Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Long chain acyl-CoA synthetase 6, peroxisomal

Gene

LACS6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.2 Publications

Cofactori

Mg2+By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 27712ATPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB
  2. multicellular organismal development Source: UniProtKB-KW
  3. response to ozone Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G05970-MONOMER.
MetaCyc:AT3G05970-MONOMER.
ReactomeiREACT_187610. alpha-linolenic acid (ALA) metabolism.
REACT_187634. PPARA activates gene expression.
REACT_221735. Linoleic acid (LA) metabolism.
REACT_235205. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Long chain acyl-CoA synthetase 6, peroxisomal (EC:6.2.1.3)
Gene namesi
Name:LACS6
Ordered Locus Names:At3g05970
ORF Names:F2O10.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G05970.

Subcellular locationi

Peroxisome 2 Publications. Glyoxysome membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. glyoxysomal membrane Source: UniProtKB-SubCell
  2. glyoxysome Source: UniProtKB-KW
  3. membrane Source: TAIR
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Membrane, Peroxisome

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 3838Removed in mature form1 PublicationPRO_0000401414Add
BLAST
Chaini39 – 701663Long chain acyl-CoA synthetase 6, peroxisomalPRO_0000401415Add
BLAST

Proteomic databases

PaxDbiQ8LPS1.
PRIDEiQ8LPS1.

Expressioni

Tissue specificityi

Preferentially expressed in seeds and senescent leaves.1 Publication

Developmental stagei

Induced during seed germination.1 Publication

Inductioni

Up-regulated by ozone.1 Publication

Gene expression databases

GenevestigatoriQ8LPS1.

Interactioni

Protein-protein interaction databases

BioGridi5102. 2 interactions.
STRINGi3702.AT3G05970.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8LPS1.
SMRiQ8LPS1. Positions 119-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni526 – 55025Fatty acid-bindingSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi15 – 239Microbody targeting signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ8LPS1.
KOiK01897.
OMAiCTIDEMG.
PhylomeDBiQ8LPS1.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8LPS1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSSSSSSSA AARRRINAIH SHLVTSSRSS PLLRSNPTAG EFCLDNGYSV
60 70 80 90 100
VLPEKLNTGS WNVYRSAKSP FKLVSRFPDH PDIATLHDNF EHAVHDFRDY
110 120 130 140 150
KYLGTRVRVD GTVGDYKWMT YGEAGTARTA LGSGLVHHGI PMGSSVGIYF
160 170 180 190 200
INRPEWLIVD HACSSYSYVS VPLYDTLGPD AVKFIVNHAT VQAIFCVAET
210 220 230 240 250
LNSLLSCLSE MPSVRLVVVV GGLIESLPSL PSSSGVKVVS YSVLLNQGRS
260 270 280 290 300
NPQRFFPPKP DDVATICYTS GTTGTPKGVV LTHANLIANV AGSSFSVKFF
310 320 330 340 350
SSDVYISYLP LAHIYERANQ ILTVYFGVAV GFYQGDNMKL LDDLAALRPT
360 370 380 390 400
VFSSVPRLYN RIYAGIINAV KTSGGLKERL FNAAYNAKKQ ALLNGKSASP
410 420 430 440 450
IWDRLVFNKI KDRLGGRVRF MTSGASPLSP EVMEFLKVCF GGRVTEGYGM
460 470 480 490 500
TETSCVISGM DEGDNLTGHV GSPNPACEVK LVDVPEMNYT SADQPHPRGE
510 520 530 540 550
ICVRGPIIFT GYYKDEIQTK EVIDEDGWLH TGDIGLWLPG GRLKIIDRKK
560 570 580 590 600
NIFKLAQGEY IAPEKIENVY AKCKFVGQCF IYGDSFNSSL VAVVSVDPDV
610 620 630 640 650
LKSWAASEGI KGGDLRELCN NPRVKAAVLS DMDTVGREAQ LRGFEFAKAV
660 670 680 690 700
TLVLEPFTLE NGLLTPTFKI KRPQAKEYFA EAITNMYKEL GASDPSANRG

L
Length:701
Mass (Da):76,603
Last modified:October 1, 2002 - v1
Checksum:i4A0F06A05FA13022
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601S → N in BAB40450. (PubMed:12481085)Curated
Sequence conflicti139 – 1391G → V in AAM28873. (PubMed:12177484)Curated
Sequence conflicti224 – 2241I → N in BAB40450. (PubMed:12481085)Curated
Sequence conflicti479 – 4791V → I in AAM28873. (PubMed:12177484)Curated
Sequence conflicti517 – 5171I → V in BAB40450. (PubMed:12481085)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_566265.1. NM_111471.2.
UniGeneiAt.25229.

Genome annotation databases

EnsemblPlantsiAT3G05970.1; AT3G05970.1; AT3G05970.
GeneIDi819767.
KEGGiath:AT3G05970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_566265.1. NM_111471.2.
UniGeneiAt.25229.

3D structure databases

ProteinModelPortaliQ8LPS1.
SMRiQ8LPS1. Positions 119-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5102. 2 interactions.
STRINGi3702.AT3G05970.1-P.

Proteomic databases

PaxDbiQ8LPS1.
PRIDEiQ8LPS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G05970.1; AT3G05970.1; AT3G05970.
GeneIDi819767.
KEGGiath:AT3G05970.

Organism-specific databases

GeneFarmi2576. 207.
TAIRiAT3G05970.

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ8LPS1.
KOiK01897.
OMAiCTIDEMG.
PhylomeDBiQ8LPS1.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciARA:AT3G05970-MONOMER.
MetaCyc:AT3G05970-MONOMER.
ReactomeiREACT_187610. alpha-linolenic acid (ALA) metabolism.
REACT_187634. PPARA activates gene expression.
REACT_221735. Linoleic acid (LA) metabolism.
REACT_235205. Synthesis of very long-chain fatty acyl-CoAs.

Gene expression databases

GenevestigatoriQ8LPS1.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiLACS6_ARATH
AccessioniPrimary (citable) accession number: Q8LPS1
Secondary accession number(s): Q8LKS6, Q9C5U7, Q9SFG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.