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Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

Acsl1

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

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: MGI

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: MGI
  2. lipid biosynthetic process Source: MGI
  3. long-chain fatty acid import Source: MGI
  4. long-chain fatty acid metabolic process Source: MGI
  5. positive regulation of protein serine/threonine kinase activity Source: MGI
  6. response to drug Source: Ensembl
  7. response to nutrient Source: Ensembl
  8. response to oleic acid Source: Ensembl
  9. response to organic cyclic compound Source: Ensembl
  10. triglyceride metabolic process Source: Ensembl
  11. xenobiotic catabolic process 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.
ReactomeiREACT_196530. Linoleic acid (LA) metabolism.
REACT_196541. alpha-linolenic acid (ALA) metabolism.
REACT_198602. PPARA activates gene expression.
REACT_252780. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Acsl1
Synonyms:Acsl2, Facl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:102797. Acsl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 4521Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini46 – 699654CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
  4. mitochondrial outer membrane Source: UniProtKB-SubCell
  5. mitochondrion Source: MGI
  6. peroxisomal membrane Source: UniProtKB-SubCell
  7. plasma membrane Source: Ensembl
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 – 699699Long-chain-fatty-acid--CoA ligase 1PRO_0000193105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei9 – 91Nitrated tyrosineBy similarity
Modified residuei85 – 851PhosphotyrosineBy similarity
Modified residuei86 – 861Nitrated tyrosineBy similarity
Glycosylationi136 – 1361O-linked (GlcNAc)By similarity
Modified residuei208 – 2081N6-acetyllysine1 Publication
Modified residuei357 – 3571N6-acetyllysine1 Publication
Modified residuei387 – 3871N6-acetyllysine1 Publication
Modified residuei621 – 6211Phosphoserine1 Publication
Modified residuei633 – 6331N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP41216.
PaxDbiP41216.
PRIDEiP41216.

PTM databases

PhosphoSiteiP41216.

Expressioni

Gene expression databases

BgeeiP41216.
CleanExiMM_ACSL1.
ExpressionAtlasiP41216. baseline and differential.
GenevestigatoriP41216.

Interactioni

Protein-protein interaction databases

IntActiP41216. 14 interactions.
MINTiMINT-1859502.

Structurei

3D structure databases

ProteinModelPortaliP41216.
SMRiP41216. Positions 112-639.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP41216.
KOiK01897.
OMAiVEVAXNG.
OrthoDBiEOG71CFKN.
TreeFamiTF313877.

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.

P41216-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA
60 70 80 90 100
LKPPCDLSMQ SVEIAGTTDG IRRSAVLEDD KLLVYYYDDV RTMYDGFQRG
110 120 130 140 150
IQVSNNGPCL GSRKPNQPYE WISYKEVAEL AECIGSGLIQ KGFKPCSEQF
160 170 180 190 200
IGLFSQNRPE WVIVEQGCFS YSMVVVPLYD TLGADAITYI VNKAELSVIF
210 220 230 240 250
ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YGSDLVERGK KCGVEIISLK
260 270 280 290 300
ALEDLGRVNR VKPKPPEPED LAIICFTSGT TGNPKGAMIT HQNIINDCSG
310 320 330 340 350
FIKATESAFI ASTDDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR
360 370 380 390 400
LLMDDLKVLQ PTIFPVVPRL LNRMFDRIFG QANTSLKRWL LDFASKRKEA
410 420 430 440 450
ELRSGIVRNN SLWDKLIFHK IQSSLGGKVR LMITGAAPVS ATVLTFLRTA
460 470 480 490 500
LGCQFYEGYG QTECTAGCCL SLPGDWTAGH VGAPMPCNYV KLVDVEEMNY
510 520 530 540 550
LASKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG DIGKWLPNGT
560 570 580 590 600
LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA
610 620 630 640 650
VVVPDVESLP SWAQKRGLQG SFEELCRNKD INKAILDDLL KLGKEAGLKP
660 670 680 690
FEQVKGIAVH PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYATIKI
Length:699
Mass (Da):77,951
Last modified:June 28, 2011 - v2
Checksum:iC8319972A764CCFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4022EL → DV in AAA52193. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15977 mRNA. Translation: AAA52193.1.
AK004897 mRNA. Translation: BAB23652.1.
AK145900 mRNA. Translation: BAE26736.1.
AK149406 mRNA. Translation: BAE28854.1.
AK152772 mRNA. Translation: BAE31484.1.
AK153050 mRNA. Translation: BAE31678.1.
AK161189 mRNA. Translation: BAE36230.1.
AK168078 mRNA. Translation: BAE40051.1.
BC056644 mRNA. Translation: AAH56644.1.
CCDSiCCDS22291.1.
RefSeqiNP_001289092.1. NM_001302163.1.
NP_032007.2. NM_007981.4.
XP_006509327.1. XM_006509264.1.
XP_006509328.1. XM_006509265.1.
XP_006509329.1. XM_006509266.1.
UniGeneiMm.210323.

Genome annotation databases

EnsembliENSMUST00000034046; ENSMUSP00000034046; ENSMUSG00000018796.
ENSMUST00000110372; ENSMUSP00000106001; ENSMUSG00000018796.
GeneIDi14081.
KEGGimmu:14081.
UCSCiuc009lqe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15977 mRNA. Translation: AAA52193.1.
AK004897 mRNA. Translation: BAB23652.1.
AK145900 mRNA. Translation: BAE26736.1.
AK149406 mRNA. Translation: BAE28854.1.
AK152772 mRNA. Translation: BAE31484.1.
AK153050 mRNA. Translation: BAE31678.1.
AK161189 mRNA. Translation: BAE36230.1.
AK168078 mRNA. Translation: BAE40051.1.
BC056644 mRNA. Translation: AAH56644.1.
CCDSiCCDS22291.1.
RefSeqiNP_001289092.1. NM_001302163.1.
NP_032007.2. NM_007981.4.
XP_006509327.1. XM_006509264.1.
XP_006509328.1. XM_006509265.1.
XP_006509329.1. XM_006509266.1.
UniGeneiMm.210323.

3D structure databases

ProteinModelPortaliP41216.
SMRiP41216. Positions 112-639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41216. 14 interactions.
MINTiMINT-1859502.

PTM databases

PhosphoSiteiP41216.

Proteomic databases

MaxQBiP41216.
PaxDbiP41216.
PRIDEiP41216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034046; ENSMUSP00000034046; ENSMUSG00000018796.
ENSMUST00000110372; ENSMUSP00000106001; ENSMUSG00000018796.
GeneIDi14081.
KEGGimmu:14081.
UCSCiuc009lqe.1. mouse.

Organism-specific databases

CTDi2180.
MGIiMGI:102797. Acsl1.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiP41216.
KOiK01897.
OMAiVEVAXNG.
OrthoDBiEOG71CFKN.
TreeFamiTF313877.

Enzyme and pathway databases

BRENDAi6.2.1.3. 3474.
ReactomeiREACT_196530. Linoleic acid (LA) metabolism.
REACT_196541. alpha-linolenic acid (ALA) metabolism.
REACT_198602. PPARA activates gene expression.
REACT_252780. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiAcsl1. mouse.
NextBioi285092.
PROiP41216.
SOURCEiSearch...

Gene expression databases

BgeeiP41216.
CleanExiMM_ACSL1.
ExpressionAtlasiP41216. baseline and differential.
GenevestigatoriP41216.

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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and C57BL/6J.
    Tissue: Liver.
  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: FVB/N.
    Tissue: Liver.
  4. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208; LYS-357 AND LYS-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACSL1_MOUSE
AccessioniPrimary (citable) accession number: P41216
Secondary accession number(s): Q6GTG6, Q9DBK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 28, 2011
Last modified: February 4, 2015
This is version 129 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, Direct protein sequencing, 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.