D14_ARATH
ID D14_ARATH Reviewed; 267 AA.
AC Q9SQR3; Q8L9M4;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Strigolactone esterase D14 {ECO:0000303|PubMed:25425668};
DE EC=3.1.-.- {ECO:0000269|PubMed:25425668};
DE AltName: Full=Protein DWARF 14 {ECO:0000303|PubMed:22357928};
DE Short=AtD14 {ECO:0000303|PubMed:22357928};
GN Name=D14 {ECO:0000303|PubMed:22357928};
GN OrderedLocusNames=At3g03990 {ECO:0000312|Araport:AT3G03990};
GN ORFNames=T11I18.10 {ECO:0000312|EMBL:AAF05858.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22357928; DOI=10.1242/dev.074567;
RA Waters M.T., Nelson D.C., Scaffidi A., Flematti G.R., Sun Y.K., Dixon K.W.,
RA Smith S.M.;
RT "Specialisation within the DWARF14 protein family confers distinct
RT responses to karrikins and strigolactones in Arabidopsis.";
RL Development 139:1285-1295(2012).
RN [6]
RP REVIEW.
RX PubMed=25179782; DOI=10.1016/j.pbi.2014.08.001;
RA Bennett T., Leyser O.;
RT "Strigolactone signalling: standing on the shoulders of DWARFs.";
RL Curr. Opin. Plant Biol. 22:7-13(2014).
RN [7]
RP FUNCTION, MUTAGENESIS OF PRO-169, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=24610723; DOI=10.1105/tpc.114.122903;
RA Chevalier F., Nieminen K., Sanchez-Ferrero J.C., Rodriguez M.L.,
RA Chagoyen M., Hardtke C.S., Cubas P.;
RT "Strigolactone promotes degradation of DWARF14, an alpha/beta hydrolase
RT essential for strigolactone signaling in Arabidopsis.";
RL Plant Cell 26:1134-1150(2014).
RN [8]
RP FUNCTION, MUTAGENESIS OF SER-97, AND ACTIVE SITES.
RX PubMed=25425668; DOI=10.1073/pnas.1410801111;
RA Abe S., Sado A., Tanaka K., Kisugi T., Asami K., Ota S., Kim H.I.,
RA Yoneyama K., Xie X., Ohnishi T., Seto Y., Yamaguchi S., Akiyama K.,
RA Yoneyama K., Nomura T.;
RT "Carlactone is converted to carlactonoic acid by MAX1 in Arabidopsis and
RT its methyl ester can directly interact with AtD14 in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:18084-18089(2014).
RN [9]
RP INTERACTION WITH SMXL6; SMXL7 AND SMXL8.
RX PubMed=26546446; DOI=10.1105/tpc.15.00605;
RA Wang L., Wang B., Jiang L., Liu X., Li X., Lu Z., Meng X., Wang Y.,
RA Smith S.M., Li J.;
RT "Strigolactone signaling in Arabidopsis regulates shoot development by
RT targeting D53-like SMXL repressor proteins for ubiquitination and
RT degradation.";
RL Plant Cell 27:3128-3142(2015).
RN [10]
RP INTERACTION WITH SMXL6; SMXL7 AND SMXL8.
RX PubMed=25713176; DOI=10.1093/pcp/pcv028;
RA Umehara M., Cao M., Akiyama K., Akatsu T., Seto Y., Hanada A., Li W.,
RA Takeda-Kamiya N., Morimoto Y., Yamaguchi S.;
RT "Structural requirements of strigolactones for shoot branching inhibition
RT in rice and Arabidopsis.";
RL Plant Cell Physiol. 56:1059-1072(2015).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH MAX2, AND MUTAGENESIS OF GLY-158.
RX PubMed=27479325; DOI=10.1038/nature19073;
RA Yao R., Ming Z., Yan L., Li S., Wang F., Ma S., Yu C., Yang M., Chen L.,
RA Chen L., Li Y., Yan C., Miao D., Sun Z., Yan J., Sun Y., Wang L., Chu J.,
RA Fan S., He W., Deng H., Nan F., Li J., Rao Z., Lou Z., Xie D.;
RT "DWARF14 is a non-canonical hormone receptor for strigolactone.";
RL Nature 536:469-473(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), FUNCTION, SUBSTRATE SPECIFICITY,
RP AND ACTIVE SITES.
RX PubMed=23381136; DOI=10.1038/cr.2013.19;
RA Zhao L.H., Zhou X.E., Wu Z.S., Yi W., Xu Y., Li S., Xu T.H., Liu Y.,
RA Chen R.Z., Kovach A., Kang Y., Hou L., He Y., Xie C., Song W., Zhong D.,
RA Xu Y., Wang Y., Li J., Zhang C., Melcher K., Xu H.E.;
RT "Crystal structures of two phytohormone signal-transducing alpha/beta
RT hydrolases: karrikin-signaling KAI2 and strigolactone-signaling DWARF14.";
RL Cell Res. 23:436-439(2013).
CC -!- FUNCTION: Involved in strigolactone signaling pathway
CC (PubMed:22357928). Does not move long distances acropetally in the
CC plant to regulate shoot branching and is rapidly degraded in the
CC presence of strigolactones (PubMed:24610723). Functions downstream of
CC strigolactone synthesis, as a component of hormone signaling and as an
CC enzyme that participates in the conversion of strigolactones to the
CC bioactive form (PubMed:22357928). Acts probably as a strigolactone
CC receptor (PubMed:24610723). Strigolactones are hormones that inhibit
CC tillering and shoot branching through the MAX-dependent pathway,
CC contribute to the regulation of shoot architectural response to
CC phosphate-limiting conditions and function as rhizosphere signal that
CC stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger
CC seed germination of root parasitic weeds (PubMed:22357928). Hydrolyzes
CC methyl carlactonoate (MeCLA), but not carlactone (CL) or carlactonoic
CC acid (CLA) (PubMed:25425668). Hydrolyzes the butenolide ring of
CC strigolactones (PubMed:23381136). The initial nucleophilic attack
CC causes an electron shift, followed by the addition of a water molecule,
CC to lead to the release of the ABC ring product and the formation of a
CC 'Ser-97'-stabilized open lactone intermediate (PubMed:23381136). Has no
CC esterase activity for 4-nitrophenyl butyrate (PubMed:23381136). Binds
CC and hydrolyzes the synthetic strigolactone analog GR24 in vitro. Forms
CC a stable covalent complex with the D-ring of strigolactone, which is
CC essential for hormone bioactivity. The D-ring is attached to His-247 of
CC the catalytic triad. The hydrolysis of strigolactone into a covalently
CC linked intermediate molecule initiates a conformational change of D14
CC to facilitate interaction with MAX2 and formation of the D14-MAX2-
CC SKP1/ASK1 complex to trigger strigolactone signaling. This mechanism
CC defines D14 as a non-canonical hormone receptor with dual functions to
CC generate and sense the active form of strigolactone (PubMed:27479325).
CC {ECO:0000269|PubMed:22357928, ECO:0000269|PubMed:23381136,
CC ECO:0000269|PubMed:24610723, ECO:0000269|PubMed:25425668,
CC ECO:0000269|PubMed:27479325}.
CC -!- SUBUNIT: Interacts with SMXL6, SMXL7 and SMXL8 (PubMed:26546446,
CC PubMed:25713176). The interaction with SMXLs occurs in the presence of
CC (2'R) stereoisomers of strigolactones, but not (2'S) stereoisomers
CC (PubMed:25713176). Interacts with MAX2. Forms a complex with MAX2 and
CC SKP1A/ASK1 in presence of strigolactone (PubMed:27479325).
CC {ECO:0000269|PubMed:25713176, ECO:0000269|PubMed:26546446,
CC ECO:0000269|PubMed:27479325}.
CC -!- INTERACTION:
CC Q9SQR3; Q9SZN7: HIPP26; NbExp=3; IntAct=EBI-25530219, EBI-2008207;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24610723}. Nucleus
CC {ECO:0000269|PubMed:24610723}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in rosette and cauline
CC leaves and at lower levels in axillary buds, inflorescences, stems,
CC roots and developing vascular tissue of cotyledons.
CC {ECO:0000269|PubMed:24610723}.
CC -!- INDUCTION: Not regulated by strigolactone, auxin signaling or bud
CC growth status. {ECO:0000269|PubMed:24610723}.
CC -!- DISRUPTION PHENOTYPE: Increased shoot branching.
CC {ECO:0000269|PubMed:22357928}.
CC -!- MISCELLANEOUS: The initial nucleophilic attack of strigolactones by D14
CC causes an electron shift, followed by the addition of a water molecule,
CC to lead to the release of the ABC ring product and the formation of a
CC S97-stabilized open lactone intermediate.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {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; AC011698; AAF05858.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74023.1; -; Genomic_DNA.
DR EMBL; AY064145; AAL36052.1; -; mRNA.
DR EMBL; AY097402; AAM19918.1; -; mRNA.
DR EMBL; AY088353; AAM65892.1; -; mRNA.
DR RefSeq; NP_566220.1; NM_111270.3.
DR PDB; 4IH4; X-ray; 3.50 A; A/B/C/D=1-267.
DR PDB; 5HZG; X-ray; 3.30 A; A/E=1-267.
DR PDBsum; 4IH4; -.
DR PDBsum; 5HZG; -.
DR AlphaFoldDB; Q9SQR3; -.
DR SMR; Q9SQR3; -.
DR BioGRID; 4889; 2.
DR IntAct; Q9SQR3; 1.
DR STRING; 3702.AT3G03990.1; -.
DR ESTHER; arath-AtD14; RsbQ-like.
DR MEROPS; S33.A18; -.
DR PaxDb; Q9SQR3; -.
DR PRIDE; Q9SQR3; -.
DR ProteomicsDB; 222743; -.
DR EnsemblPlants; AT3G03990.1; AT3G03990.1; AT3G03990.
DR GeneID; 819554; -.
DR Gramene; AT3G03990.1; AT3G03990.1; AT3G03990.
DR KEGG; ath:AT3G03990; -.
DR Araport; AT3G03990; -.
DR TAIR; locus:2095913; AT3G03990.
DR eggNOG; ENOG502QVRR; Eukaryota.
DR HOGENOM; CLU_020336_30_0_1; -.
DR InParanoid; Q9SQR3; -.
DR OMA; DQSVWQR; -.
DR OrthoDB; 1061420at2759; -.
DR PhylomeDB; Q9SQR3; -.
DR PRO; PR:Q9SQR3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQR3; baseline and differential.
DR Genevisible; Q9SQR3; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1902348; P:cellular response to strigolactone; IEP:TAIR.
DR GO; GO:0010223; P:secondary shoot formation; IMP:UniProtKB.
DR GO; GO:1901601; P:strigolactone biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR031143; D14_fam.
DR PANTHER; PTHR43039:SF4; PTHR43039:SF4; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..267
FT /note="Strigolactone esterase D14"
FT /id="PRO_0000422053"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23381136,
FT ECO:0000269|PubMed:25425668"
FT ACT_SITE 218
FT /evidence="ECO:0000305|PubMed:23381136"
FT ACT_SITE 247
FT /evidence="ECO:0000305|PubMed:23381136"
FT MUTAGEN 97
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25425668"
FT MUTAGEN 158
FT /note="G->E: Loss of interaction with MAX2."
FT /evidence="ECO:0000269|PubMed:27479325"
FT MUTAGEN 169
FT /note="P->L: In d14-seto; loss of activity."
FT /evidence="ECO:0000269|PubMed:24610723"
FT CONFLICT 236
FT /note="D -> E (in Ref. 4; AAM65892)"
FT /evidence="ECO:0000305"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4IH4"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:5HZG"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5HZG"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4IH4"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4IH4"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:5HZG"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4IH4"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5HZG"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:5HZG"
SQ SEQUENCE 267 AA; 29625 MW; 47E326EEE2AE5204 CRC64;
MSQHNILEAL NVRVVGTGDR ILFLAHGFGT DQSAWHLILP YFTQNYRVVL YDLVCAGSVN
PDYFDFNRYT TLDPYVDDLL NIVDSLGIQN CAYVGHSVSA MIGIIASIRR PELFSKLILI
GFSPRFLNDE DYHGGFEEGE IEKVFSAMEA NYEAWVHGFA PLAVGADVPA AVREFSRTLF
NMRPDISLFV SRTVFNSDLR GVLGLVRVPT CVIQTAKDVS VPASVAEYLR SHLGGDTTVE
TLKTEGHLPQ LSAPAQLAQF LRRALPR
