcagcctccattcagatattgtcatgccctatattgcaaattacggcacaaaagaacagatcgagcagtttatcccccagatgacggcgggcaagtgtattggtgccatagccatgacagagcctggggctggaagtgacttacaaggagtaagaacaaatgccaaaaggtctgggagtgattggattctcaatggaagcaaggtgttcatcactaatggctggttaagtgatctcgtgatcgtagtggccgtcaccaatcgtgaagctcgatcgcccgctcatggcattagcctctttttggtggagaatggaatgaaaggatttattaagggcaagaagctacataagatgggaatgaaagcccaggacacagcagaactattctttgaagatgttcgattgccagctagtgccctacttggggaagagaataaaggcttctactacctcatgcaagagctcccacaggaaaggcttttaattgctgatttggcaatttctgcctgtgagttcatgtttgaagaaaccaggaactacgtgagacaaagaaaggcttttggaaaaacagtcgcacacatccagactgtgcagcacaaactagcagaattgaagacgaacatatgtgttaccagagcttttgtggacagctgcctacagctgcatgaaaccaaacgtctggactccgcctccgcttccatggcgaaatattgggcatctgaattacaaaacactgtagcttatcagtgtgttcaactccatggaggctggggttacatgtgggaatacccgattgcaaaagcctacgtggatgctcgagttcagccgatctacggtggtaccaacgaaatcatgaaagagctgatcgcaagacagatcgtcagtgacagctagacatctgcctacatcctgaaatcctactacatcacagctaatccggattcaaatatacttgagataaagtggaacctggaagggggggggggtagtaaagctggttttatgtatggttgttacagagaaagaaataaaagaattataaagattg
//
by
@meso_cacase at
DBCLS
This page is licensed under a
Creative Commons Attribution 4.0 International License (CC BY 4.0).
If you use GGRNA in your work, please cite:
Naito Y, Bono H. (2012)
GGRNA: an ultrafast, transcript-oriented search engine for genes and transcripts.
Nucleic Acids Res., 40, W592-W596.
[Full Text]