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Protein

Long-chain-fatty-acid--CoA ligase 5

Gene

Acsl5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity). It was suggested that it may also stimulate fatty acid oxidation (By similarity). At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity). May have a role in the survival of glioma cells (By similarity). Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. long-chain fatty acid metabolic process Source: MGI
  2. regulation of extrinsic apoptotic signaling pathway Source: MGI
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 5 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 5
Short name:
LACS 5
Gene namesi
Name:Acsl5
Synonyms:Facl5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1919129. Acsl5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 683651CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
  5. mitochondrial inner membrane Source: MGI
  6. mitochondrial outer membrane Source: UniProtKB-SubCell
  7. mitochondrion Source: MGI
  8. nucleolus Source: MGI
  9. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Long-chain-fatty-acid--CoA ligase 5PRO_0000193113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8JZR0.
PaxDbiQ8JZR0.
PRIDEiQ8JZR0.

PTM databases

PhosphoSiteiQ8JZR0.

Expressioni

Gene expression databases

BgeeiQ8JZR0.
CleanExiMM_ACSL5.
ExpressionAtlasiQ8JZR0. baseline and differential.
GenevestigatoriQ8JZR0.

Interactioni

Protein-protein interaction databases

IntActiQ8JZR0. 2 interactions.
MINTiMINT-1862123.

Structurei

3D structure databases

ProteinModelPortaliQ8JZR0.
SMRiQ8JZR0. Positions 106-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ8JZR0.
KOiK01897.
OMAiIKDGARK.
OrthoDBiEOG71CFKN.
PhylomeDBiQ8JZR0.
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.

Q8JZR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG
60 70 80 90 100
IEGGARRGAF QKNNDLILYY FSDAKTLYEN FQRGLAVSDN GPCLGYRKPN
110 120 130 140 150
QPYKWISYKQ VSDRAEYLGS CLLHKGYKSS QDQFVGIFAQ NRPEWVISEL
160 170 180 190 200
ACYTYSMVAV PLYDTLGTEA IIFVINRADI PVVICDTPQK ATMLVENVEK
210 220 230 240 250
GLTPGLKTII LMDPFDDDLM KRGEKCGVEM LSLHDAENIG KENFKKPVPP
260 270 280 290 300
KPEDLSVICF TSGTTGDPKG AMLTHENVVS NMAAFLKFLE PIFQPTSDDV
310 320 330 340 350
TISYLPLAHM FERLVQGILF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT
360 370 380 390 400
VPRLLNRVYD KVQNEAKTPL KKFLLNLAII SKFNEVKNGI IRRDSLWDKL
410 420 430 440 450
VFSKIQGSLG GKVRLMITGA APISTPVLTF FRAAMGCWVF EAYGQTECTG
460 470 480 490 500
GCSITSPGDW TAGHVGTPVA CNFVKLEDVA DMNYFSVNNE GEICIKGNNV
510 520 530 540 550
FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIVDR KKNIFKLAQG
560 570 580 590 600
EYIAPEKIEN VYSRSRPVLQ VFVHGESLRS FLIGVVVPDP DSLPSFAAKI
610 620 630 640 650
GVKGSFEELC KNQCVKEAIL EDLQKIGKEG GLKSFEQVKS IFVHPEPFTI
660 670 680
ENGLLTPTLK AKRVELAKFF QTQIKSLYES IEE
Length:683
Mass (Da):76,206
Last modified:October 1, 2002 - v1
Checksum:i734A1A5878741D70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031544 mRNA. Translation: AAH31544.1.
CCDSiCCDS29908.1.
PIRiS49487.
RefSeqiNP_082252.1. NM_027976.2.
XP_006527241.1. XM_006527178.1.
UniGeneiMm.292056.

Genome annotation databases

EnsembliENSMUST00000043150; ENSMUSP00000046585; ENSMUSG00000024981.
GeneIDi433256.
KEGGimmu:433256.
UCSCiuc008hxp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031544 mRNA. Translation: AAH31544.1.
CCDSiCCDS29908.1.
PIRiS49487.
RefSeqiNP_082252.1. NM_027976.2.
XP_006527241.1. XM_006527178.1.
UniGeneiMm.292056.

3D structure databases

ProteinModelPortaliQ8JZR0.
SMRiQ8JZR0. Positions 106-620.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8JZR0. 2 interactions.
MINTiMINT-1862123.

PTM databases

PhosphoSiteiQ8JZR0.

Proteomic databases

MaxQBiQ8JZR0.
PaxDbiQ8JZR0.
PRIDEiQ8JZR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043150; ENSMUSP00000046585; ENSMUSG00000024981.
GeneIDi433256.
KEGGimmu:433256.
UCSCiuc008hxp.1. mouse.

Organism-specific databases

CTDi51703.
MGIiMGI:1919129. Acsl5.

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ8JZR0.
KOiK01897.
OMAiIKDGARK.
OrthoDBiEOG71CFKN.
PhylomeDBiQ8JZR0.
TreeFamiTF313877.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAcsl5. mouse.
NextBioi408505.
PROiQ8JZR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZR0.
CleanExiMM_ACSL5.
ExpressionAtlasiQ8JZR0. baseline and differential.
GenevestigatoriQ8JZR0.

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

  1. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  2. "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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACSL5_MOUSE
AccessioniPrimary (citable) accession number: Q8JZR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: April 1, 2015
This is version 109 of the entry and version 1 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.