SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41216

- ACSL1_MOUSE

UniProt

P41216 - ACSL1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Long-chain-fatty-acid--CoA ligase 1
Gene
Acsl1, Acsl2, Facl2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Magnesium.

GO - Molecular functioni

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

GO - Biological processi

  1. adiponectin-activated signaling pathway Source: MGI
  2. lipid biosynthetic process Source: Ensembl
  3. long-chain fatty acid import Source: Ensembl
  4. positive regulation of protein serine/threonine kinase activity Source: MGI
  5. response to drug Source: Ensembl
  6. response to nutrient Source: Ensembl
  7. response to oleic acid Source: Ensembl
  8. response to organic cyclic compound Source: Ensembl
  9. triglyceride metabolic process Source: Ensembl
  10. 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.

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 protein; Reviewed prediction
Add
BLAST
Topological domaini46 – 699654Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: MGI
  5. peroxisomal membrane Source: UniProtKB-SubCell
  6. 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 1
PRO_0000193105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei9 – 91Nitrated tyrosine By similarity
Modified residuei85 – 851Phosphotyrosine By similarity
Modified residuei86 – 861Nitrated tyrosine By 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-acetyllysine By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP41216.
PaxDbiP41216.
PRIDEiP41216.

PTM databases

PhosphoSiteiP41216.

Expressioni

Gene expression databases

ArrayExpressiP41216.
BgeeiP41216.
CleanExiMM_ACSL1.
GenevestigatoriP41216.

Interactioni

Protein-protein interaction databases

IntActiP41216. 14 interactions.
MINTiMINT-1859502.

Structurei

3D structure databases

ProteinModelPortaliP41216.
SMRiP41216. Positions 112-639.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ6GTG6.
KOiK01897.
OMAiQATNKHA.
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

MEVHELFRYF RMPELIDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA    50
LKPPCDLSMQ SVEIAGTTDG IRRSAVLEDD KLLVYYYDDV RTMYDGFQRG 100
IQVSNNGPCL GSRKPNQPYE WISYKEVAEL AECIGSGLIQ KGFKPCSEQF 150
IGLFSQNRPE WVIVEQGCFS YSMVVVPLYD TLGADAITYI VNKAELSVIF 200
ADKPEKAKLL LEGVENKLTP CLKIIVIMDS YGSDLVERGK KCGVEIISLK 250
ALEDLGRVNR VKPKPPEPED LAIICFTSGT TGNPKGAMIT HQNIINDCSG 300
FIKATESAFI ASTDDVLISF LPLAHMFETV VECVMLCHGA KIGFFQGDIR 350
LLMDDLKVLQ PTIFPVVPRL LNRMFDRIFG QANTSLKRWL LDFASKRKEA 400
ELRSGIVRNN SLWDKLIFHK IQSSLGGKVR LMITGAAPVS ATVLTFLRTA 450
LGCQFYEGYG QTECTAGCCL SLPGDWTAGH VGAPMPCNYV KLVDVEEMNY 500
LASKGEGEVC VKGANVFKGY LKDPARTAEA LDKDGWLHTG DIGKWLPNGT 550
LKIIDRKKHI FKLAQGEYIA PEKIENIYLR SEAVAQVFVH GESLQAFLIA 600
VVVPDVESLP SWAQKRGLQG SFEELCRNKD INKAILDDLL KLGKEAGLKP 650
FEQVKGIAVH PELFSIDNGL LTPTLKAKRP ELRNYFRSQI DELYATIKI 699
Length:699
Mass (Da):77,951
Last modified:June 28, 2011 - v2
Checksum:iC8319972A764CCFA
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_032007.2. NM_007981.3.
XP_006509326.1. XM_006509263.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22291.1.
RefSeqi NP_032007.2. NM_007981.3.
XP_006509326.1. XM_006509263.1.
XP_006509327.1. XM_006509264.1.
XP_006509328.1. XM_006509265.1.
XP_006509329.1. XM_006509266.1.
UniGenei Mm.210323.

3D structure databases

ProteinModelPortali P41216.
SMRi P41216. Positions 112-639.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P41216. 14 interactions.
MINTi MINT-1859502.

PTM databases

PhosphoSitei P41216.

Proteomic databases

MaxQBi P41216.
PaxDbi P41216.
PRIDEi P41216.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034046 ; ENSMUSP00000034046 ; ENSMUSG00000018796 .
ENSMUST00000110372 ; ENSMUSP00000106001 ; ENSMUSG00000018796 .
GeneIDi 14081.
KEGGi mmu:14081.
UCSCi uc009lqe.1. mouse.

Organism-specific databases

CTDi 2180.
MGIi MGI:102797. Acsl1.

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000101725.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi Q6GTG6.
KOi K01897.
OMAi QATNKHA.
OrthoDBi EOG71CFKN.
TreeFami TF313877.

Enzyme and pathway databases

BRENDAi 6.2.1.3. 3474.
Reactomei REACT_196530. Linoleic acid (LA) metabolism.
REACT_196541. alpha-linolenic acid (ALA) metabolism.
REACT_198602. PPARA activates gene expression.

Miscellaneous databases

NextBioi 285092.
PROi P41216.
SOURCEi Search...

Gene expression databases

ArrayExpressi P41216.
Bgeei P41216.
CleanExi MM_ACSL1.
Genevestigatori P41216.

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. 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: September 3, 2014
This is version 124 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