Long-chain-fatty-acid--CoA ligase 3 - Pongo abelii (Sumatran orangutan)

Preferred order of sections

Names and origin

Protein names

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 names

Name:

ACSL3

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	720 AA.
Sequence status	Complete.
Protein existence	Evidence 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 carboxylic 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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane Peroxisome
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 720

720

Long-chain-fatty-acid--CoA ligase 3

PRO_0000240276

Regions

Transmembrane

21 – 41

21

Helical; Signal-anchor for type III membrane protein; Potential

Topological domain

42 – 720

679

Cytoplasmic Potential

Amino acid modifications

Modified residue

593

1

Phosphoserine By similarity

Modified residue

683

1

Phosphoserine By similarity

Modified residue

688

1

Phosphothreonine By similarity

Experimental info

Sequence conflict

104

1

L → P in CAH91520. Ref.1

Sequence conflict

112

1

N → S in CAH93302. Ref.1

Sequence conflict

117

1

V → I in CAH93302. Ref.1

Sequence conflict

210

1

I → T in CAH91520. Ref.1

Sequence conflict

270

1

N → D in CAH93302. Ref.1

Sequence conflict

386

1

I → T in CAH92748. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q5R668 [UniParc].

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

720

80,445

        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

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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.
RefSeq	NP_001127581.1. NM_001134109.1. NP_001128901.1. NM_001135429.1.
UniGene	Pab.18013. Pab.19655.
3D structure databases
ProteinModelPortal	Q5R668.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100174659. 100189843.
KEGG	pon:100174659. pon:100189843.
Organism-specific databases
CTD	2181.
Phylogenomic databases
HOVERGEN	HBG106947.
InParanoid	Q5R668.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01897.
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSL3_PONAB

Accession

Primary (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:	November 16, 2011
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents