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Q9XIA9 (LACS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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 2

EC=6.2.1.3
Alternative name(s):
Protein Botrytis resistant 1
Protein LATERAL ROOT DEVELOPMENT 2
Gene names
Name:LACS2
Synonyms:BRE1, LRD2, SMA4
Ordered Locus Names:At1g49430
ORF Names:F13F21.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length665 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. Acts in the cutin pathway. Preferentially uses palmitate, palmitoleate, oleate and linoleate. Required for repression of lateral root formation through its role in cutin biosynthesis and subsequent aerial tissues permeability. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

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.

Subcellular location

Endoplasmic reticulum Ref.13.

Tissue specificity

Expressed along the entire length of the stem, but expression was not entirely epidermal specific, with some expression found in internal cell layers as well. Was expressed in leave epidermal cells, flowers (sepals, petals, stamens, filaments and carpel), siliques and developing seeds. In roots, expression was detected in an internal cell layer, probably the endodermal layer. Ref.6 Ref.12

Induction

Positively regulated by WIN1. Ref.9

Disruption phenotype

Dwarf phenotype with smaller, wrinkled leaves and overall reduced vigor. Higher water loss rate and susceptibility to drought stress. Defective in the cuticular membrane. Strong resistance to virulent Botrytis cinerea and enhanced susceptibility to avirulent Pseudomonas syringae. Ref.6 Ref.8 Ref.10 Ref.13

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Long chain acyl-CoA synthetase 2
PRO_0000401410

Regions

Nucleotide binding228 – 23912ATP Potential
Region496 – 52025Fatty acid-binding Potential

Sequences

Sequence LengthMass (Da)Tools
Q9XIA9 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9B1566F79A1B2D1A

FASTA66574,389
        10         20         30         40         50         60 
MSLAADNVLL VEEGRPATAE HPSAGPVYRC KYAKDGLLDL PTDIDSPWQF FSEAVKKYPN 

        70         80         90        100        110        120 
EQMLGQRVTT DSKVGPYTWI TYKEAHDAAI RIGSAIRSRG VDPGHCCGIY GANCPEWIIA 

       130        140        150        160        170        180 
MEACMSQGIT YVPLYDSLGV NAVEFIINHA EVSLVFVQEK TVSSILSCQK GCSSNLKTIV 

       190        200        210        220        230        240 
SFGEVSSTQK EEAKNQCVSL FSWNEFSLMG NLDEANLPRK RKTDICTIMY TSGTTGEPKG 

       250        260        270        280        290        300 
VILNNAAISV QVLSIDKMLE VTDRSCDTSD VFFSYLPLAH CYDQVMEIYF LSRGSSVGYW 

       310        320        330        340        350        360 
RGDIRYLMDD VQALKPTVFC GVPRVYDKLY AGIMQKISAS GLIRKKLFDF AYNYKLGNMR 

       370        380        390        400        410        420 
KGFSQEEASP RLDRLMFDKI KEALGGRAHM LLSGAAPLPR HVEEFLRIIP ASNLSQGYGL 

       430        440        450        460        470        480 
TESCGGSFTT LAGVFSMVGT VGVPMPTVEA RLVSVPEMGY DAFSADVPRG EICLRGNSMF 

       490        500        510        520        530        540 
SGYHKRQDLT DQVLIDGWFH TGDIGEWQED GSMKIIDRKK NIFKLSQGEY VAVENLENTY 

       550        560        570        580        590        600 
SRCPLIAQIW VYGNSFESFL VGVVVPDRKA IEDWAKLNYQ SPNDFESLCQ NLKAQKYFLD 

       610        620        630        640        650        660 
ELNSTAKQYQ LKGFEMLKAI HLEPNPFDIE RDLITPTFKL KRPQLLQHYK GIVDQLYSEA 


KRSMA 

« 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 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. expand/collapse author list , 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. 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.
[6]"The acyl-CoA synthetase encoded by LACS2 is essential for normal cuticle development in Arabidopsis."
Schnurr J., Shockey J., Browse J.
Plant Cell 16:629-642(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[7]"Osmotic regulation of root system architecture."
Deak K.I., Malamy J.
Plant J. 43:17-28(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A permeable cuticle in Arabidopsis leads to a strong resistance to Botrytis cinerea."
Bessire M., Chassot C., Jacquat A.C., Humphry M., Borel S., Petetot J.M., Metraux J.P., Nawrath C.
EMBO J. 26:2158-2168(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"The transcription factor WIN1/SHN1 regulates Cutin biosynthesis in Arabidopsis thaliana."
Kannangara R., Branigan C., Liu Y., Penfield T., Rao V., Mouille G., Hoefte H., Pauly M., Riechmann J.L., Broun P.
Plant Cell 19:1278-1294(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY WIN1.
[10]"Mutations in LACS2, a long-chain acyl-coenzyme A synthetase, enhance susceptibility to avirulent Pseudomonas syringae but confer resistance to Botrytis cinerea in Arabidopsis."
Tang D., Simonich M.T., Innes R.W.
Plant Physiol. 144:1093-1103(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[11]"Root system architecture in Arabidopsis grown in culture is regulated by sucrose uptake in the aerial tissues."
Macgregor D.R., Deak K.I., Ingram P.A., Malamy J.E.
Plant Cell 20:2643-2660(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Arabidopsis CER8 encodes LONG-CHAIN ACYL-COA SYNTHETASE 1 (LACS1) that has overlapping functions with LACS2 in plant wax and cutin synthesis."
Lue S., Song T., Kosma D.K., Parsons E.P., Rowland O., Jenks M.A.
Plant J. 59:553-564(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"Organ fusion and defective cuticle function in a lacs1 lacs2 double mutant of Arabidopsis."
Weng H., Molina I., Shockey J., Browse J.
Planta 231:1089-1100(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503752 mRNA. Translation: AAM28869.1.
AC007504 Genomic DNA. Translation: AAD43157.1.
CP002684 Genomic DNA. Translation: AEE32429.1.
AY065424 mRNA. Translation: AAL38865.1.
AY094420 mRNA. Translation: AAM19793.1.
BT001970 mRNA. Translation: AAN71969.1.
PIRG96530.
RefSeqNP_175368.2. NM_103833.4.
UniGeneAt.27757.

3D structure databases

ProteinModelPortalQ9XIA9.
SMRQ9XIA9. Positions 48-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G49430.1-P.

Protein family/group databases

TCDB4.C.1.1.14. the proposed fatty acid transporter (fat) family.

Proteomic databases

PaxDbQ9XIA9.
PRIDEQ9XIA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G49430.1; AT1G49430.1; AT1G49430.
GeneID841367.
KEGGath:AT1G49430.

Organism-specific databases

TAIRAT1G49430.

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
InParanoidQ9XIA9.
KOK01897.
OMARIGSAIR.
PhylomeDBQ9XIA9.
ProtClustDBPLN02861.

Enzyme and pathway databases

BioCycARA:AT1G49430-MONOMER.
MetaCyc:AT1G49430-MONOMER.
SABIO-RKQ9XIA9.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorQ9XIA9.

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 nameLACS2_ARATH
AccessionPrimary (citable) accession number: Q9XIA9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 85 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