ID   LACS4_ARATH             Reviewed;         666 AA.
AC   Q9T0A0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Long chain acyl-CoA synthetase 4;
DE            EC=6.2.1.3;
GN   Name=LACS4; OrderedLocusNames=At4g23850; ORFNames=T32A16_20;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   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).
CC   -!- FUNCTION: Activation of long-chain fatty acids for both synthesis of
CC       cellular lipids, and degradation via beta-oxidation. Preferentially
CC       uses palmitate, palmitoleate, oleate and linoleate.
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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF503754; AAM28871.1; -; mRNA.
DR   EMBL; AL078468; CAB43885.1; -; Genomic_DNA.
DR   EMBL; AL161560; CAB81303.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84812.1; -; Genomic_DNA.
DR   EMBL; AY049239; AAK83581.1; -; mRNA.
DR   PIR; T08904; T08904.
DR   RefSeq; NP_194116.1; NM_118516.5.
DR   AlphaFoldDB; Q9T0A0; -.
DR   SMR; Q9T0A0; -.
DR   BioGRID; 13773; 4.
DR   STRING; 3702.AT4G23850.1; -.
DR   iPTMnet; Q9T0A0; -.
DR   PaxDb; Q9T0A0; -.
DR   PRIDE; Q9T0A0; -.
DR   ProteomicsDB; 238406; -.
DR   EnsemblPlants; AT4G23850.1; AT4G23850.1; AT4G23850.
DR   GeneID; 828484; -.
DR   Gramene; AT4G23850.1; AT4G23850.1; AT4G23850.
DR   KEGG; ath:AT4G23850; -.
DR   Araport; AT4G23850; -.
DR   TAIR; locus:2138141; AT4G23850.
DR   eggNOG; KOG1256; Eukaryota.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   InParanoid; Q9T0A0; -.
DR   OMA; YAYKHHN; -.
DR   OrthoDB; 630541at2759; -.
DR   PhylomeDB; Q9T0A0; -.
DR   BioCyc; ARA:AT4G23850-MON; -.
DR   BioCyc; MetaCyc:AT4G23850-MON; -.
DR   SABIO-RK; Q9T0A0; -.
DR   UniPathway; UPA00199; -.
DR   PRO; PR:Q9T0A0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T0A0; baseline and differential.
DR   Genevisible; Q9T0A0; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR   GO; GO:0080024; P:indolebutyric acid metabolic process; IDA:TAIR.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..666
FT                   /note="Long chain acyl-CoA synthetase 4"
FT                   /id="PRO_0000401412"
FT   REGION          495..519
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   666 AA;  74508 MW;  8E663756D60B0E57 CRC64;
     MSQQKKYIFQ VEEGKEGSDG RPSVGPVYRS IFAKDGFPDP IEGMDSCWDV FRMSVEKYPN
     NPMLGRREIV DGKPGKYVWQ TYQEVYDIVM KLGNSLRSVG VKDEAKCGIY GANSPEWIIS
     MEACNAHGLY CVPLYDTLGA DAVEFIISHS EVSIVFVEEK KISELFKTCP NSTEYMKTVV
     SFGGVSREQK EEAETFGLVI YAWDEFLKLG EGKQYDLPIK KKSDICTIMY TSGTTGDPKG
     VMISNESIVT LIAGVIRLLK SANEALTVKD VYLSYLPLAH IFDRVIEECF IQHGAAIGFW
     RGDVKLLIED LAELKPTIFC AVPRVLDRVY SGLQKKLSDG GFLKKFIFDS AFSYKFGYMK
     KGQSHVEASP LFDKLVFSKV KQGLGGNVRI ILSGAAPLAS HVESFLRVVA CCHVLQGYGL
     TESCAGTFVS LPDELGMLGT VGPPVPNVDI RLESVPEMEY DALASTARGE ICIRGKTLFS
     GYYKREDLTK EVLIDGWLHT GDVGEWQPDG SMKIIDRKKN IFKLSQGEYV AVENIENIYG
     EVQAVDSVWV YGNSFESFLI AIANPNQHIL ERWAAENGVS GDYDALCQNE KAKEFILGEL
     VKMAKEKKMK GFEIIKAIHL DPVPFDMERD LLTPTFKKKR PQLLKYYQSV IDEMYKTINA
     KFASRG