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Q9CZW4 (ACSL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. 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 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 fatty 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.5

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
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Ensembl

fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

positive regulation of Golgi to plasma membrane protein transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of secretion

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 720720Long-chain-fatty-acid--CoA ligase 3
PRO_0000193108

Regions

Transmembrane21 – 4121Helical; Signal-anchor for type III membrane protein; Potential
Topological domain42 – 720679Cytoplasmic Potential

Amino acid modifications

Modified residue6831Phosphoserine By similarity

Experimental info

Sequence conflict2231D → E in BAB28022. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CZW4 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 27F9CCA6961B5BA0

FASTA72080,492
        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 LKDIVSLVPR 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 

« Hide

References

« Hide '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. 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: C57BL/6J.
Tissue: Embryo.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Czech II.
Tissue: Mammary tumor.
[4]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[5]"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. 284:30474-30483(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012088 mRNA. Translation: BAB28022.1.
AK161708 mRNA. Translation: BAE36543.1.
CH466548 Genomic DNA. Translation: EDL00440.1.
CH466548 Genomic DNA. Translation: EDL00441.1.
BC031529 mRNA. Translation: AAH31529.1.
RefSeqNP_001028778.2. NM_001033606.2.
NP_001129694.1. NM_001136222.1.
NP_083093.2. NM_028817.3.
UniGeneMm.276016.

3D structure databases

ProteinModelPortalQ9CZW4.
SMRQ9CZW4. Positions 135-664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CZW4. 1 interaction.
MINTMINT-4117014.
STRING10090.ENSMUSP00000121695.

PTM databases

PhosphoSiteQ9CZW4.

Proteomic databases

PaxDbQ9CZW4.
PRIDEQ9CZW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883.
ENSMUST00000142704; ENSMUSP00000121695; ENSMUSG00000032883.
GeneID74205.
KEGGmmu:74205.
UCSCuc007bqo.2. mouse.

Organism-specific databases

CTD2181.
MGIMGI:1921455. Acsl3.

Phylogenomic databases

eggNOGCOG1022.
GeneTreeENSGT00690000102168.
HOGENOMHOG000159459.
HOVERGENHBG106947.
InParanoidQ8K1J7.
KOK01897.
OMAVFMYAKN.
OrthoDBEOG7P2XRD.
TreeFamTF314012.

Enzyme and pathway databases

BRENDA6.2.1.3. 3474.

Gene expression databases

ArrayExpressQ9CZW4.
BgeeQ9CZW4.
GenevestigatorQ9CZW4.

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

NextBio340106.
PROQ9CZW4.
SOURCESearch...

Entry information

Entry nameACSL3_MOUSE
AccessionPrimary (citable) accession number: Q9CZW4
Secondary accession number(s): Q8K1J7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 103 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