O88813 (ACSL5_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Acsl5
Synonyms:	Acs5, Facl5

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	683 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. ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villus axis of the small intestine By similarity. May have a role in the survival of glioma cells By similarity. May activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. It was suggested that it may also stimulate fatty acid oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. Ref.1 Ref.2 Ref.3
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Subcellular location	Mitochondrion. Endoplasmic reticulum. Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity Ref.2.
Tissue specificity	Expressed most abundantly in the small intestine, and to a much lesser extent in the lung, liver, adrenal gland, adipose tissue and kidney. Ref.1
Induction	Expression decreases in response to fast and increases after high sucrose diet. Ref.2
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 Mitochondrion Mitochondrion outer membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to insulin stimulus Inferred from expression pattern. Source: RGD fatty acid metabolic process Traceable author statement Ref.1. Source: RGD fatty acid transport Inferred from genetic interaction. Source: RGD positive regulation of plasma membrane long-chain fatty acid transport Inferred from direct assay Ref.2. Source: RGD positive regulation of triglyceride biosynthetic process Inferred from direct assay Ref.2. Source: RGD response to cholesterol Inferred from expression pattern Ref.1. Source: RGD response to glucose stimulus Inferred from expression pattern. Source: RGD response to nutrient Inferred from expression pattern. Source: RGD response to sucrose stimulus Inferred from expression pattern Ref.1. Source: RGD
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer 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 direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 683	683	Long-chain-fatty-acid--CoA ligase 5		PRO_0000193114
Regions
	Transmembrane	12 – 32	21	Helical; Signal-anchor for type III membrane protein; Potential
	Topological domain	33 – 683	651	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	O88813 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D4EC2A58FD29040C	FASTA	683	76,405
	10 20 30 40 50 60 MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF 70 80 90 100 110 120 QKNNDLILYY FSDAKTLYEV FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS 130 140 150 160 170 180 CLLHKGYKPS QDQFIGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGAEA IIYVINRADI 190 200 210 220 230 240 SVVICDTPQK ATMLIENVEK DLTPGLKTVI LMDPFDDDLM KRGEKCGIEM LSLHDAENLG 250 260 270 280 290 300 KENFKKPMPP NPEDLSVICF TSGTTGDPKG AMLTHQNIVS NMAAFLKFLE PIFQPTPEDV 310 320 330 340 350 360 TISYLPLAHM FERLVQGVIF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD 370 380 390 400 410 420 KVQNEAKTPL KKFLLNLAII SKFNEVRNGI IRRNSLWDKL VFSKIQSSLG GKVRLMITGA 430 440 450 460 470 480 APISTPVLTF FRAAMGCWVF EAYGQTECTA GCSITSPGDW TAGHVGTPVS CNFVKLEDVA 490 500 510 520 530 540 DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIIDR 550 560 570 580 590 600 KKNIFKLAQG EYIAPEKIEN VYSRSRPILQ VFVHGESLRS FLIGVVVPDP ESLPSFAAKI 610 620 630 640 650 660 GVKGSFEELC QNQCVKKAIL EDLQKVGKEG GLKSFEQVKS IFVHPEPFSI ENGLLTPTLK 670 680 AKRVELAKFF QTQIKSLYES IEE

References

[1]	"A novel acyl-CoA synthetase, ACS5, expressed in intestinal epithelial cells and proliferating preadipocytes." Oikawa E., Iijima H., Suzuki T., Sasano H., Sato H., Kamataki A., Nagura H., Kang M.-J., Fujino T., Suzuki H., Yamamoto T.T. J. Biochem. 124:679-685(1998) [PubMed: 9722683] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells." Mashek D.G., McKenzie M.A., Van Horn C.G., Coleman R.A. J. Biol. Chem. 281:945-950(2006) [PubMed: 16263710] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[3]	"Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation." Zhou Y., Abidi P., Kim A., Chen W., Huang T.-T., Kraemer F.B., Liu J. Arterioscler. Thromb. Vasc. Biol. 27:2198-2205(2007) [PubMed: 17761945] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012933 mRNA. Translation: BAA33581.1.
IPI	IPI00213231.
PIR	JE0262.
RefSeq	NP_446059.1. NM_053607.1.
UniGene	Rn.105862.
3D structure databases
ProteinModelPortal	O88813.
ModBase	Search...
Protein-protein interaction databases
STRING	O88813.
Proteomic databases
PRIDE	O88813.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	94340.
KEGG	rno:94340.
Organism-specific databases
CTD	51703.
RGD	69402. Acsl5.
Phylogenomic databases
eggNOG	roNOG11371.
HOVERGEN	HBG050452.
OrthoDB	EOG4P2Q1T.
PhylomeDB	O88813.
Enzyme and pathway databases
BRENDA	6.2.1.3. 5301.
Gene expression databases
Genevestigator	O88813.
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...
Other
NextBio	617929.

Entry information

Entry name

ACSL5_RAT

Accession

Primary (citable) accession number: O88813

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1998
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program