DCR_ARATH
ID DCR_ARATH Reviewed; 484 AA.
AC Q9FF86;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=BAHD acyltransferase DCR;
DE EC=2.3.1.-;
DE AltName: Full=Protein DEFECTIVE IN CUTICULAR RIDGES;
DE AltName: Full=Protein PERMEABLE LEAVES 3;
GN Name=DCR; Synonyms=PEL3; OrderedLocusNames=At5g23940; ORFNames=MRO11.2;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14675439; DOI=10.1046/j.1365-313x.2003.01946.x;
RA Tanaka T., Tanaka H., Machida C., Watanabe M., Machida Y.;
RT "A new method for rapid visualization of defects in leaf cuticle reveals
RT five intrinsic patterns of surface defects in Arabidopsis.";
RL Plant J. 37:139-146(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19626137; DOI=10.1093/mp/ssp037;
RA Marks M.D., Wenger J.P., Gilding E., Jilk R., Dixon R.A.;
RT "Transcriptome analysis of Arabidopsis wild-type and gl3-sst sim trichomes
RT identifies four additional genes required for trichome development.";
RL Mol. Plant 2:803-822(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19828672; DOI=10.1104/pp.109.143388;
RA Panikashvili D., Shi J.X., Schreiber L., Aharoni A.;
RT "The Arabidopsis DCR encoding a soluble BAHD acyltransferase is required
RT for cutin polyester formation and seed hydration properties.";
RL Plant Physiol. 151:1773-1789(2009).
CC -!- FUNCTION: Required for incorporation of 9(10),16-dihydroxy-hexadecanoic
CC acid into cutin. {ECO:0000269|PubMed:19828672}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19626137,
CC ECO:0000269|PubMed:19828672}.
CC -!- TISSUE SPECIFICITY: Expressed in root caps and lateral root emerging
CC sites, in trichomes, in epidermis in stems, sepals and anther
CC filaments, and in pollen grains and torpedo stage seeds.
CC {ECO:0000269|PubMed:19828672}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all 3 inner integumenta layers and 2
CC outer integument layers in young seeds, but specifically restricted to
CC the inner integumenta in mature seeds. {ECO:0000269|PubMed:19828672}.
CC -!- DISRUPTION PHENOTYPE: Smaller rosettes, collapsed or tangled trichomes,
CC postgenital fusions between the rosette leaves and flower buds, fusions
CC between sepals, altered cuticle permeability, loss of cuticular folding
CC in petals, abnormal flower and silique development, altered seeds
CC surface, defective mucilage extrusion and semisterility. Increased
CC susceptibility to salinity, osmotic and water deprivation stresses.
CC {ECO:0000269|PubMed:14675439, ECO:0000269|PubMed:19626137,
CC ECO:0000269|PubMed:19828672}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AB005244; BAB10067.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93236.1; -; Genomic_DNA.
DR EMBL; AY128300; AAM91107.1; -; mRNA.
DR EMBL; BT000770; AAN31909.1; -; mRNA.
DR EMBL; BT001043; AAN46797.1; -; mRNA.
DR RefSeq; NP_197782.1; NM_122299.3.
DR AlphaFoldDB; Q9FF86; -.
DR SMR; Q9FF86; -.
DR BioGRID; 17734; 4.
DR IntAct; Q9FF86; 1.
DR STRING; 3702.AT5G23940.1; -.
DR PaxDb; Q9FF86; -.
DR PRIDE; Q9FF86; -.
DR ProteomicsDB; 222759; -.
DR DNASU; 832459; -.
DR EnsemblPlants; AT5G23940.1; AT5G23940.1; AT5G23940.
DR GeneID; 832459; -.
DR Gramene; AT5G23940.1; AT5G23940.1; AT5G23940.
DR KEGG; ath:AT5G23940; -.
DR Araport; AT5G23940; -.
DR TAIR; locus:2172813; AT5G23940.
DR eggNOG; ENOG502QUE6; Eukaryota.
DR HOGENOM; CLU_014546_3_0_1; -.
DR InParanoid; Q9FF86; -.
DR OMA; WGKPESV; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9FF86; -.
DR BioCyc; ARA:AT5G23940-MON; -.
DR PRO; PR:Q9FF86; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF86; baseline and differential.
DR Genevisible; Q9FF86; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0051179; P:localization; IDA:TAIR.
DR GO; GO:0090626; P:plant epidermis morphogenesis; IMP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="BAHD acyltransferase DCR"
FT /id="PRO_0000391068"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 53514 MW; 0C90079C2AD003C4 CRC64;
MKIKIMSKTH VKPTKPVLGK KQFHLTTFDL PYLAFYYNQK FLLYKFQNLL DLEEPTFQNE
VVENLKDGLG LVLEDFYQLA GKLAKDDEGV FRVEYDAEDS EINGVEFSVA HAADVTVDDL
TAEDGTAKFK ELVPYNGILN LEGLSRPLLA VQVTKLKDGL AMGLAFNHAV LDGTSTWHFM
SSWAEICRGA QSISTQPFLD RSKARDTRVK LDLTAPKDPN ETSNGEDAAN PTVEPPQLVE
KIFRFSDFAV HTIKSRANSV IPSDSSKPFS TFQSLTSHIW RHVTLARGLK PEDITIFTVF
ADCRRRVDPP MPEEYFGNLI QAIFTGTAAG LLAAHGPEFG ASVIQKAIAA HDASVIDARN
DEWEKSPKIF QFKDAGVNCV AVGSSPRFRV YEVDFGFGKP ETVRSGSNNR FNGMMYLYQG
KAGGISIDVE ITLEASVMEK LVKSKEFLLS EEEEEDDGKK LTNGNGHVNG NGNGYVNGNG
NGFV
