Reviewed, UniProtKB/Swiss-Prot P41216 (ACSL1_MOUSE)

Names and origin

Protein names

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

Gene names

Name:	Acsl1
Synonyms:	Acsl2, Facl2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 carboxylic 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane Peroxisome
Domain	Signal-anchor Transmembrane
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 699	699	Long-chain-fatty-acid--CoA ligase 1		PRO_0000193105
Regions
	Transmembrane	25 – 45	21	Signal-anchor for type III membrane protein Potential
	Topological domain	46 – 699	654	Cytoplasmic Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.3
	Modified residue	85	1	Phosphotyrosine By similarity
	Modified residue	544	1	N6-acetyllysine Ref.4
	Modified residue	633	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	401 – 402	2	DV → EL in BAB23652. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P41216-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E521CED12A662745	FASTA	699	77,923
	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 DVRSGIVRNN 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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[3]	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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-544, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U15977 mRNA. Translation: AAA52193.1. AK004897 mRNA. Translation: BAB23652.1.
IPI	IPI00112549.
RefSeq	NP_032007.2.
UniGene	Mm.210323
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Protein-protein interaction databases
STRING	P41216.
PTM databases
PhosphoSite	P41216.
Proteomic databases
PRIDE	P41216.
Genome annotation databases
Ensembl	ENSMUST00000034046; ENSMUSP00000034046; ENSMUSG00000018796; Mus musculus. [Genome view] ENSMUST00000110372; ENSMUSP00000106001; ENSMUSG00000018796; Mus musculus. [Genome view]
GeneID	14081.
KEGG	mmu:14081.
Organism-specific databases
CTD	14081.
MGI	MGI:102797. Acsl1.
Phylogenomic databases
HOGENOM	P41216.
HOVERGEN	P41216.
Enzyme and pathway databases
BRENDA	6.2.1.3. 244.
Gene expression databases
ArrayExpress	P41216.
Bgee	P41216.
CleanEx	MM_ACSL1.
Genevestigator	P41216.
GermOnline	ENSMUSG00000018796. Mus musculus.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 2 hits. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	285092.
SOURCE	Search...

Entry information

Entry name

ACSL1_MOUSE

Accession

Primary (citable) accession number: P41216
Secondary accession number(s): Q9DBK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	October 13, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)