LACS2_ARATH
ID LACS2_ARATH Reviewed; 665 AA.
AC Q9XIA9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Long chain acyl-CoA synthetase 2;
DE EC=6.2.1.3;
DE AltName: Full=Protein Botrytis resistant 1;
DE AltName: Full=Protein LATERAL ROOT DEVELOPMENT 2;
GN Name=LACS2; Synonyms=BRE1, LRD2, SMA4; OrderedLocusNames=At1g49430;
GN ORFNames=F13F21.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND ENZYME ACTIVITY.
RX PubMed=12177484; DOI=10.1104/pp.003269;
RA Shockey J.M., Fulda M.S., Browse J.A.;
RT "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that
RT participate in fatty acid and glycerolipid metabolism.";
RL Plant Physiol. 129:1710-1722(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=14973169; DOI=10.1105/tpc.017608;
RA Schnurr J., Shockey J., Browse J.;
RT "The acyl-CoA synthetase encoded by LACS2 is essential for normal cuticle
RT development in Arabidopsis.";
RL Plant Cell 16:629-642(2004).
RN [7]
RP FUNCTION.
RX PubMed=15960613; DOI=10.1111/j.1365-313x.2005.02425.x;
RA Deak K.I., Malamy J.;
RT "Osmotic regulation of root system architecture.";
RL Plant J. 43:17-28(2005).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17396154; DOI=10.1038/sj.emboj.7601658;
RA Bessire M., Chassot C., Jacquat A.C., Humphry M., Borel S., Petetot J.M.,
RA Metraux J.P., Nawrath C.;
RT "A permeable cuticle in Arabidopsis leads to a strong resistance to
RT Botrytis cinerea.";
RL EMBO J. 26:2158-2168(2007).
RN [9]
RP INDUCTION BY WIN1.
RX PubMed=17449808; DOI=10.1105/tpc.106.047076;
RA Kannangara R., Branigan C., Liu Y., Penfield T., Rao V., Mouille G.,
RA Hoefte H., Pauly M., Riechmann J.L., Broun P.;
RT "The transcription factor WIN1/SHN1 regulates Cutin biosynthesis in
RT Arabidopsis thaliana.";
RL Plant Cell 19:1278-1294(2007).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17434992; DOI=10.1104/pp.106.094318;
RA Tang D., Simonich M.T., Innes R.W.;
RT "Mutations in LACS2, a long-chain acyl-coenzyme A synthetase, enhance
RT susceptibility to avirulent Pseudomonas syringae but confer resistance to
RT Botrytis cinerea in Arabidopsis.";
RL Plant Physiol. 144:1093-1103(2007).
RN [11]
RP FUNCTION.
RX PubMed=18952782; DOI=10.1105/tpc.107.055475;
RA Macgregor D.R., Deak K.I., Ingram P.A., Malamy J.E.;
RT "Root system architecture in Arabidopsis grown in culture is regulated by
RT sucrose uptake in the aerial tissues.";
RL Plant Cell 20:2643-2660(2008).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=19392700; DOI=10.1111/j.1365-313x.2009.03892.x;
RA Lue S., Song T., Kosma D.K., Parsons E.P., Rowland O., Jenks M.A.;
RT "Arabidopsis CER8 encodes LONG-CHAIN ACYL-COA SYNTHETASE 1 (LACS1) that has
RT overlapping functions with LACS2 in plant wax and cutin synthesis.";
RL Plant J. 59:553-564(2009).
RN [13]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20237894; DOI=10.1007/s00425-010-1110-4;
RA Weng H., Molina I., Shockey J., Browse J.;
RT "Organ fusion and defective cuticle function in a lacs1 lacs2 double mutant
RT of Arabidopsis.";
RL Planta 231:1089-1100(2010).
CC -!- FUNCTION: Activation of long-chain fatty acids for both synthesis of
CC cellular lipids, and degradation via beta-oxidation. Acts in the cutin
CC pathway. Preferentially uses palmitate, palmitoleate, oleate and
CC linoleate. Required for repression of lateral root formation through
CC its role in cutin biosynthesis and subsequent aerial tissues
CC permeability. {ECO:0000269|PubMed:14973169,
CC ECO:0000269|PubMed:15960613, ECO:0000269|PubMed:17396154,
CC ECO:0000269|PubMed:17434992, ECO:0000269|PubMed:18952782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:12177484};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20237894}.
CC -!- TISSUE SPECIFICITY: Expressed along the entire length of the stem, but
CC expression was not entirely epidermal specific, with some expression
CC found in internal cell layers as well. Was expressed in leave epidermal
CC cells, flowers (sepals, petals, stamens, filaments and carpel),
CC siliques and developing seeds. In roots, expression was detected in an
CC internal cell layer, probably the endodermal layer.
CC {ECO:0000269|PubMed:14973169, ECO:0000269|PubMed:19392700}.
CC -!- INDUCTION: Positively regulated by WIN1. {ECO:0000269|PubMed:17449808}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype with smaller, wrinkled leaves and
CC overall reduced vigor. Higher water loss rate and susceptibility to
CC drought stress. Defective in the cuticular membrane. Strong resistance
CC to virulent Botrytis cinerea and enhanced susceptibility to avirulent
CC Pseudomonas syringae. {ECO:0000269|PubMed:14973169,
CC ECO:0000269|PubMed:17396154, ECO:0000269|PubMed:17434992,
CC ECO:0000269|PubMed:20237894}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF503752; AAM28869.1; -; mRNA.
DR EMBL; AC007504; AAD43157.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32429.1; -; Genomic_DNA.
DR EMBL; AY065424; AAL38865.1; -; mRNA.
DR EMBL; AY094420; AAM19793.1; -; mRNA.
DR EMBL; BT001970; AAN71969.1; -; mRNA.
DR PIR; G96530; G96530.
DR RefSeq; NP_175368.2; NM_103833.5.
DR AlphaFoldDB; Q9XIA9; -.
DR SMR; Q9XIA9; -.
DR STRING; 3702.AT1G49430.1; -.
DR TCDB; 4.C.1.1.14; the fatty acid group translocation (fat) family.
DR PaxDb; Q9XIA9; -.
DR PRIDE; Q9XIA9; -.
DR ProteomicsDB; 237070; -.
DR EnsemblPlants; AT1G49430.1; AT1G49430.1; AT1G49430.
DR GeneID; 841367; -.
DR Gramene; AT1G49430.1; AT1G49430.1; AT1G49430.
DR KEGG; ath:AT1G49430; -.
DR Araport; AT1G49430; -.
DR TAIR; locus:2010177; AT1G49430.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; Q9XIA9; -.
DR OMA; DGLMEMP; -.
DR OrthoDB; 630541at2759; -.
DR PhylomeDB; Q9XIA9; -.
DR BioCyc; ARA:AT1G49430-MON; -.
DR BioCyc; MetaCyc:AT1G49430-MON; -.
DR SABIO-RK; Q9XIA9; -.
DR UniPathway; UPA00199; -.
DR PRO; PR:Q9XIA9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIA9; baseline and differential.
DR Genevisible; Q9XIA9; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:TAIR.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0010025; P:wax biosynthetic process; IBA:GO_Central.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045311; LC-FACS_euk.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endoplasmic reticulum; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome.
FT CHAIN 1..665
FT /note="Long chain acyl-CoA synthetase 2"
FT /id="PRO_0000401410"
FT REGION 496..520
FT /note="Fatty acid-binding"
FT /evidence="ECO:0000255"
FT BINDING 228..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 665 AA; 74389 MW; 9B1566F79A1B2D1A CRC64;
MSLAADNVLL VEEGRPATAE HPSAGPVYRC KYAKDGLLDL PTDIDSPWQF FSEAVKKYPN
EQMLGQRVTT DSKVGPYTWI TYKEAHDAAI RIGSAIRSRG VDPGHCCGIY GANCPEWIIA
MEACMSQGIT YVPLYDSLGV NAVEFIINHA EVSLVFVQEK TVSSILSCQK GCSSNLKTIV
SFGEVSSTQK EEAKNQCVSL FSWNEFSLMG NLDEANLPRK RKTDICTIMY TSGTTGEPKG
VILNNAAISV QVLSIDKMLE VTDRSCDTSD VFFSYLPLAH CYDQVMEIYF LSRGSSVGYW
RGDIRYLMDD VQALKPTVFC GVPRVYDKLY AGIMQKISAS GLIRKKLFDF AYNYKLGNMR
KGFSQEEASP RLDRLMFDKI KEALGGRAHM LLSGAAPLPR HVEEFLRIIP ASNLSQGYGL
TESCGGSFTT LAGVFSMVGT VGVPMPTVEA RLVSVPEMGY DAFSADVPRG EICLRGNSMF
SGYHKRQDLT DQVLIDGWFH TGDIGEWQED GSMKIIDRKK NIFKLSQGEY VAVENLENTY
SRCPLIAQIW VYGNSFESFL VGVVVPDRKA IEDWAKLNYQ SPNDFESLCQ NLKAQKYFLD
ELNSTAKQYQ LKGFEMLKAI HLEPNPFDIE RDLITPTFKL KRPQLLQHYK GIVDQLYSEA
KRSMA
