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Q5R668 (ACSL3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ACSL3
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Peroxisome membrane; Single-pass type III membrane protein By similarity. Microsome membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Long-chain-fatty-acid--CoA ligase 3
PRO_0000240276

Regions

Transmembrane21 – 4121Helical; Signal-anchor for type III membrane protein; Potential
Topological domain42 – 720679Cytoplasmic Potential

Amino acid modifications

Modified residue6831Phosphoserine By similarity

Experimental info

Sequence conflict1041L → P in CAH91520. Ref.1
Sequence conflict1121N → S in CAH93302. Ref.1
Sequence conflict1171V → I in CAH93302. Ref.1
Sequence conflict2101I → T in CAH91520. Ref.1
Sequence conflict2701N → D in CAH93302. Ref.1
Sequence conflict3861I → T in CAH92748. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R668 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: C5E83CFBD6904101

FASTA72080,445
        10         20         30         40         50         60 
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV 

        70         80         90        100        110        120 
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN 

       130        140        150        160        170        180 
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF 

       190        200        210        220        230        240 
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK 

       250        260        270        280        290        300 
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS 

       310        320        330        340        350        360 
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 

       370        380        390        400        410        420 
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI 

       430        440        450        460        470        480 
SKGRNTPLCN SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 

       490        500        510        520        530        540 
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQIVTMGYY 

       550        560        570        580        590        600 
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 

       610        620        630        640        650        660 
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK 

       670        680        690        700        710        720 
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859345 mRNA. Translation: CAH91520.1.
CR860628 mRNA. Translation: CAH92748.1.
CR861232 mRNA. Translation: CAH93302.1.
RefSeqNP_001127581.1. NM_001134109.1.
NP_001128901.1. NM_001135429.1.
UniGenePab.19655.

3D structure databases

ProteinModelPortalQ5R668.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174659.
100189843.
KEGGpon:100174659.
pon:100189843.

Organism-specific databases

CTD2181.

Phylogenomic databases

HOVERGENHBG106947.
InParanoidQ5R668.
KOK01897.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSL3_PONAB
AccessionPrimary (citable) accession number: Q5R668
Secondary accession number(s): Q5R4L4, Q5R9P0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families