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P18163

- ACSL1_RAT

UniProt

P18163 - ACSL1_RAT

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Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

Acsl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Kineticsi

  1. KM=649 µM for ATP1 Publication
  2. KM=6.4 µM for CoA1 Publication
  3. KM=5.0 µM for palmitate1 Publication

Vmax=1695 nmol/min/mg enzyme with palmitate as substrate1 Publication

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: Ensembl
  2. fatty acid metabolic process Source: RGD
  3. fatty acid transport Source: RGD
  4. lipid biosynthetic process Source: Ensembl
  5. lipid metabolic process Source: RGD
  6. long-chain fatty acid import Source: Ensembl
  7. long-chain fatty acid metabolic process Source: GOC
  8. positive regulation of protein serine/threonine kinase activity Source: Ensembl
  9. response to drug Source: RGD
  10. response to nutrient Source: RGD
  11. response to oleic acid Source: RGD
  12. response to organic cyclic compound Source: RGD
  13. response to organic substance Source: RGD
  14. triglyceride metabolic process Source: RGD
  15. xenobiotic catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14442.
BRENDAi6.2.1.3. 5301.
ReactomeiREACT_196408. PPARA activates gene expression.
REACT_198818. alpha-linolenic acid (ALA) metabolism.
REACT_198820. Linoleic acid (LA) metabolism.
REACT_232376. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RKP18163.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 1 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 1
Short name:
LACS 1
Long-chain-fatty-acid--CoA ligase, liver isozyme
Gene namesi
Name:Acsl1
Synonyms:Acs1, Acsl2, Facl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi2015. Acsl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 4521Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini46 – 699654CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: RGD
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: RGD
  4. peroxisomal membrane Source: HGNC
  5. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Long-chain-fatty-acid--CoA ligase 1PRO_0000193106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei9 – 91Nitrated tyrosine1 Publication
Modified residuei85 – 851Phosphotyrosine1 Publication
Modified residuei86 – 861Nitrated tyrosine1 Publication
Glycosylationi136 – 1361O-linked (GlcNAc)1 Publication
Modified residuei208 – 2081N6-acetyllysineBy similarity
Modified residuei357 – 3571N6-acetyllysineBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei633 – 6331N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP18163.
PRIDEiP18163.

PTM databases

PhosphoSiteiP18163.

Expressioni

Tissue specificityi

Liver, heart, epididymal adipose and to a lesser extent brain, small intestine and lung.

Developmental stagei

Levels remain constant during development.

Inductioni

By high fat and high carbohydrate diets.

Gene expression databases

GenevestigatoriP18163.

Interactioni

Protein-protein interaction databases

IntActiP18163. 28 interactions.
MINTiMINT-4570488.
STRINGi10116.ENSRNOP00000014235.

Structurei

3D structure databases

ProteinModelPortaliP18163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP18163.
KOiK01897.
OMAiWDRLIFH.
OrthoDBiEOG71CFKN.
PhylomeDBiP18163.
TreeFamiTF313877.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18163-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA
60 70 80 90 100
LKPPCDLSMQ SVEVTGTTEG VRRSAVLEDD KLLLYYYDDV RTMYDGFQRG
110 120 130 140 150
IQVSNDGPCL GSRKPNQPYE WISYKQVAEM AECIGSALIQ KGFKPCSEQF
160 170 180 190 200
IGIFSQNRPE WVTIEQGCFT YSMVVVPLYD TLGTDAITYI VNKAELSVIF
210 220 230 240 250
ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YDNDLVERGQ KCGVEIIGLK
260 270 280 290 300
ALEDLGRVNR TKPKPPEPED LAIICFTSGT TGNPKGAMVT HQNIMNDCSG
310 320 330 340 350
FIKATESAFI ASPEDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR
360 370 380 390 400
LLMDDLKVLQ PTIFPVVPRL LNRMFDRIFG QANTSVKRWL LDFASKRKEA
410 420 430 440 450
ELRSGIVRNN SLWDKLIFHK IQSSLGGKVR LMITGAAPVS ATVLTFLRAA
460 470 480 490 500
LGCQFYEGYG QTECTAGCCL SLPGDWTAGH VGAPMPCNYI KLVDVEDMNY
510 520 530 540 550
QAAKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG DIGKWLPNGT
560 570 580 590 600
LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
610 620 630 640 650
IVVPDVEILP SWAQKRGFQG SFEELCRNKD INKAILEDMV KLGKNAGLKP
660 670 680 690
FEQVKGIAVH PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYSTIKI
Length:699
Mass (Da):78,179
Last modified:November 1, 1990 - v1
Checksum:i6E1EACE0EAE8A85C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90109 mRNA. Translation: BAA14136.1.
PIRiA36275.
RefSeqiNP_036952.1. NM_012820.1.
XP_006253184.1. XM_006253122.1.
XP_006253185.1. XM_006253123.1.
XP_006253186.1. XM_006253124.2.
XP_006253187.1. XM_006253125.2.
XP_006253188.1. XM_006253126.1.
XP_006253189.1. XM_006253127.1.
XP_008769476.1. XM_008771254.1.
UniGeneiRn.6215.

Genome annotation databases

EnsembliENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633.
GeneIDi25288.
KEGGirno:25288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90109 mRNA. Translation: BAA14136.1 .
PIRi A36275.
RefSeqi NP_036952.1. NM_012820.1.
XP_006253184.1. XM_006253122.1.
XP_006253185.1. XM_006253123.1.
XP_006253186.1. XM_006253124.2.
XP_006253187.1. XM_006253125.2.
XP_006253188.1. XM_006253126.1.
XP_006253189.1. XM_006253127.1.
XP_008769476.1. XM_008771254.1.
UniGenei Rn.6215.

3D structure databases

ProteinModelPortali P18163.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P18163. 28 interactions.
MINTi MINT-4570488.
STRINGi 10116.ENSRNOP00000014235.

PTM databases

PhosphoSitei P18163.

Proteomic databases

PaxDbi P18163.
PRIDEi P18163.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000014235 ; ENSRNOP00000014235 ; ENSRNOG00000010633 .
GeneIDi 25288.
KEGGi rno:25288.

Organism-specific databases

CTDi 2180.
RGDi 2015. Acsl1.

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000101725.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi P18163.
KOi K01897.
OMAi WDRLIFH.
OrthoDBi EOG71CFKN.
PhylomeDBi P18163.
TreeFami TF313877.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14442.
BRENDAi 6.2.1.3. 5301.
Reactomei REACT_196408. PPARA activates gene expression.
REACT_198818. alpha-linolenic acid (ALA) metabolism.
REACT_198820. Linoleic acid (LA) metabolism.
REACT_232376. Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RK P18163.

Miscellaneous databases

NextBioi 606025.
PROi P18163.

Gene expression databases

Genevestigatori P18163.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure and regulation of rat long-chain acyl-CoA synthetase."
    Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S., Hashimoto T., Yamamoto T.
    J. Biol. Chem. 265:8681-8685(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  2. "Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry."
    Distler A.M., Kerner J., Hoppel C.L.
    Biochim. Biophys. Acta 1774:628-636(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  3. "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2."
    Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T.
    Eur. J. Biochem. 242:186-190(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6."
    Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A.
    Biochemistry 44:1635-1642(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Brain.
  5. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-136.

Entry informationi

Entry nameiACSL1_RAT
AccessioniPrimary (citable) accession number: P18163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

5 rat isozymes encoded by different genes have been described. ACSL6 corresponds to isozyme 2 (ACS2).1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3