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 24-JAN-2024, entry version 122. 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 DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=32399509; DOI=10.1002/pld3.219; RA Yoneyama K., Akiyama K., Brewer P.B., Mori N., Kawano-Kawada M., Haruta S., RA Nishiwaki H., Yamauchi S., Xie X., Umehara M., Beveridge C.A., Yoneyama K., RA Nomura T.; RT "Hydroxyl carlactone derivatives are predominant strigolactones in RT Arabidopsis."; RL Plant Direct 4:e00219-e00219(2020). RN [13] 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 (PubMed:22357928, CC PubMed:32399509). Accumulation of carlactone (CL), carlactonoate (CLA), CC methyl carlactonoate (MeCLA) and of their derivatives, including 3- CC hydroxycarlactone (3-HO-CL), 4-hydroxycarlactone (4-HO-CL) and 16- CC hydroxycarlactone (16-HO-CL) (PubMed:32399509). Corresponding CC hydroxycarlactonoates are also observed, such as 3-hydroxycarlactonoate CC (3-HO-CLA), 4-hydroxycarlactonoate (4-HO-CLA) and 16- CC hydroxycarlactonoate (16-HO-CLA), as well as methylated derivatives CC (11R)-hydroxymethyl carlactonoate (1'-HO-MeCLA), 4-hydroxymethyl CC carlactonoate (4-HO-MeCLA) and 16-hydroxymethyl carlactonoate (16-HO- CC MeCLA) (PubMed:32399509). {ECO:0000269|PubMed:22357928, CC ECO:0000269|PubMed:32399509}. 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.Q9SQR3; -. DR ESTHER; arath-AtD14; RsbQ-like. DR MEROPS; S33.A18; -. DR PaxDb; 3702-AT3G03990-1; -. 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; AT3G03990; D14. DR eggNOG; ENOG502QVRR; Eukaryota. DR HOGENOM; CLU_020336_30_0_1; -. DR InParanoid; Q9SQR3; -. DR OMA; DQSVWQR; -. DR OrthoDB; 455849at2759; -. DR PhylomeDB; Q9SQR3; -. DR PRO; PR:Q9SQR3; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SQR3; baseline and differential. 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; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR43039; ESTERASE-RELATED; 1. DR PANTHER; PTHR43039:SF4; STRIGOLACTONE ESTERASE D14; 1. DR Pfam; PF12697; Abhydrolase_6; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR Genevisible; Q9SQR3; AT. 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 //