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P41216 (ACSL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:Acsl1
Synonyms:Acsl2, Facl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

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

Cofactor

Magnesium.

Subcellular location

Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Peroxisome membrane; Single-pass type III membrane protein By similarity. Microsome membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
Mitochondrion
Mitochondrion outer membrane
Peroxisome
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Nitration
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadiponectin-activated signaling pathway

Inferred from mutant phenotype PubMed 20667975. Source: MGI

lipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 20667975. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to oleic acid

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

xenobiotic catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

peroxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 699699Long-chain-fatty-acid--CoA ligase 1
PRO_0000193105

Regions

Transmembrane25 – 4521Helical; Signal-anchor for type III membrane protein; Potential
Topological domain46 – 699654Cytoplasmic Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.4
Modified residue91Nitrated tyrosine By similarity
Modified residue851Phosphotyrosine By similarity
Modified residue861Nitrated tyrosine By similarity
Modified residue2081N6-acetyllysine Ref.6
Modified residue3571N6-acetyllysine Ref.6
Modified residue3871N6-acetyllysine Ref.6
Modified residue6211Phosphoserine Ref.5
Modified residue6331N6-acetyllysine By similarity

Experimental info

Sequence conflict401 – 4022EL → DV in AAA52193. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P41216 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: C8319972A764CCFA

FASTA69977,951
        10         20         30         40         50         60 
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ 

        70         80         90        100        110        120 
SVEIAGTTDG IRRSAVLEDD KLLVYYYDDV RTMYDGFQRG IQVSNNGPCL GSRKPNQPYE 

       130        140        150        160        170        180 
WISYKEVAEL AECIGSGLIQ KGFKPCSEQF IGLFSQNRPE WVIVEQGCFS YSMVVVPLYD 

       190        200        210        220        230        240 
TLGADAITYI VNKAELSVIF ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YGSDLVERGK 

       250        260        270        280        290        300 
KCGVEIISLK ALEDLGRVNR VKPKPPEPED LAIICFTSGT TGNPKGAMIT HQNIINDCSG 

       310        320        330        340        350        360 
FIKATESAFI ASTDDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ 

       370        380        390        400        410        420 
PTIFPVVPRL LNRMFDRIFG QANTSLKRWL LDFASKRKEA ELRSGIVRNN SLWDKLIFHK 

       430        440        450        460        470        480 
IQSSLGGKVR LMITGAAPVS ATVLTFLRTA LGCQFYEGYG QTECTAGCCL SLPGDWTAGH 

       490        500        510        520        530        540 
VGAPMPCNYV KLVDVEEMNY LASKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG 

       550        560        570        580        590        600 
DIGKWLPNGT LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA 

       610        620        630        640        650        660 
VVVPDVESLP SWAQKRGLQG SFEELCRNKD INKAILDDLL KLGKEAGLKP FEQVKGIAVH 

       670        680        690 
PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYATIKI 

« Hide

References

« Hide 'large scale' references
[1]Schaffer J.E.
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[4]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-8; 358-369; 389-396; 563-573; 617-627 AND 634-641, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208; LYS-357 AND LYS-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15977 mRNA. Translation: AAA52193.1.
AK004897 mRNA. Translation: BAB23652.1.
AK145900 mRNA. Translation: BAE26736.1.
AK149406 mRNA. Translation: BAE28854.1.
AK152772 mRNA. Translation: BAE31484.1.
AK153050 mRNA. Translation: BAE31678.1.
AK161189 mRNA. Translation: BAE36230.1.
AK168078 mRNA. Translation: BAE40051.1.
BC056644 mRNA. Translation: AAH56644.1.
CCDSCCDS22291.1.
RefSeqNP_032007.2. NM_007981.3.
XP_006509326.1. XM_006509263.1.
XP_006509327.1. XM_006509264.1.
XP_006509328.1. XM_006509265.1.
XP_006509329.1. XM_006509266.1.
UniGeneMm.210323.

3D structure databases

ProteinModelPortalP41216.
SMRP41216. Positions 112-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP41216. 14 interactions.
MINTMINT-1859502.

PTM databases

PhosphoSiteP41216.

Proteomic databases

MaxQBP41216.
PaxDbP41216.
PRIDEP41216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034046; ENSMUSP00000034046; ENSMUSG00000018796.
ENSMUST00000110372; ENSMUSP00000106001; ENSMUSG00000018796.
GeneID14081.
KEGGmmu:14081.
UCSCuc009lqe.1. mouse.

Organism-specific databases

CTD2180.
MGIMGI:102797. Acsl1.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000101725.
HOGENOMHOG000159459.
HOVERGENHBG050452.
InParanoidQ6GTG6.
KOK01897.
OMAQATNKHA.
OrthoDBEOG71CFKN.
TreeFamTF313877.

Enzyme and pathway databases

BRENDA6.2.1.3. 3474.

Gene expression databases

ArrayExpressP41216.
BgeeP41216.
CleanExMM_ACSL1.
GenevestigatorP41216.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285092.
PROP41216.
SOURCESearch...

Entry information

Entry nameACSL1_MOUSE
AccessionPrimary (citable) accession number: P41216
Secondary accession number(s): Q6GTG6, Q9DBK5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot