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Q9CZW4

- ACSL3_MOUSE

UniProt

Q9CZW4 - ACSL3_MOUSE

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Protein
Long-chain-fatty-acid--CoA ligase 3
Gene
Acsl3, Acs3, Facl3
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Magnesium By similarity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. brain development Source: Ensembl
  2. fatty acid biosynthetic process Source: Ensembl
  3. long-chain fatty acid import Source: Ensembl
  4. positive regulation of Golgi to plasma membrane protein transport Source: Ensembl
  5. positive regulation of phosphatidylcholine biosynthetic process Source: Ensembl
  6. positive regulation of secretion Source: Ensembl
  7. response to nutrient Source: Ensembl
  8. response to organic cyclic compound Source: Ensembl
  9. very-low-density lipoprotein particle assembly Source: Ensembl
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.

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: 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 protein; Reviewed prediction
Add
BLAST
Topological domaini42 – 720679Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. lipid particle Source: Ensembl
  5. mitochondrial outer membrane Source: UniProtKB-SubCell
  6. perinuclear region of cytoplasm Source: Ensembl
  7. peroxisomal membrane Source: UniProtKB-SubCell
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 3
PRO_0000193108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei683 – 6831Phosphoserine By 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

ArrayExpressiQ9CZW4.
BgeeiQ9CZW4.
GenevestigatoriQ9CZW4.

Interactioni

Protein-protein interaction databases

IntActiQ9CZW4. 1 interaction.
MINTiMINT-4117014.
STRINGi10090.ENSMUSP00000121695.

Structurei

3D structure databases

ProteinModelPortaliQ9CZW4.
SMRiQ9CZW4. Positions 135-664.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000102168.
HOGENOMiHOG000159459.
HOVERGENiHBG106947.
InParanoidiQ8K1J7.
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

MNNHVSSTPS TMKLKQTINP ILLYFIHFII SLYTILTYIP FYFLCESKQE    50
KPNQIKAKPV SSKPDSAYRS INSVDGLASV LYPGCDTLDK VFMYAKNKFK 100
NKRLLGTREI LNEEDEIQPN GKIFKKVILG HYNWLSYEDV FIRALDFGNG 150
LQMLGQKPKA NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH 200
GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG 250
VIVHTMAAVQ ALGVKANVEK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 300
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG 350
YSSPQTLADQ SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE 400
MSAFQRNLFI LAYNYKMEQI SKGCSTPLCD RFVFRNVRRL LGGNIRLLLC 450
GGAPLSATTQ RFMNICFCCP VGQGYGLTES TGAGTITEVW DYNTGRVGAP 500
LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY KNEAKTKTDF 550
FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FKGTWEELCN 650
SSEMENEVLK VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL 700
KRKELKTHYQ ADIERMYGRK 720
Length:720
Mass (Da):80,492
Last modified:July 27, 2011 - v2
Checksum:i27F9CCA6961B5BA0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231D → E in BAB28022. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS15087.1.
RefSeqi NP_001028778.2. NM_001033606.2.
NP_001129694.1. NM_001136222.1.
NP_083093.2. NM_028817.3.
UniGenei Mm.276016.

3D structure databases

ProteinModelPortali Q9CZW4.
SMRi Q9CZW4. Positions 135-664.
ModBasei Search...

Protein-protein interaction databases

IntActi Q9CZW4. 1 interaction.
MINTi MINT-4117014.
STRINGi 10090.ENSMUSP00000121695.

PTM databases

PhosphoSitei Q9CZW4.

Proteomic databases

MaxQBi Q9CZW4.
PaxDbi Q9CZW4.
PRIDEi Q9CZW4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035779 ; ENSMUSP00000045291 ; ENSMUSG00000032883 .
ENSMUST00000142704 ; ENSMUSP00000121695 ; ENSMUSG00000032883 .
GeneIDi 74205.
KEGGi mmu:74205.
UCSCi uc007bqo.2. mouse.

Organism-specific databases

CTDi 2181.
MGIi MGI:1921455. Acsl3.

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000102168.
HOGENOMi HOG000159459.
HOVERGENi HBG106947.
InParanoidi Q8K1J7.
KOi K01897.
OMAi CDRFIFR.
OrthoDBi EOG7P2XRD.
TreeFami TF314012.

Enzyme and pathway databases

BRENDAi 6.2.1.3. 3474.

Miscellaneous databases

NextBioi 340106.
PROi Q9CZW4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9CZW4.
Bgeei Q9CZW4.
Genevestigatori Q9CZW4.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 105 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