KAI2_ARATH
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 25-MAY-2022, entry version 130.
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; A0A178W7C6: At1g72800; NbExp=3; IntAct=EBI-25519488, EBI-25530192;
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; 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}.
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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.AT4G37470.1; -.
DR ESTHER; arath-KAI2.D14L; RsbQ-like.
DR MEROPS; S33.A29; -.
DR PaxDb; Q9SZU7; -.
DR PRIDE; Q9SZU7; -.
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; locus:2126357; AT4G37470.
DR eggNOG; ENOG502QQIJ; Eukaryota.
DR HOGENOM; CLU_020336_30_0_1; -.
DR InParanoid; Q9SZU7; -.
DR OMA; VCPSPCF; -.
DR OrthoDB; 1061420at2759; -.
DR PhylomeDB; Q9SZU7; -.
DR PRO; PR:Q9SZU7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZU7; baseline and differential.
DR Genevisible; Q9SZU7; AT.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_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..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
