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Long-chain-fatty-acid--CoA ligase 6 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 6) (LACS 6) (Long-chain-fatty-acid--CoA ligase, brain isozyme)

 ACSL6_RAT               Reviewed;         697 AA.
P33124; Q63835; Q6IU14;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=Long-chain-fatty-acid--CoA ligase 6;
EC=6.2.1.3;
AltName: Full=Long-chain acyl-CoA synthetase 6;
Short=LACS 6;
AltName: Full=Long-chain-fatty-acid--CoA ligase, brain isozyme;
Name=Acsl6; Synonyms=Acs2, Facl6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Wistar; TISSUE=Brain;
PubMed=1569043;
Fujino T., Yamamoto T.;
"Cloning and functional expression of a novel long-chain acyl-CoA
synthetase expressed in brain.";
J. Biochem. 111:197-203(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=15683247; DOI=10.1021/bi047721l;
Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A.,
Coleman R.A.;
"Characterization of recombinant long-chain rat acyl-CoA synthetase
isoforms 3 and 6: identification of a novel variant of isoform 6.";
Biochemistry 44:1635-1642(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-160 (ISOFORM 1).
TISSUE=Spinal ganglion;
Amgen EST program;
"Amgen rat EST program.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
RETRACTED PAPER.
TISSUE=Brain;
PubMed=1654331;
Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H.,
Suzuki K., Takenawa T.;
"Molecular cloning and sequencing of cDNA encoding the
phosphatidylinositol kinase from rat brain.";
J. Biol. Chem. 266:17580-17583(1991).
[5]
RETRACTION NOTICE OF PUBMED:1654331.
PubMed=1460058;
Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H.,
Suzuki K., Takenawa T.;
J. Biol. Chem. 267:25620-25620(1992).
[6]
DEVELOPMENTAL STAGE.
PubMed=8973631; DOI=10.1111/j.1432-1033.1996.0186r.x;
Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J.,
Yamamoto T.T.;
"Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2.";
Eur. J. Biochem. 242:186-190(1996).
-!- FUNCTION: Activation of long-chain fatty acids for both synthesis
of cellular lipids, and degradation via beta-oxidation. Plays an
important role in fatty acid metabolism in brain and the acyl-CoAs
produced may be utilized exclusively for the synthesis of the
brain lipid.
-!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
diphosphate + an acyl-CoA.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12210 uM for ATP (Isoform 1) {ECO:0000269|PubMed:15683247};
KM=4.7 uM for CoA (Isoform 1) {ECO:0000269|PubMed:15683247};
KM=6.0 uM for palmitate (Isoform 1)
{ECO:0000269|PubMed:15683247};
KM=3.0 uM for oleate (Isoform 1) {ECO:0000269|PubMed:15683247};
KM=9.7 uM for arachidonate (Isoform 1)
{ECO:0000269|PubMed:15683247};
KM=1480 uM for ATP (Isoform 2) {ECO:0000269|PubMed:15683247};
KM=2.4 uM for CoA (Isoform 2) {ECO:0000269|PubMed:15683247};
KM=3.6 uM for palmitate (Isoform 2)
{ECO:0000269|PubMed:15683247};
KM=5.3 uM for oleate (Isoform 2) {ECO:0000269|PubMed:15683247};
KM=6.5 uM for arachidonate (Isoform 2)
{ECO:0000269|PubMed:15683247};
Vmax=208 nmol/min/mg enzyme with palmitate as substrate (Isoform
1) {ECO:0000269|PubMed:15683247};
Vmax=153 nmol/min/mg enzyme with oleate as substrate (Isoform 1)
{ECO:0000269|PubMed:15683247};
Vmax=139 nmol/min/mg enzyme with arachidonate as substrate
(Isoform 1) {ECO:0000269|PubMed:15683247};
Vmax=739 nmol/min/mg enzyme with palmitate as substrate (Isoform
2) {ECO:0000269|PubMed:15683247};
Vmax=1088 nmol/min/mg enzyme with oleate as substrate (Isoform
2) {ECO:0000269|PubMed:15683247};
Vmax=1212 nmol/min/mg enzyme with arachidonate as substrate
(Isoform 2) {ECO:0000269|PubMed:15683247};
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
Single-pass type III membrane protein {ECO:0000250}. Peroxisome
membrane {ECO:0000250}; Single-pass type III membrane protein
{ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type
III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type III membrane protein
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=ACSL6_vs1;
IsoId=P33124-1; Sequence=Displayed;
Note=Contains exon 14.;
Name=2; Synonyms=ACSL6_vs2;
IsoId=P33124-2; Sequence=VSP_057107, VSP_057108;
Note=Contains exon 13. No differences in the affinity for fatty
acids and CoA. Decreased affinity for ATP. Could play an
important role at lower ATP levels. Expressed at lower level in
the brain compared to isoform 1. {ECO:0000269|PubMed:15683247};
-!- TISSUE SPECIFICITY: Expressed predominantly in brain and, to a
much lesser extent, in heart and adrenal.
-!- DEVELOPMENTAL STAGE: Isoform 1 is detected 10 days after birth,
and increased in a coordinate fashion during the development of
brain, and the amount did not decrease when myelination was
completed. {ECO:0000269|PubMed:8973631}.
-!- MISCELLANEOUS: 5 rat isozymes encoded by different genes have been
described. ACSL6 corresponds to isozyme 2 (ACS2).
{ECO:0000303|PubMed:15683247}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; S56508; AAB19809.2; -; mRNA.
EMBL; D10041; BAA00932.1; -; mRNA.
EMBL; CB582512; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY625254; AAT41589.1; -; mRNA.
PIR; JX0205; JX0205.
RefSeq; NP_570095.1; NM_130739.1.
RefSeq; XP_006246285.1; XM_006246223.3. [P33124-2]
RefSeq; XP_006246286.1; XM_006246224.3. [P33124-2]
UniGene; Rn.33697; -.
ProteinModelPortal; P33124; -.
SMR; P33124; -.
STRING; 10116.ENSRNOP00000055608; -.
SwissLipids; SLP:000001686; -.
iPTMnet; P33124; -.
PhosphoSitePlus; P33124; -.
PaxDb; P33124; -.
PRIDE; P33124; -.
Ensembl; ENSRNOT00000030760; ENSRNOP00000033248; ENSRNOG00000026745. [P33124-1]
GeneID; 117243; -.
KEGG; rno:117243; -.
UCSC; RGD:69403; rat. [P33124-1]
CTD; 23305; -.
RGD; 69403; Acsl6.
eggNOG; KOG1256; Eukaryota.
eggNOG; COG1022; LUCA.
GeneTree; ENSGT00690000101725; -.
HOGENOM; HOG000159459; -.
HOVERGEN; HBG050452; -.
InParanoid; P33124; -.
KO; K01897; -.
PhylomeDB; P33124; -.
BRENDA; 6.2.1.3; 5301.
Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
PRO; PR:P33124; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000026745; Expressed in 6 organ(s), highest expression level in brain.
ExpressionAtlas; P33124; baseline and differential.
Genevisible; P33124; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0015908; P:fatty acid transport; IGI:RGD.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:RGD.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IGI:RGD.
GO; GO:0048666; P:neuron development; IEP:RGD.
GO; GO:0008654; P:phospholipid biosynthetic process; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0010747; P:positive regulation of plasma membrane long-chain fatty acid transport; IMP:RGD.
GO; GO:0009629; P:response to gravity; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Endoplasmic reticulum; Fatty acid metabolism; Ligase;
Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion;
Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 697 Long-chain-fatty-acid--CoA ligase 6.
/FTId=PRO_0000193117.
TRANSMEM 25 45 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 46 697 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 306 319 SQWAPTCADVHFSY -> KVIFPRQDDVLISF (in
isoform 2).
{ECO:0000303|PubMed:15683247}.
/FTId=VSP_057107.
VAR_SEQ 329 330 MV -> VI (in isoform 2).
{ECO:0000303|PubMed:15683247}.
/FTId=VSP_057108.
SEQUENCE 697 AA; 78180 MW; 0B0CA7EFD653E2BE CRC64;
MQTQEILRIL RLPELSDLGQ FFRSLSATTL VSMGALAAIL AYWLTHRPKA LQPPCNLLMQ
SEEVEDSGGA RRSVIGDCTQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPEQPYQW
LSYQEVAKRA EFLGSGLLQH DCKVGTEQFI GVFAQNRPEW IIAELACYTY SMVVVPLYDT
LGPGSIRYII NTADICTVIV DKPHKAILLL EHVERKETPG LKLVILMEPF DDALRERGKK
CGVDIKSMQA IEDSGQENHR VPVPPRPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF
LKVTESQWAP TCADVHFSYL PLAHMFERMV QSVVYCHGGR VGFFQGDIRL LSDDMKALRP
TIFPVVPRLL NRMYDKIFHQ ADTSLKRWLL EFAAKRKQAE VRSGIIRNNS IWDELFFNKI
QASLGGHVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV
GAPLPCNHIK LVDAEELNYW TSKGEGEICV KGPNVFKGYL KDEDRTKEAL DSDGWLHTGD
IGKWLPEGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS EPVAQIYVHG DSLKAFLVGI
VVPDPEVMPC WAQKKGIEGN YQELCKSKEL KKAILDDMVM LGKESGLHSF EQVKAIYIHC
DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM


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