Reviewed, UniProtKB/Swiss-Prot Q9CZW4 (ACSL3_MOUSE)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase 3
    EC=6.2.1.3
Alternative name(s):
    Long-chain acyl-CoA synthetase 3
      Short name=LACS 3

Gene names

Name:	Acsl3
Synonyms:	Acs3, Facl3

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	720 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 has mainly an anabolic role in energy metabolism By similarity. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) By similarity. Mediates hepatic lipogenesis By similarity. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates By similarity.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium By similarity.
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.
Induction	High expression in ob/ob mice (obese) and mice fed at high sucrose diet. Ref.2
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	Phosphoprotein
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 peroxisome 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 – 720	720	Long-chain-fatty-acid--CoA ligase 3		PRO_0000193108
Regions
	Transmembrane	21 – 41	21	Signal-anchor for type III membrane protein Potential
	Topological domain	42 – 720	679	Cytoplasmic Potential
Amino acid modifications
	Modified residue	593	1	Phosphoserine By similarity
	Modified residue	683	1	Phosphoserine By similarity
	Modified residue	688	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CZW4-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 97F995CAE7DC47D1	FASTA	720	80,506
	10 20 30 40 50 60 MNNHVSSTPS TMKLKQTINP ILLYFIHFII SLYTILTYIP FYFLCESKQE KPNQIKAKPV 70 80 90 100 110 120 SSKPDSAYRS INSVDGLASV LYPGCDTLDK VFMYAKNKFK NKRLLGTREI LNEEDEIQPN 130 140 150 160 170 180 GKIFKKVILG HYNWLSYEDV FIRALDFGNG LQMLGQKPKA NIAIFCETRA EWMIAAQACF 190 200 210 220 230 240 MYNFQLVTLY ATLGGPAIVH GLNETEVTNI ITSKELLQTK LKEIVSLVPR LRHIITVDGK 250 260 270 280 290 300 PPTWSEFPKG VIVHTMAAVQ ALGVKANVEK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 310 320 330 340 350 360 HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 370 380 390 400 410 420 SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE MSAFQRNLFI LAYNYKMEQI 430 440 450 460 470 480 SKGCSTPLCD RFVFRNVRRL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 490 500 510 520 530 540 TGAGTITEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY 550 560 570 580 590 600 KNEAKTKTDF FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 610 620 630 640 650 660 LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FKGTWEELCN SSEMENEVLK 670 680 690 700 710 720 VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Embryo.
[2]	"Suppression of long chain acyl-CoA synthetase 3 (ACSL3) decreases hepatic de novo fatty acid synthesis through decreased transcriptional activity." Bu S.Y., Mashek M.T., Mashek D.G. J. Biol. Chem. 0:0-0(2009) [PubMed: 19737935] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK012088 mRNA. Translation: BAB28022.1.
IPI	IPI00169772.
RefSeq	NP_001028778.2.
UniGene	Mm.276016 Mm.427252
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CZW4.
PTM databases
PhosphoSite	Q9CZW4.
Proteomic databases
PRIDE	Q9CZW4.
Genome annotation databases
Ensembl	ENSMUST00000012393; ENSMUSP00000012393; ENSMUSG00000032883; Mus musculus. [Genome view] ENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883; Mus musculus. [Genome view] ENSMUST00000113521; ENSMUSP00000109149; ENSMUSG00000032883; Mus musculus. [Genome view]
GeneID	74205.
KEGG	mmu:74205.
UCSC	uc007bqp.1. mouse.
Organism-specific databases
MGI	MGI:1921455. Acsl3.
Phylogenomic databases
HOVERGEN	Q9CZW4.
Enzyme and pathway databases
BRENDA	6.2.1.3. 244.
Gene expression databases
ArrayExpress	Q9CZW4.
Bgee	Q9CZW4.
Genevestigator	Q9CZW4.
GermOnline	ENSMUSG00000032883. Mus musculus.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	340106.
SOURCE	Search...

Entry information

Entry name

ACSL3_MOUSE

Accession

Primary (citable) accession number: Q9CZW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	June 1, 2001
Last modified:	October 13, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)