ID   LACS1_ARATH             Reviewed;         660 AA.
AC   O22898; Q56WP3; Q56ZG8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Long chain acyl-CoA synthetase 1;
DE            EC=6.2.1.3;
DE   AltName: Full=Protein ECERIFERUM 8;
GN   Name=LACS1; Synonyms=CER8; OrderedLocusNames=At2g47240;
GN   ORFNames=T8I13.8;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-660.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION.
RX   PubMed=12228482; DOI=10.1104/pp.108.1.369;
RA   Jenks M.A., Tuttle H.A., Eigenbrode S.D., Feldmann K.A.;
RT   "Leaf epicuticular waxes of the eceriferum mutants in Arabidopsis.";
RL   Plant Physiol. 108:369-377(1995).
RN   [8]
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   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND 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   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
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 both the
CC       wax and cutin pathways. Preferentially uses palmitate, palmitoleate,
CC       linoleate and eicosenoate. Seems to have a specific activity against
CC       very long-chain fatty acid (VLCFA) class with acids longer than 24
CC       carbons (C(24)). {ECO:0000269|PubMed:12228482,
CC       ECO:0000269|PubMed:19392700, ECO:0000269|PubMed:20237894}.
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: Epidermal-specific expression along the entire
CC       stem. In cauline leaves, was expressed over the entire leaf surface,
CC       most strongly in trichomes and guard cells, but not in mesophyll cells.
CC       In flowers, the expression was detected in the stigma and filaments of
CC       the stamens, and in the carpel was expressed specifically in ovaries.
CC       In roots, was expressed in primary and lateral roots, but not in the
CC       root tips. {ECO:0000269|PubMed:19392700, ECO:0000269|PubMed:20237894}.
CC   -!- DISRUPTION PHENOTYPE: In stem, fewer and flatter wax crystals and
CC       disorganized cuticle proper and thinner cuticular layer. Reduced amount
CC       of wax in all chemical classes on the stem and leaf, except in the very
CC       long-chain fatty acid (VLCFA) class with acids longer than 24 carbons
CC       (C(24)). {ECO:0000269|PubMed:19392700, ECO:0000269|PubMed:20237894}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF503751; AAM28868.1; -; mRNA.
DR   EMBL; AC002337; AAB63824.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10818.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10819.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM63045.1; -; Genomic_DNA.
DR   EMBL; AY056380; AAL08236.1; -; mRNA.
DR   EMBL; AY133648; AAM91478.1; -; mRNA.
DR   EMBL; AK317315; BAH19991.1; -; mRNA.
DR   EMBL; AK220997; BAD94634.1; -; mRNA.
DR   EMBL; AK221992; BAD94568.1; -; mRNA.
DR   PIR; G84912; G84912.
DR   RefSeq; NP_001031554.1; NM_001036477.1.
DR   RefSeq; NP_001318440.1; NM_001337254.1.
DR   RefSeq; NP_182246.1; NM_130292.4.
DR   AlphaFoldDB; O22898; -.
DR   SMR; O22898; -.
DR   STRING; 3702.O22898; -.
DR   iPTMnet; O22898; -.
DR   PaxDb; 3702-AT2G47240-1; -.
DR   ProteomicsDB; 250728; -.
DR   EnsemblPlants; AT2G47240.1; AT2G47240.1; AT2G47240.
DR   EnsemblPlants; AT2G47240.2; AT2G47240.2; AT2G47240.
DR   EnsemblPlants; AT2G47240.3; AT2G47240.3; AT2G47240.
DR   GeneID; 819337; -.
DR   Gramene; AT2G47240.1; AT2G47240.1; AT2G47240.
DR   Gramene; AT2G47240.2; AT2G47240.2; AT2G47240.
DR   Gramene; AT2G47240.3; AT2G47240.3; AT2G47240.
DR   KEGG; ath:AT2G47240; -.
DR   Araport; AT2G47240; -.
DR   TAIR; AT2G47240; LACS1.
DR   eggNOG; KOG1256; Eukaryota.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   InParanoid; O22898; -.
DR   OMA; DHSFAHT; -.
DR   OrthoDB; 22305at2759; -.
DR   PhylomeDB; O22898; -.
DR   BioCyc; ARA:AT2G47240-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G47240-MONOMER; -.
DR   UniPathway; UPA00199; -.
DR   PRO; PR:O22898; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22898; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR   GO; GO:0010025; P:wax biosynthetic process; IMP:TAIR.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   PANTHER; PTHR43272:SF6; LONG CHAIN ACYL-COA SYNTHETASE 1; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; O22898; AT.
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..660
FT                   /note="Long chain acyl-CoA synthetase 1"
FT                   /id="PRO_0000401409"
FT   REGION          492..516
FT                   /note="Fatty acid-binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         225..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        434
FT                   /note="M -> L (in Ref. 6; BAD94568)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   660 AA;  74598 MW;  7CB31F95107E20D3 CRC64;
     MKSFAAKVEE GVKGIDGKPS VGPVYRNLLS EKGFPPIDSE ITTAWDIFSK SVEKFPDNNM
     LGWRRIVDEK VGPYMWKTYK EVYEEVLQIG SALRAAGAEP GSRVGIYGVN CPQWIIAMEA
     CAAHTLICVP LYDTLGSGAV DYIVEHAEID FVFVQDTKIK GLLEPDCKCA KRLKAIVSFT
     NVSDELSHKA SEIGVKTYSW IDFLHMGREK PEDTNPPKAF NICTIMYTSG TSGDPKGVVL
     THQAVATFVV GMDLYMDQFE DKMTHDDVYL SFLPLAHILD RMNEEYFFRK GASVGYYHGN
     LNVLRDDIQE LKPTYLAGVP RVFERIHEGI QKALQELNPR RRFIFNALYK HKLAWLNRGY
     SHSKASPMAD FIAFRKIRDK LGGRIRLLVS GGAPLSPEIE EFLRVTCCCF VVQGYGLTET
     LGGTALGFPD EMCMLGTVGI PAVYNEIRLE EVSEMGYDPL GENPAGEICI RGQCMFSGYY
     KNPELTEEVM KDGWFHTGDI GEILPNGVLK IIDRKKNLIK LSQGEYVALE HLENIFGQNS
     VVQDIWVYGD SFKSMLVAVV VPNPETVNRW AKDLGFTKPF EELCSFPELK EHIISELKST
     AEKNKLRKFE YIKAVTVETK PFDVERDLVT ATLKNRRNNL LKYYQVQIDE MYRKLASKKI
//