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Protein

Long-chain-fatty-acid--CoA ligase 3

Gene

Acsl3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

GO - Molecular functioni

GO - Biological processi

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

BRENDAi6.2.1.3. 3474.
ReactomeiREACT_292148. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Acsl3
Synonyms:Acs3, Facl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1921455. Acsl3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei21 – 4121Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini42 – 720679CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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 – 720720Long-chain-fatty-acid--CoA ligase 3PRO_0000193108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei683 – 6831PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CZW4.
PaxDbiQ9CZW4.
PRIDEiQ9CZW4.

PTM databases

PhosphoSiteiQ9CZW4.

Expressioni

Inductioni

High expression in ob/ob mice (obese) and mice fed at high sucrose diet.1 Publication

Gene expression databases

BgeeiQ9CZW4.
ExpressionAtlasiQ9CZW4. baseline and differential.
GenevisibleiQ9CZW4. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9CZW4. 1 interaction.
MINTiMINT-4117014.
STRINGi10090.ENSMUSP00000045291.

Structurei

3D structure databases

ProteinModelPortaliQ9CZW4.
SMRiQ9CZW4. Positions 135-664.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiQ9CZW4.
KOiK01897.
OMAiCDRFIFR.
OrthoDBiEOG7P2XRD.
TreeFamiTF314012.

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.

Q9CZW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNHVSSTPS TMKLKQTINP ILLYFIHFII SLYTILTYIP FYFLCESKQE
60 70 80 90 100
KPNQIKAKPV SSKPDSAYRS INSVDGLASV LYPGCDTLDK VFMYAKNKFK
110 120 130 140 150
NKRLLGTREI LNEEDEIQPN GKIFKKVILG HYNWLSYEDV FIRALDFGNG
160 170 180 190 200
LQMLGQKPKA NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH
210 220 230 240 250
GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG
260 270 280 290 300
VIVHTMAAVQ ALGVKANVEK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS
310 320 330 340 350
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG
360 370 380 390 400
YSSPQTLADQ SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE
410 420 430 440 450
MSAFQRNLFI LAYNYKMEQI SKGCSTPLCD RFVFRNVRRL LGGNIRLLLC
460 470 480 490 500
GGAPLSATTQ RFMNICFCCP VGQGYGLTES TGAGTITEVW DYNTGRVGAP
510 520 530 540 550
LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY KNEAKTKTDF
560 570 580 590 600
FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
610 620 630 640 650
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FKGTWEELCN
660 670 680 690 700
SSEMENEVLK VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL
710 720
KRKELKTHYQ ADIERMYGRK
Length:720
Mass (Da):80,492
Last modified:July 27, 2011 - v2
Checksum:i27F9CCA6961B5BA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231D → E in BAB28022 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15087.1.
RefSeqiNP_001028778.2. NM_001033606.2.
NP_001129694.1. NM_001136222.1.
NP_083093.2. NM_028817.3.
UniGeneiMm.276016.

Genome annotation databases

EnsembliENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883.
ENSMUST00000142704; ENSMUSP00000121695; ENSMUSG00000032883.
GeneIDi74205.
KEGGimmu:74205.
UCSCiuc007bqo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15087.1.
RefSeqiNP_001028778.2. NM_001033606.2.
NP_001129694.1. NM_001136222.1.
NP_083093.2. NM_028817.3.
UniGeneiMm.276016.

3D structure databases

ProteinModelPortaliQ9CZW4.
SMRiQ9CZW4. Positions 135-664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CZW4. 1 interaction.
MINTiMINT-4117014.
STRINGi10090.ENSMUSP00000045291.

PTM databases

PhosphoSiteiQ9CZW4.

Proteomic databases

MaxQBiQ9CZW4.
PaxDbiQ9CZW4.
PRIDEiQ9CZW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035779; ENSMUSP00000045291; ENSMUSG00000032883.
ENSMUST00000142704; ENSMUSP00000121695; ENSMUSG00000032883.
GeneIDi74205.
KEGGimmu:74205.
UCSCiuc007bqo.2. mouse.

Organism-specific databases

CTDi2181.
MGIiMGI:1921455. Acsl3.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiQ9CZW4.
KOiK01897.
OMAiCDRFIFR.
OrthoDBiEOG7P2XRD.
TreeFamiTF314012.

Enzyme and pathway databases

BRENDAi6.2.1.3. 3474.
ReactomeiREACT_292148. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi340106.
PROiQ9CZW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZW4.
ExpressionAtlasiQ9CZW4. baseline and differential.
GenevisibleiQ9CZW4. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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.

Entry informationi

Entry nameiACSL3_MOUSE
AccessioniPrimary (citable) accession number: Q9CZW4
Secondary accession number(s): Q8K1J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.