BRAT1_ARATH
ID BRAT1_ARATH Reviewed; 458 AA.
AC Q9SZ58; Q9SZ47;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Brassinosteroid-related acyltransferase 1 {ECO:0000303|PubMed:23020607};
DE Short=BR-related acyltransferase 1 {ECO:0000303|PubMed:23020607};
DE EC=2.3.1.- {ECO:0000269|PubMed:23071642, ECO:0000269|PubMed:23204503};
DE AltName: Full=Protein DWARF AND ROUND LEAF 1 {ECO:0000303|PubMed:23204503};
DE AltName: Full=Protein PIZZA {ECO:0000303|PubMed:23071642};
GN Name=BAT1 {ECO:0000303|PubMed:23020607};
GN Synonyms=DRL1 {ECO:0000303|PubMed:23204503},
GN PIZ {ECO:0000303|PubMed:23071642};
GN OrderedLocusNames=At4g31910 {ECO:0000312|Araport:AT4G31910};
GN ORFNames=F10N7.280 {ECO:0000312|EMBL:CAA16598.1},
GN F11C18.110 {ECO:0000312|EMBL:CAB40761.1};
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 [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 [2]
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 [3]
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 [4]
RP PATHWAY, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23071642; DOI=10.1371/journal.pone.0046805;
RA Schneider K., Breuer C., Kawamura A., Jikumaru Y., Hanada A., Fujioka S.,
RA Ichikawa T., Kondou Y., Matsui M., Kamiya Y., Yamaguchi S., Sugimoto K.;
RT "Arabidopsis PIZZA has the capacity to acylate brassinosteroids.";
RL PLoS ONE 7:E46805-E46805(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY 24-EPIBL
RP AND ABA, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=23204503; DOI=10.1093/mp/sss144;
RA Zhu W., Wang H., Fujioka S., Zhou T., Tian H., Tian W., Wang X.;
RT "Homeostasis of brassinosteroids regulated by DRL1, a putative
RT acyltransferase in Arabidopsis.";
RL Mol. Plant 6:546-558(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY AUXIN, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23020607; DOI=10.1111/tpj.12036;
RA Choi S., Cho Y.H., Kim K., Matsui M., Son S.-H., Kim S.-K., Fujioka S.,
RA Hwang I.;
RT "BAT1, a putative acyltransferase, modulates brassinosteroid levels in
RT Arabidopsis.";
RL Plant J. 73:380-391(2013).
CC -!- FUNCTION: Brassinosteroids (BR) acyltransferase with acyl-CoA ligase
CC activity toward brassinolide (BL), castasterone (CS), typhasterol (TY),
CC 6-deoxotyphasterol (6-deoxoTY), and 6-deoxocastasterone (6-deoxoCS) and
CC thus converts them to corresponding lauroyl esters (PubMed:23071642,
CC PubMed:23204503, PubMed:23020607). Regulates BR homeostasis and
CC promotes BR-mediated cell growth regulation (PubMed:23071642,
CC PubMed:23204503). Involved in vascular bundle development
CC (PubMed:23020607). {ECO:0000269|PubMed:23020607,
CC ECO:0000269|PubMed:23071642, ECO:0000269|PubMed:23204503}.
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:23071642, ECO:0000269|PubMed:23204503}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23020607}. Nucleus {ECO:0000269|PubMed:23020607}.
CC Note=Localizes in the endoplasmic reticulum in young tissues and the
CC phloem of vascular bundles. {ECO:0000269|PubMed:23020607}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young tissues and vascular
CC bundles (PubMed:23020607). Mostly expressed in young leaves, primary
CC roots, flowers (including petals and sepals), and siliques
CC (PubMed:23204503). {ECO:0000269|PubMed:23020607,
CC ECO:0000269|PubMed:23204503}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, mainly observed in the
CC vascular cylinder of cotyledons, leaves and hypocotyls. Accumulates
CC also in root tips, lateral root initiation sites and the maturation
CC zone of the primary root. In adult plants, present in the vasculature
CC of the inflorescence stems, especially in phloem cells.
CC {ECO:0000269|PubMed:23020607}.
CC -!- INDUCTION: Induced by 24-epi-brassinolide (24-epiBL, eBL) and inhibited
CC by abscisic acid (ABA) (PubMed:23204503). Stimulated by auxin
CC (PubMed:23020607). {ECO:0000269|PubMed:23020607,
CC ECO:0000269|PubMed:23204503}.
CC -!- DISRUPTION PHENOTYPE: No obvious growth phenotype under standard growth
CC conditions (PubMed:23071642, PubMed:23204503). The bat1-1 mutant
CC exhibits longer stems before flowering, but reaches normal height after
CC flowering, with larger inflorescence stems containing an increased
CC number of vascular bundles (PubMed:23020607).
CC {ECO:0000269|PubMed:23020607, ECO:0000269|PubMed:23071642,
CC ECO:0000269|PubMed:23204503}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021636; CAA16598.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049607; CAB40761.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79909.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85978.1; -; Genomic_DNA.
DR EMBL; AY052280; AAK96473.1; -; mRNA.
DR EMBL; AY139805; AAM98111.1; -; mRNA.
DR PIR; T06313; T06313.
DR RefSeq; NP_194919.1; NM_119342.3.
DR AlphaFoldDB; Q9SZ58; -.
DR SMR; Q9SZ58; -.
DR STRING; 3702.AT4G31910.1; -.
DR iPTMnet; Q9SZ58; -.
DR PaxDb; Q9SZ58; -.
DR PRIDE; Q9SZ58; -.
DR ProteomicsDB; 240411; -.
DR EnsemblPlants; AT4G31910.1; AT4G31910.1; AT4G31910.
DR GeneID; 829321; -.
DR Gramene; AT4G31910.1; AT4G31910.1; AT4G31910.
DR KEGG; ath:AT4G31910; -.
DR Araport; AT4G31910; -.
DR TAIR; locus:2116757; AT4G31910.
DR eggNOG; ENOG502QSIF; Eukaryota.
DR HOGENOM; CLU_014546_2_2_1; -.
DR InParanoid; Q9SZ58; -.
DR OMA; KLNVYPR; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9SZ58; -.
DR BioCyc; ARA:AT4G31910-MON; -.
DR UniPathway; UPA00381; -.
DR PRO; PR:Q9SZ58; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ58; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:CACAO.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:TAIR.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Acyltransferase; Brassinosteroid biosynthesis; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Nucleus; Reference proteome;
KW Steroid biosynthesis; Transferase.
FT CHAIN 1..458
FT /note="Brassinosteroid-related acyltransferase 1"
FT /id="PRO_0000436332"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 458 AA; 51145 MW; 62B75FCB1762DB30 CRC64;
MPMLMATRID IIQKLNVYPR FQNHDKKKLI TLSNLDRQCP LLMYSVFFYK NTTTRDFDSV
FSNLKLGLEE TMSVWYPAAG RLGLDGGGCK LNIRCNDGGA VMVEAVATGV KLSELGDLTQ
YNEFYENLVY KPSLDGDFSV MPLVVAQVTR FACGGYSIGI GTSHSLFDGI SAYEFIHAWA
SNSHIHNKSN SKITNKKEDV VIKPVHDRRN LLVNRDAVRE TNAAAICHLY QLIKQAMMTY
QEQNRNLELP DSGFVIKTFE LNGDAIESMK KKSLEGFMCS SFEFLAAHLW KARTRALGLR
RDAMVCLQFA VDIRKRTETP LPEGFSGNAY VLASVASTAR ELLEELTLES IVNKIREAKK
SIDQGYINSY MEALGGSNDG NLPPLKELTL ISDWTKMPFH NVGFGNGGEP ADYMAPLCPP
VPQVAYFMKN PKDAKGVLVR IGLDPRDVNG FSNHFLDC
