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Q9T0A0 (LACS4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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 4

EC=6.2.1.3
Gene names
Name:LACS4
Ordered Locus Names:At4g23850
ORF Names:T32A16_20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 and linoleate.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Pathway

Lipid metabolism; fatty acid metabolism.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 666666Long chain acyl-CoA synthetase 4
PRO_0000401412

Regions

Nucleotide binding228 – 23912ATP Potential
Region495 – 51925Fatty acid-binding Potential

Sequences

Sequence LengthMass (Da)Tools
Q9T0A0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8E663756D60B0E57

FASTA66674,508
        10         20         30         40         50         60 
MSQQKKYIFQ VEEGKEGSDG RPSVGPVYRS IFAKDGFPDP IEGMDSCWDV FRMSVEKYPN 

        70         80         90        100        110        120 
NPMLGRREIV DGKPGKYVWQ TYQEVYDIVM KLGNSLRSVG VKDEAKCGIY GANSPEWIIS 

       130        140        150        160        170        180 
MEACNAHGLY CVPLYDTLGA DAVEFIISHS EVSIVFVEEK KISELFKTCP NSTEYMKTVV 

       190        200        210        220        230        240 
SFGGVSREQK EEAETFGLVI YAWDEFLKLG EGKQYDLPIK KKSDICTIMY TSGTTGDPKG 

       250        260        270        280        290        300 
VMISNESIVT LIAGVIRLLK SANEALTVKD VYLSYLPLAH IFDRVIEECF IQHGAAIGFW 

       310        320        330        340        350        360 
RGDVKLLIED LAELKPTIFC AVPRVLDRVY SGLQKKLSDG GFLKKFIFDS AFSYKFGYMK 

       370        380        390        400        410        420 
KGQSHVEASP LFDKLVFSKV KQGLGGNVRI ILSGAAPLAS HVESFLRVVA CCHVLQGYGL 

       430        440        450        460        470        480 
TESCAGTFVS LPDELGMLGT VGPPVPNVDI RLESVPEMEY DALASTARGE ICIRGKTLFS 

       490        500        510        520        530        540 
GYYKREDLTK EVLIDGWLHT GDVGEWQPDG SMKIIDRKKN IFKLSQGEYV AVENIENIYG 

       550        560        570        580        590        600 
EVQAVDSVWV YGNSFESFLI AIANPNQHIL ERWAAENGVS GDYDALCQNE KAKEFILGEL 

       610        620        630        640        650        660 
VKMAKEKKMK GFEIIKAIHL DPVPFDMERD LLTPTFKKKR PQLLKYYQSV IDEMYKTINA 


KFASRG 

« 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]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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. 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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503754 mRNA. Translation: AAM28871.1.
AL078468 Genomic DNA. Translation: CAB43885.1.
AL161560 Genomic DNA. Translation: CAB81303.1.
CP002687 Genomic DNA. Translation: AEE84812.1.
AY049239 mRNA. Translation: AAK83581.1.
PIRT08904.
RefSeqNP_194116.1. NM_118516.4.
UniGeneAt.3384.

3D structure databases

ProteinModelPortalQ9T0A0.
SMRQ9T0A0. Positions 51-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13773. 1 interaction.
STRING3702.AT4G23850.1-P.

Proteomic databases

PaxDbQ9T0A0.
PRIDEQ9T0A0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G23850.1; AT4G23850.1; AT4G23850.
GeneID828484.
KEGGath:AT4G23850.

Organism-specific databases

TAIRAT4G23850.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
InParanoidQ9T0A0.
KOK01897.
OMAICIRGDT.
PhylomeDBQ9T0A0.

Enzyme and pathway databases

BioCycARA:AT4G23850-MONOMER.
MetaCyc:AT4G23850-MONOMER.
SABIO-RKQ9T0A0.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorQ9T0A0.

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 nameLACS4_ARATH
AccessionPrimary (citable) accession number: Q9T0A0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 88 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