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Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain-fatty-acid--CoA ligase, liver isozyme)

 ACSL1_RAT               Reviewed;         699 AA.
P18163;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
EC=6.2.1.3;
AltName: Full=Long-chain acyl-CoA synthetase 1;
Short=LACS 1;
AltName: Full=Long-chain-fatty-acid--CoA ligase, liver isozyme;
Name=Acsl1; Synonyms=Acs1, Acsl2, Facl2;
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], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Wistar; TISSUE=Liver;
PubMed=2341402;
Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S.,
Hashimoto T., Yamamoto T.;
"Structure and regulation of rat long-chain acyl-CoA synthetase.";
J. Biol. Chem. 265:8681-8685(1990).
[2]
PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND
LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=17478130; DOI=10.1016/j.bbapap.2007.03.012;
Distler A.M., Kerner J., Hoppel C.L.;
"Post-translational modifications of rat liver mitochondrial outer
membrane proteins identified by mass spectrometry.";
Biochim. Biophys. Acta 1774:628-636(2007).
[3]
CHARACTERIZATION.
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).
[4]
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).
[5]
GLYCOSYLATION AT SER-136.
PubMed=24098488; DOI=10.1371/journal.pone.0076399;
Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
"Discovery and confirmation of O-GlcNAcylated proteins in rat liver
mitochondria by combination of mass spectrometry and immunological
methods.";
PLoS ONE 8:E76399-E76399(2013).
-!- FUNCTION: Activation of long-chain fatty acids for both synthesis
of cellular lipids, and degradation via beta-oxidation.
Preferentially uses oleate, arachidonate, eicosapentaenoate and
docosahexaenoate as substrates.
-!- 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=649 uM for ATP {ECO:0000269|PubMed:15683247};
KM=6.4 uM for CoA {ECO:0000269|PubMed:15683247};
KM=5.0 uM for palmitate {ECO:0000269|PubMed:15683247};
Vmax=1695 nmol/min/mg enzyme with palmitate as substrate
{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}.
-!- TISSUE SPECIFICITY: Liver, heart, epididymal adipose and to a
lesser extent brain, small intestine and lung.
-!- DEVELOPMENTAL STAGE: Levels remain constant during development.
-!- INDUCTION: By high fat and high carbohydrate diets.
-!- 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; D90109; BAA14136.1; -; mRNA.
PIR; A36275; A36275.
RefSeq; NP_036952.1; NM_012820.1.
RefSeq; XP_006253184.1; XM_006253122.1.
RefSeq; XP_006253185.1; XM_006253123.1.
RefSeq; XP_006253186.1; XM_006253124.2.
RefSeq; XP_006253187.1; XM_006253125.3.
RefSeq; XP_006253188.1; XM_006253126.2.
RefSeq; XP_006253189.1; XM_006253127.1.
RefSeq; XP_008769476.1; XM_008771254.1.
UniGene; Rn.6215; -.
ProteinModelPortal; P18163; -.
SMR; P18163; -.
CORUM; P18163; -.
IntAct; P18163; 28.
STRING; 10116.ENSRNOP00000014235; -.
SwissLipids; SLP:000001018; -.
CarbonylDB; P18163; -.
iPTMnet; P18163; -.
PhosphoSitePlus; P18163; -.
PaxDb; P18163; -.
PRIDE; P18163; -.
Ensembl; ENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
Ensembl; ENSRNOT00000089501; ENSRNOP00000072677; ENSRNOG00000010633.
GeneID; 25288; -.
KEGG; rno:25288; -.
CTD; 2180; -.
RGD; 2015; Acsl1.
eggNOG; KOG1256; Eukaryota.
eggNOG; COG1022; LUCA.
GeneTree; ENSGT00690000101725; -.
HOGENOM; HOG000159459; -.
HOVERGEN; HBG050452; -.
InParanoid; P18163; -.
KO; K01897; -.
OMA; ECVMLCH; -.
PhylomeDB; P18163; -.
TreeFam; TF313877; -.
BioCyc; MetaCyc:MONOMER-14442; -.
BRENDA; 6.2.1.3; 5301.
Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RK; P18163; -.
PRO; PR:P18163; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000010633; Expressed in 10 organ(s), highest expression level in liver.
Genevisible; P18163; RN.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0003987; F:acetate-CoA ligase activity; TAS:RGD.
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:UniProtKB.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; IMP:RGD.
GO; GO:0015908; P:fatty acid transport; IGI:RGD.
GO; GO:0006629; P:lipid metabolic process; TAS:RGD.
GO; GO:0044539; P:long-chain fatty acid import; IEA:Ensembl.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IGI:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0034201; P:response to oleic acid; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
GO; GO:0042178; P:xenobiotic catabolic process; IDA: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;
Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum;
Fatty acid metabolism; Glycoprotein; Ligase; Lipid metabolism;
Magnesium; Membrane; Microsome; Mitochondrion;
Mitochondrion outer membrane; Nitration; Nucleotide-binding;
Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 699 Long-chain-fatty-acid--CoA ligase 1.
/FTId=PRO_0000193106.
TRANSMEM 25 45 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 46 699 Cytoplasmic. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 9 9 Nitrated tyrosine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 85 85 Phosphotyrosine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 86 86 Nitrated tyrosine.
{ECO:0000269|PubMed:17478130}.
MOD_RES 208 208 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 357 357 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 387 387 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000250|UniProtKB:P33121}.
MOD_RES 633 633 N6-acetyllysine.
{ECO:0000269|PubMed:17478130}.
CARBOHYD 136 136 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:24098488}.
SEQUENCE 699 AA; 78179 MW; 6E1EACE0EAE8A85C CRC64;
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ
SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG IQVSNDGPCL GSRKPNQPYE
WISYKQVAEM AECIGSALIQ KGFKPCSEQF IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD
TLGTDAITYI VNKAELSVIF ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ
KCGVEIIGLK ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG
FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ
PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA ELRSGIVRNN SLWDKLIFHK
IQSSLGGKVR LMITGAAPVS ATVLTFLRAA LGCQFYEGYG QTECTAGCCL SLPGDWTAGH
VGAPMPCNYI KLVDVEDMNY QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG
DIGKWLPNGT LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP FEQVKGIAVH
PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI


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