Long-chain-fatty-acid--CoA ligase 6 - Rattus norvegicus (Rat)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Natural variations

Experimental info

Preferred order of sections

Molecule processing

Regions

Natural variations

Experimental info

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

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P33124 (ACSL6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended name:
Long-chain-fatty-acid--CoA ligase 6
EC=6.2.1.3

Alternative name(s):
Long-chain acyl-CoA synthetase 6
Short name=LACS 6
Long-chain-fatty-acid--CoA ligase, brain isozyme

Gene names

Name:	Acsl6
Synonyms:	Acs2, Facl6

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Sequence length	697 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Function	Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid.
Catalytic activity	ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium.
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.
Tissue specificity	Expressed predominantly in brain and, to a much lesser extent, in heart and adrenal.
Developmental stage	Detected 5 days after birth, and increased in a coordinate fashion during the development of brain, and the amount did not decrease when myelination was completed.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane Peroxisome
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to insulin stimulus Inferred from expression pattern PubMed 16428347. Source: RGD fatty acid transport Inferred from genetic interaction PubMed 16466685. Source: RGD neuroblast proliferation Inferred from electronic annotation. Source: Compara neuron development Inferred from expression pattern PubMed 16848632. Source: RGD phospholipid biosynthetic process Inferred from mutant phenotype PubMed 15655248. Source: RGD positive regulation of neuron projection development Inferred from mutant phenotype PubMed 15051725. Source: RGD positive regulation of plasma membrane long-chain fatty acid transport Inferred from mutant phenotype PubMed 15655248. Source: RGD positive regulation of triglyceride biosynthetic process Inferred from genetic interaction PubMed 16466685. Source: RGD response to gravity Inferred from expression pattern PubMed 16848632. Source: RGD response to hypoxia Inferred from expression pattern PubMed 15942958. Source: RGD response to nutrient Inferred from expression pattern PubMed 16772660. Source: RGD response to steroid hormone stimulus Inferred from expression pattern PubMed 11118002. Source: RGD triglyceride metabolic process Inferred from genetic interaction PubMed 16466685. 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 nucleus Inferred from direct assay PubMed 15942958. Source: RGD 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 direct assay Ref.3. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 20429931 PubMed 20429931. Source: UniProtKB
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 697

697

Long-chain-fatty-acid--CoA ligase 6

PRO_0000193117

Transmembrane

25 – 45

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

Topological domain

46 – 697

652

Cytoplasmic Potential

Alternative sequence

M → MLTFFLVSGGSLWLFAEIAL SLLEKM in isoform 2.

VSP_037825

Sequence conflict

558

H → D in AAB19809. Ref.1

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 0B0CA7EFD653E2BE Show »	FASTA	697	78,180
10 20 30 40 50 60 MQTQEILRIL RLPELSDLGQ FFRSLSATTL VSMGALAAIL AYWLTHRPKA LQPPCNLLMQ 70 80 90 100 110 120 SEEVEDSGGA RRSVIGDCTQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPEQPYQW 130 140 150 160 170 180 LSYQEVAKRA EFLGSGLLQH DCKVGTEQFI GVFAQNRPEW IIAELACYTY SMVVVPLYDT 190 200 210 220 230 240 LGPGSIRYII NTADICTVIV DKPHKAILLL EHVERKETPG LKLVILMEPF DDALRERGKK 250 260 270 280 290 300 CGVDIKSMQA IEDSGQENHR VPVPPRPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF 310 320 330 340 350 360 LKVTESQWAP TCADVHFSYL PLAHMFERMV QSVVYCHGGR VGFFQGDIRL LSDDMKALRP 370 380 390 400 410 420 TIFPVVPRLL NRMYDKIFHQ ADTSLKRWLL EFAAKRKQAE VRSGIIRNNS IWDELFFNKI 430 440 450 460 470 480 QASLGGHVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV 490 500 510 520 530 540 GAPLPCNHIK LVDAEELNYW TSKGEGEICV KGPNVFKGYL KDEDRTKEAL DSDGWLHTGD 550 560 570 580 590 600 IGKWLPEGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS EPVAQIYVHG DSLKAFLVGI 610 620 630 640 650 660 VVPDPEVMPC WAQKKGIEGN YQELCKSKEL KKAILDDMVM LGKESGLHSF EQVKAIYIHC 670 680 690 DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM « Hide
Isoform 2 [UniParc]. Checksum: 3E3F54AAFDF059F8 Show »	FASTA	722	80,949
10 20 30 40 50 60 MLTFFLVSGG SLWLFAEIAL SLLEKMQTQE ILRILRLPEL SDLGQFFRSL SATTLVSMGA 70 80 90 100 110 120 LAAILAYWLT HRPKALQPPC NLLMQSEEVE DSGGARRSVI GDCTQLLTHY YDDARTMYQV 130 140 150 160 170 180 FRRGLSISGN GPCLGFRKPE QPYQWLSYQE VAKRAEFLGS GLLQHDCKVG TEQFIGVFAQ 190 200 210 220 230 240 NRPEWIIAEL ACYTYSMVVV PLYDTLGPGS IRYIINTADI CTVIVDKPHK AILLLEHVER 250 260 270 280 290 300 KETPGLKLVI LMEPFDDALR ERGKKCGVDI KSMQAIEDSG QENHRVPVPP RPDDLSIVCF 310 320 330 340 350 360 TSGTTGNPKG AMLTHGNVVA DFSGFLKVTE SQWAPTCADV HFSYLPLAHM FERMVQSVVY 370 380 390 400 410 420 CHGGRVGFFQ GDIRLLSDDM KALRPTIFPV VPRLLNRMYD KIFHQADTSL KRWLLEFAAK 430 440 450 460 470 480 RKQAEVRSGI IRNNSIWDEL FFNKIQASLG GHVRMIVTGA APASPTVLGF LRAALGCQVY 490 500 510 520 530 540 EGYGQTECTA GCTFTTPGDW TSGHVGAPLP CNHIKLVDAE ELNYWTSKGE GEICVKGPNV 550 560 570 580 590 600 FKGYLKDEDR TKEALDSDGW LHTGDIGKWL PEGTLKIIDR KKHIFKLAQG EYVAPEKIEN 610 620 630 640 650 660 IYIRSEPVAQ IYVHGDSLKA FLVGIVVPDP EVMPCWAQKK GIEGNYQELC KSKELKKAIL 670 680 690 700 710 720 DDMVMLGKES GLHSFEQVKA IYIHCDMFSV QNGLLTPTLK AKRPELREYF KKQIEELYSI SM « Hide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of cDNA encoding the phosphatidylinositol kinase from rat brain." Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K., Takenawa T. J. Biol. Chem. 266:17580-17583(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 491-503; 544-551; 573-579 AND 633-636. Tissue: Brain.
[2]	Erratum Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K., Takenawa T. J. Biol. Chem. 267:25620-25620(1992) [PubMed] [Europe PMC] [Abstract] Cited for: RETRACTION.
[3]	"Cloning and functional expression of a novel long-chain acyl-CoA synthetase expressed in brain." Fujino T., Yamamoto T. J. Biochem. 111:197-203(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Wistar. Tissue: Brain.
[4]	"Amgen rat EST program." Amgen EST program Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-160 (ISOFORM 2). Tissue: Spinal ganglion.
+	Additional computationally mapped references.

Sequence databases
EMBL GenBank DDBJ	S56508 mRNA. Translation: AAB19809.2. D10041 mRNA. Translation: BAA00932.1. CB582512 mRNA. No translation available.
IPI	IPI00324041. IPI00776455.
PIR	JX0205.
RefSeq	NP_570095.1. NM_130739.1.
UniGene	Rn.33697.
3D structure databases
ProteinModelPortal	P33124.
ModBase	Search...
PTM databases
PhosphoSite	P33124.
Proteomic databases
PaxDb	P33124.
PRIDE	P33124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000030760; ENSRNOP00000033248; ENSRNOG00000026745. ENSRNOT00000058817; ENSRNOP00000055608; ENSRNOG00000026745.
GeneID	117243.
KEGG	rno:117243.
UCSC	RGD:69403. rat.
Organism-specific databases
CTD	23305.
RGD	69403. Acsl6.
Phylogenomic databases
eggNOG	COG1022.
GeneTree	ENSGT00690000101725.
HOGENOM	HOG000159459.
HOVERGEN	HBG050452.
KO	K01897.
Enzyme and pathway databases
BRENDA	6.2.1.3. 5301.
Gene expression databases
ArrayExpress	P33124.
Genevestigator	P33124.
GermOnline	ENSRNOG00000026745. Rattus norvegicus.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	620076.

Entry name

ACSL6_RAT

Accession

Primary (citable) accession number: P33124
Secondary accession number(s): Q63835

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P33124-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P33124-2)

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MLTFFLVSGGSLWLFAEIALSLLEKM