ID KAI2_ARATH Reviewed; 270 AA. AC Q9SZU7; DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Probable esterase KAI2; DE AltName: Full=Protein DWARF-14-like; DE Short=Protein D14-like; DE AltName: Full=Protein HYPOSENSITIVE TO LIGHT; DE AltName: Full=Protein KARRIKIN INSENSITIVE 2; GN Name=KAI2; Synonyms=D14L, HTL; OrderedLocusNames=At4g37470; GN ORFNames=F6G17.120; 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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RC STRAIN=cv. Landsberg erecta; RX PubMed=20864454; DOI=10.1093/mp/ssq055; RA Sun X.D., Ni M.; RT "HYPOSENSITIVE TO LIGHT, an alpha/beta fold protein, acts downstream of RT ELONGATED HYPOCOTYL 5 to regulate seedling de-etiolation."; RL Mol. Plant 4:116-126(2011). RN [5] RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-133. RC STRAIN=cv. Landsberg erecta; 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 FUNCTION, AND INDUCTION BY LIGHT. RC STRAIN=cv. Landsberg erecta; RX PubMed=23142794; DOI=10.1093/mp/sss127; RA Waters M.T., Smith S.M.; RT "KAI2- and MAX2-mediated responses to karrikins and strigolactones are RT largely independent of HY5 in Arabidopsis seedlings."; RL Mol. Plant 6:63-75(2013). RN [7] 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF RP GLY-133. RX PubMed=23301669; DOI=10.1111/gtc.12025; RA Kagiyama M., Hirano Y., Mori T., Kim S.Y., Kyozuka J., Seto Y., RA Yamaguchi S., Hakoshima T.; RT "Structures of D14 and D14L in the strigolactone and karrikin signaling RT pathways."; RL Genes Cells 18:147-160(2013). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS). 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). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RX PubMed=23349965; DOI=10.1371/journal.pone.0054758; RA Bythell-Douglas R., Waters M.T., Scaffidi A., Flematti G.R., Smith S.M., RA Bond C.S.; RT "The structure of the karrikin-insensitive protein (KAI2) in Arabidopsis RT thaliana."; RL PLoS ONE 8:E54758-E54758(2013). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) ALONE AND IN COMPLEX WITH KARRIKIN, RP FUNCTION, AND MUTAGENESIS OF PHE-134; PHE-194 AND HIS-246. RX PubMed=23613584; DOI=10.1073/pnas.1306265110; RA Guo Y., Zheng Z., La Clair J.J., Chory J., Noel J.P.; RT "Smoke-derived karrikin perception by the alpha/beta-hydrolase KAI2 from RT Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 110:8284-8289(2013). CC -!- FUNCTION: Involved in seed germination and seedling development. CC Essential for plant responses to karrikins, a class of butenolide CC compounds, structurally similar to strigolactones, released from CC burning vegetation that stimulate seed germination and enhance seedling CC photomorphogenesis. KAI2 is not required for strigolactone-mediated CC responses, but MAX2 is necessary for responses to karrikins and CC strigolactones (PubMed:20864454, PubMed:22357928, PubMed:23142794, CC PubMed:23301669). Lacks detectable hydrolase activity against karrikin CC (PubMed:23613584). Karrikin binding induces a conformational change CC (PubMed:23613584). {ECO:0000269|PubMed:20864454, CC ECO:0000269|PubMed:22357928, ECO:0000269|PubMed:23142794, CC ECO:0000269|PubMed:23301669, ECO:0000269|PubMed:23613584}. CC -!- INTERACTION: CC Q9SZU7; Q9LNT9: ASK4; NbExp=3; IntAct=EBI-25519488, EBI-604085; CC Q9SZU7; Q9M995: At1g48930; NbExp=3; IntAct=EBI-25519488, EBI-25530015; CC Q9SZU7; O22842: At2g43610; NbExp=3; IntAct=EBI-25519488, EBI-25530116; CC Q9SZU7; Q8GY60: At4g03415; NbExp=3; IntAct=EBI-25519488, EBI-25529942; CC Q9SZU7; O82754: At4g23050; NbExp=3; IntAct=EBI-25519488, EBI-1238561; CC Q9SZU7; A0A178UN96: At5g09480; NbExp=3; IntAct=EBI-25519488, EBI-25530052; CC Q9SZU7; Q94AW8: ATJ3; NbExp=3; IntAct=EBI-25519488, EBI-1999282; CC Q9SZU7; A0A178W7C6: AXX17_At1g66980; NbExp=3; IntAct=EBI-25519488, EBI-25530192; CC Q9SZU7; A0A178V0W2: AXX17_At4g30790; NbExp=3; IntAct=EBI-25519488, EBI-25529973; CC Q9SZU7; Q8GXL7: GATA24; NbExp=3; IntAct=EBI-25519488, EBI-4426127; CC Q9SZU7; Q9SZN7: HIPP26; NbExp=3; IntAct=EBI-25519488, EBI-2008207; CC Q9SZU7; O80480: IMPA4; NbExp=3; IntAct=EBI-25519488, EBI-2131464; CC Q9SZU7; Q38997: KIN10; NbExp=3; IntAct=EBI-25519488, EBI-2107143; CC Q9SZU7; F4JH01: MEE44; NbExp=3; IntAct=EBI-25519488, EBI-25530149; CC Q9SZU7; Q38950: PP2AA2; NbExp=3; IntAct=EBI-25519488, EBI-4467372; CC Q9SZU7; Q9STT1: PUB39; NbExp=3; IntAct=EBI-25519488, EBI-25530170; CC Q9SZU7; Q39255: SKP1A; NbExp=3; IntAct=EBI-25519488, EBI-532357; CC Q9SZU7; Q9FHW7: SKP1B; NbExp=3; IntAct=EBI-25519488, EBI-604076; CC Q9SZU7; Q93Z00: TCP14; NbExp=3; IntAct=EBI-25519488, EBI-4424563; CC Q9SZU7; O64647: TCP9; NbExp=3; IntAct=EBI-25519488, EBI-9838721; CC Q9SZU7; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25519488, EBI-4426557; CC Q9SZU7; Q9SP35: TIM17-2; NbExp=5; IntAct=EBI-25519488, EBI-25529919; CC Q9SZU7; A0ME53; NbExp=3; IntAct=EBI-25519488, EBI-25530104; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20864454}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:20864454}. Note=Weak expression in the CC cytosol. CC -!- TISSUE SPECIFICITY: In young seedlings, expressed in hypocotyls and CC roots. In adult plants, expressed in rosette leaves, stigma, sepals and CC silique peduncles and tips. {ECO:0000269|PubMed:20864454}. CC -!- INDUCTION: By red light. {ECO:0000269|PubMed:23142794}. CC -!- DISRUPTION PHENOTYPE: Increased seed dormancy. Long hypocotyl phenotype CC under red, far-red, and blue light. {ECO:0000269|PubMed:20864454, CC ECO:0000269|PubMed:22357928}. 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; AL035601; CAB38214.1; -; Genomic_DNA. DR EMBL; AL161591; CAB80412.1; -; Genomic_DNA. DR EMBL; CP002687; AEE86798.1; -; Genomic_DNA. DR EMBL; AY056190; AAL07039.1; -; mRNA. DR EMBL; AY091347; AAM14286.1; -; mRNA. DR PIR; T04741; T04741. DR RefSeq; NP_195463.1; NM_119911.4. DR PDB; 3W06; X-ray; 1.15 A; A=1-270. DR PDB; 4HRX; X-ray; 2.11 A; A=1-270. DR PDB; 4HRY; X-ray; 1.50 A; A=1-270. DR PDB; 4HTA; X-ray; 1.90 A; A=1-270. DR PDB; 4IH1; X-ray; 1.55 A; A=1-270. DR PDB; 4JYM; X-ray; 1.35 A; A/B=1-270. DR PDB; 4JYP; X-ray; 1.30 A; A/B=1-270. DR PDB; 5Z9G; X-ray; 1.49 A; A=1-270. DR PDB; 5Z9H; X-ray; 1.49 A; A=1-270. DR PDBsum; 3W06; -. DR PDBsum; 4HRX; -. DR PDBsum; 4HRY; -. DR PDBsum; 4HTA; -. DR PDBsum; 4IH1; -. DR PDBsum; 4JYM; -. DR PDBsum; 4JYP; -. DR PDBsum; 5Z9G; -. DR PDBsum; 5Z9H; -. DR AlphaFoldDB; Q9SZU7; -. DR SMR; Q9SZU7; -. DR BioGRID; 15183; 24. DR IntAct; Q9SZU7; 23. DR STRING; 3702.Q9SZU7; -. DR ESTHER; arath-KAI2.D14L; RsbQ-like. DR MEROPS; S33.A29; -. DR PaxDb; 3702-AT4G37470-1; -. DR ProteomicsDB; 232272; -. DR EnsemblPlants; AT4G37470.1; AT4G37470.1; AT4G37470. DR GeneID; 829902; -. DR Gramene; AT4G37470.1; AT4G37470.1; AT4G37470. DR KEGG; ath:AT4G37470; -. DR Araport; AT4G37470; -. DR TAIR; AT4G37470; KAI2. DR eggNOG; ENOG502QQIJ; Eukaryota. DR HOGENOM; CLU_020336_30_0_1; -. DR InParanoid; Q9SZU7; -. DR OMA; FGCDQSM; -. DR OrthoDB; 455849at2759; -. DR PhylomeDB; Q9SZU7; -. DR PRO; PR:Q9SZU7; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9SZU7; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0009704; P:de-etiolation; IMP:TAIR. DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR. DR GO; GO:0080167; P:response to karrikin; IMP:TAIR. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR43039:SF3; ESTERASE KAI2-RELATED; 1. DR PANTHER; PTHR43039; ESTERASE-RELATED; 1. DR Pfam; PF12697; Abhydrolase_6; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR Genevisible; Q9SZU7; AT. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Reference proteome. FT CHAIN 1..270 FT /note="Probable esterase KAI2" FT /id="PRO_0000422056" FT ACT_SITE 95 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:23349965, FT ECO:0000305|PubMed:23381136" FT ACT_SITE 217 FT /evidence="ECO:0000305|PubMed:23349965, FT ECO:0000305|PubMed:23381136" FT ACT_SITE 246 FT /evidence="ECO:0000305|PubMed:23349965, FT ECO:0000305|PubMed:23381136" FT MUTAGEN 133 FT /note="G->E: In kai2-1; loss of function." FT /evidence="ECO:0000269|PubMed:22357928, FT ECO:0000269|PubMed:23301669" FT MUTAGEN 134 FT /note="F->A: Fivefold decreased affinity for karrikin." FT /evidence="ECO:0000269|PubMed:23613584" FT MUTAGEN 194 FT /note="F->A: Fivefold decreased affinity for karrikin." FT /evidence="ECO:0000269|PubMed:23613584" FT MUTAGEN 246 FT /note="H->A: Threefold decreased affinity for karrikin." FT /evidence="ECO:0000269|PubMed:23613584" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 19..23 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:3W06" FT TURN 34..36 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:3W06" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 44..48 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 70..83 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 96..107 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 136..148 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 150..162 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 169..180 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 222..231 FT /evidence="ECO:0007829|PDB:3W06" FT STRAND 236..247 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:3W06" FT HELIX 253..265 FT /evidence="ECO:0007829|PDB:3W06" SQ SEQUENCE 270 AA; 29791 MW; DE49CA592174FFBE CRC64; MGVVEEAHNV KVIGSGEATI VLGHGFGTDQ SVWKHLVPHL VDDYRVVLYD NMGAGTTNPD YFDFDRYSNL EGYSFDLIAI LEDLKIESCI FVGHSVSAMI GVLASLNRPD LFSKIVMISA SPRYVNDVDY QGGFEQEDLN QLFEAIRSNY KAWCLGFAPL AVGGDMDSIA VQEFSRTLFN MRPDIALSVG QTIFQSDMRQ ILPFVTVPCH ILQSVKDLAV PVVVSEYLHA NLGCESVVEV IPSDGHLPQL SSPDSVIPVI LRHIRNDIAM //