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Protein

Long chain acyl-CoA synthetase 3

Gene

LACS3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi228 – 23912ATPSequence 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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G64400-MONOMER.
MetaCyc:AT1G64400-MONOMER.
ReactomeiREACT_235205. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Long chain acyl-CoA synthetase 3 (EC:6.2.1.3)
Gene namesi
Name:LACS3
Ordered Locus Names:At1g64400
ORF Names:F15H21.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G64400.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665Long chain acyl-CoA synthetase 3PRO_0000401411Add
BLAST

Proteomic databases

PaxDbiQ9C7W4.
PRIDEiQ9C7W4.

Expressioni

Gene expression databases

GenevestigatoriQ9C7W4.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G64400.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9C7W4.
SMRiQ9C7W4. Positions 69-586.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 51925Fatty acid-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ9C7W4.
KOiK01897.
OMAiFESICRN.
PhylomeDBiQ9C7W4.

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.

Q9C7W4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATGRYIVEV EKGKQGVDGG SPSVGPVYRS IYAKDGFPEP PDDLVSAWDI
60 70 80 90 100
FRLSVEKSPN NPMLGRREIV DGKAGKYVWQ TYKEVHNVVI KLGNSIRTIG
110 120 130 140 150
VGKGDKCGIY GANSPEWIIS MEACNAHGLY CVPLYDTLGA GAIEFIICHA
160 170 180 190 200
EVSLAFAEEN KISELLKTAP KSTKYLKYIV SFGEVTNNQR VEAERHRLTI
210 220 230 240 250
YSWDQFLKLG EGKHYELPEK RRSDVCTIMY TSGTTGDPKG VLLTNESIIH
260 270 280 290 300
LLEGVKKLLK TIDEELTSKD VYLSYLPLAH IFDRVIEELC IYEAASIGFW
310 320 330 340 350
RGDVKILIED IAALKPTVFC AVPRVLERIY TGLQQKLSDG GFVKKKLFNF
360 370 380 390 400
AFKYKHKNME KGQPHEQASP IADKIVFKKV KEGLGGNVRL ILSGAAPLAA
410 420 430 440 450
HIESFLRVVA CAHVLQGYGL TESCGGTFVS IPNELSMLGT VGPPVPNVDI
460 470 480 490 500
RLESVPEMGY DALASNPRGE ICIRGKTLFS GYYKREDLTQ EVFIDGWLHT
510 520 530 540 550
GDVGEWQPDG AMKIIDRKKN IFKLSQGEYV AVENLENIYS HVAAIESIWV
560 570 580 590 600
YGNSYESYLV AVVCPSKIQI EHWAKEHKVS GDFESICRNQ KTKEFVLGEF
610 620 630 640 650
NRVAKDKKLK GFELIKGVHL DTVPFDMERD LITPSYKMKR PQLLKYYQKE
660
IDEMYKKNRE VQLRV
Length:665
Mass (Da):74,751
Last modified:June 1, 2001 - v1
Checksum:iB546A845F101DB6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503753 mRNA. Translation: AAM28870.1.
AC066689 Genomic DNA. Translation: AAG51719.1.
CP002684 Genomic DNA. Translation: AEE34237.1.
AY039935 mRNA. Translation: AAK64039.1.
AY079314 mRNA. Translation: AAL85045.1.
PIRiB96668.
RefSeqiNP_176622.1. NM_105115.3.
UniGeneiAt.24316.

Genome annotation databases

EnsemblPlantsiAT1G64400.1; AT1G64400.1; AT1G64400.
GeneIDi842748.
KEGGiath:AT1G64400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF503753 mRNA. Translation: AAM28870.1.
AC066689 Genomic DNA. Translation: AAG51719.1.
CP002684 Genomic DNA. Translation: AEE34237.1.
AY039935 mRNA. Translation: AAK64039.1.
AY079314 mRNA. Translation: AAL85045.1.
PIRiB96668.
RefSeqiNP_176622.1. NM_105115.3.
UniGeneiAt.24316.

3D structure databases

ProteinModelPortaliQ9C7W4.
SMRiQ9C7W4. Positions 69-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G64400.1-P.

Proteomic databases

PaxDbiQ9C7W4.
PRIDEiQ9C7W4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G64400.1; AT1G64400.1; AT1G64400.
GeneIDi842748.
KEGGiath:AT1G64400.

Organism-specific databases

TAIRiAT1G64400.

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
InParanoidiQ9C7W4.
KOiK01897.
OMAiFESICRN.
PhylomeDBiQ9C7W4.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciARA:AT1G64400-MONOMER.
MetaCyc:AT1G64400-MONOMER.
ReactomeiREACT_235205. Synthesis of very long-chain fatty acyl-CoAs.

Gene expression databases

GenevestigatoriQ9C7W4.

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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.

Entry informationi

Entry nameiLACS3_ARATH
AccessioniPrimary (citable) accession number: Q9C7W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 83 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, 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.