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Q8LPS1 (LACS6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 acyl-CoA synthetase 6, peroxisomal

EC=6.2.1.3
Gene names
Name:LACS6
Ordered Locus Names:At3g05970
ORF Names:F2O10.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate. Might play a regulatory role both in fatty acid import into glyoxysomes and in fatty acid beta-oxidation. Displays redundant function with LACS7 into the seed development process. Ref.2 Ref.8

Catalytic activity

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1 Ref.6

Cofactor

Magnesium By similarity.

Pathway

Lipid metabolism; fatty acid metabolism.

Subcellular location

Peroxisome. Glyoxysome membrane; Peripheral membrane protein By similarity Ref.2 Ref.6.

Tissue specificity

Preferentially expressed in seeds and senescent leaves. Ref.9

Developmental stage

Induced during seed germination. Ref.6

Induction

Up-regulated by ozone. Ref.9

Disruption phenotype

Seedlings of the lacs6 and lacs7 double mutant were arrested in postgerminative growth due to inability to mobilize fatty acids into beta-oxidation, a necessary process to pursue the development. Ref.8

Sequence similarities

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

Sequence caution

The sequence AAF23219.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 3838Removed in mature form
PRO_0000401414
Chain39 – 701663Long chain acyl-CoA synthetase 6, peroxisomal
PRO_0000401415

Regions

Nucleotide binding266 – 27712ATP Potential
Region526 – 55025Fatty acid-binding Potential
Motif15 – 239Microbody targeting signal Potential

Experimental info

Sequence conflict601S → N in BAB40450. Ref.2
Sequence conflict1391G → V in AAM28873. Ref.1
Sequence conflict2241I → N in BAB40450. Ref.2
Sequence conflict4791V → I in AAM28873. Ref.1
Sequence conflict5171I → V in BAB40450. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8LPS1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4A0F06A05FA13022

FASTA70176,603
        10         20         30         40         50         60 
MDSSSSSSSA AARRRINAIH SHLVTSSRSS PLLRSNPTAG EFCLDNGYSV VLPEKLNTGS 

        70         80         90        100        110        120 
WNVYRSAKSP FKLVSRFPDH PDIATLHDNF EHAVHDFRDY KYLGTRVRVD GTVGDYKWMT 

       130        140        150        160        170        180 
YGEAGTARTA LGSGLVHHGI PMGSSVGIYF INRPEWLIVD HACSSYSYVS VPLYDTLGPD 

       190        200        210        220        230        240 
AVKFIVNHAT VQAIFCVAET LNSLLSCLSE MPSVRLVVVV GGLIESLPSL PSSSGVKVVS 

       250        260        270        280        290        300 
YSVLLNQGRS NPQRFFPPKP DDVATICYTS GTTGTPKGVV LTHANLIANV AGSSFSVKFF 

       310        320        330        340        350        360 
SSDVYISYLP LAHIYERANQ ILTVYFGVAV GFYQGDNMKL LDDLAALRPT VFSSVPRLYN 

       370        380        390        400        410        420 
RIYAGIINAV KTSGGLKERL FNAAYNAKKQ ALLNGKSASP IWDRLVFNKI KDRLGGRVRF 

       430        440        450        460        470        480 
MTSGASPLSP EVMEFLKVCF GGRVTEGYGM TETSCVISGM DEGDNLTGHV GSPNPACEVK 

       490        500        510        520        530        540 
LVDVPEMNYT SADQPHPRGE ICVRGPIIFT GYYKDEIQTK EVIDEDGWLH TGDIGLWLPG 

       550        560        570        580        590        600 
GRLKIIDRKK NIFKLAQGEY IAPEKIENVY AKCKFVGQCF IYGDSFNSSL VAVVSVDPDV 

       610        620        630        640        650        660 
LKSWAASEGI KGGDLRELCN NPRVKAAVLS DMDTVGREAQ LRGFEFAKAV TLVLEPFTLE 

       670        680        690        700 
NGLLTPTFKI KRPQAKEYFA EAITNMYKEL GASDPSANRG L 

« Hide

References

« Hide 'large scale' references
[1]"Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that participate in fatty acid and glycerolipid metabolism."
Shockey J.M., Fulda M.S., Browse J.A.
Plant Physiol. 129:1710-1722(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, ENZYME ACTIVITY.
[2]"Molecular characterization of an Arabidopsis acyl-coenzyme A synthetase localized on glyoxysomal membranes."
Hayashi H., De Bellis L., Hayashi Y., Nito K., Kato A., Hayashi M., Hara-Nishimura I., Nishimura M.
Plant Physiol. 130:2019-2026(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-60, FUNCTION, SUBCELLULAR LOCATION.
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Two long-chain acyl-CoA synthetases from Arabidopsis thaliana involved in peroxisomal fatty acid beta-oxidation."
Fulda M., Shockey J., Werber M., Wolter F.P., Heinz E.
Plant J. 32:93-103(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, ENZYME ACTIVITY.
[7]"Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases."
Shockey J.M., Fulda M.S., Browse J.
Plant Physiol. 132:1065-1076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY ORGANIZATION.
[8]"Peroxisomal Acyl-CoA synthetase activity is essential for seedling development in Arabidopsis thaliana."
Fulda M., Schnurr J., Abbadi A., Heinz E., Browse J.
Plant Cell 16:394-405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5."
Bonsegna S., Slocombe S.P., De Bellis L., Baker A.
Arch. Biochem. Biophys. 443:74-81(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503756 mRNA. Translation: AAM28873.1.
AB030317 mRNA. Translation: BAB40450.1.
AC013454 Genomic DNA. Translation: AAF23219.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74324.1.
AY094418 mRNA. Translation: AAM19792.1.
BT001117 mRNA. Translation: AAN64508.1.
RefSeqNP_566265.1. NM_111471.2.
UniGeneAt.25229.

3D structure databases

ProteinModelPortalQ8LPS1.
SMRQ8LPS1. Positions 80-680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5102. 1 interaction.
STRING3702.AT3G05970.1-P.

Proteomic databases

PaxDbQ8LPS1.
PRIDEQ8LPS1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G05970.1; AT3G05970.1; AT3G05970.
GeneID819767.
KEGGath:AT3G05970.

Organism-specific databases

GeneFarm2576. 207.
TAIRAT3G05970.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
InParanoidQ8LPS1.
KOK01897.
OMALKIKRHI.
PhylomeDBQ8LPS1.
ProtClustDBPLN02736.

Enzyme and pathway databases

BioCycARA:AT3G05970-MONOMER.
MetaCyc:AT3G05970-MONOMER.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorQ8LPS1.

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 nameLACS6_ARATH
AccessionPrimary (citable) accession number: Q8LPS1
Secondary accession number(s): Q8LKS6, Q9C5U7, Q9SFG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names