D6KL3_ARATH
ID D6KL3_ARATH Reviewed; 578 AA.
AC Q05999; Q67YR9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serine/threonine-protein kinase D6PKL3;
DE EC=2.7.11.1;
DE AltName: Full=D6 protein kinase-like 3;
DE AltName: Full=Serine/threonine-protein kinase AtPK7;
GN Name=D6PKL3; Synonyms=PK7; OrderedLocusNames=At3g27580; ORFNames=MMJ24.14;
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 [GENOMIC DNA].
RX PubMed=1446831; DOI=10.1016/0378-1119(92)90138-f;
RA Hayashida N., Mizoguchi T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Characterization of a gene that encodes a homologue of protein kinase in
RT Arabidopsis thaliana.";
RL Gene 121:325-330(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND REVIEW.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19168677; DOI=10.1242/dev.028365;
RA Zourelidou M., Muller I., Willige B.C., Nill C., Jikumaru Y., Li H.,
RA Schwechheimer C.;
RT "The polarly localized D6 PROTEIN KINASE is required for efficient auxin
RT transport in Arabidopsis thaliana.";
RL Development 136:627-636(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23709629; DOI=10.1105/tpc.113.111484;
RA Willige B.C., Ahlers S., Zourelidou M., Barbosa I.C., Demarsy E.,
RA Trevisan M., Davis P.A., Roelfsema M.R., Hangarter R., Fankhauser C.,
RA Schwechheimer C.;
RT "D6PK AGCVIII kinases are required for auxin transport and phototropic
RT hypocotyl bending in Arabidopsis.";
RL Plant Cell 25:1674-1688(2013).
CC -!- FUNCTION: Protein kinase that regulates the auxin transport activity of
CC PIN auxin efflux facilitators by direct phosphorylation. D6PK-mediated
CC PIN phosphorylation promotes auxin transport in the hypocotyl and this
CC is a prerequisite for PHOT1-dependent hypocotyl bending.
CC {ECO:0000269|PubMed:19168677, ECO:0000269|PubMed:23709629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- INTERACTION:
CC Q05999; Q17TI5: BRX; NbExp=4; IntAct=EBI-1103648, EBI-4426649;
CC Q05999; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103648, EBI-1103587;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Colocalizes with PIN1 to the basal (lower)
CC membrane of root cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in root tissue with lower
CC levels found in leaf, stem, seed and flower.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the quadruple d6pk, d6pkl1, d6pkl2 and d6pkl3 mutants
CC are deficient in lateral root formation and mildly agravitropic, have
CC fused or single cotyledons and narrow and twisted leaves, form few
CC axillary shoots, are almost infertile and impaired in phototropic
CC hypocotyl bending when exposed to lateral white light.
CC {ECO:0000269|PubMed:19168677, ECO:0000269|PubMed:23709629}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {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; D10910; BAA01716.1; -; Genomic_DNA.
DR EMBL; AB025626; BAB01288.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77339.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77340.1; -; Genomic_DNA.
DR EMBL; BT010571; AAQ65194.1; -; mRNA.
DR EMBL; AK175529; BAD43292.1; -; mRNA.
DR EMBL; AK176399; BAD44162.1; -; mRNA.
DR PIR; JC1385; JC1385.
DR RefSeq; NP_001030784.1; NM_001035707.3.
DR RefSeq; NP_189395.1; NM_113674.4.
DR AlphaFoldDB; Q05999; -.
DR SMR; Q05999; -.
DR BioGRID; 7710; 3.
DR IntAct; Q05999; 4.
DR STRING; 3702.AT3G27580.1; -.
DR PaxDb; Q05999; -.
DR PRIDE; Q05999; -.
DR ProteomicsDB; 222742; -.
DR EnsemblPlants; AT3G27580.1; AT3G27580.1; AT3G27580.
DR EnsemblPlants; AT3G27580.2; AT3G27580.2; AT3G27580.
DR GeneID; 822380; -.
DR Gramene; AT3G27580.1; AT3G27580.1; AT3G27580.
DR Gramene; AT3G27580.2; AT3G27580.2; AT3G27580.
DR KEGG; ath:AT3G27580; -.
DR Araport; AT3G27580; -.
DR TAIR; locus:2091443; AT3G27580.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q05999; -.
DR OMA; ECNTSLA; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q05999; -.
DR PRO; PR:Q05999; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q05999; baseline and differential.
DR Genevisible; Q05999; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010540; P:basipetal auxin transport; TAS:UniProtKB.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0062075; P:pollen aperture formation; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..578
FT /note="Serine/threonine-protein kinase D6PKL3"
FT /id="PRO_0000086166"
FT DOMAIN 182..516
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..426
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT MOTIF 575..578
FT /note="PIF"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 188..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 578 AA; 64286 MW; EC91B1463241578F CRC64;
MDSSSSVVYV GSSSKSRNFQ SKSKGSITSF SIDSRGTKKS MKTLLIPEPE PTSPEVIESS
VSSVSAESET PISIIRKKKQ SEPRFYSSPT NTFYTEAKQS FTNTEFSECA SISTIGIGGI
DLEKNGVMIY RGSIGSDVSD ESSSSGLSNA AYKPHRDNND KRWVAIQEVR SRVGSSLEAK
DFKLIKKLGG GDIGNVYLAE LIGTGVSFAV KVMEKAAIAA RKKLVRAQTE KEILQSLDHP
FLPTLYSHFE TEMNSCLVME FCPGGDLHSL RQKQRGKYFP EQAARFYVAE VLLAMEYLHM
LGIIYRDLKP ENVLVREDGH IMLSDFDLSL RCAVSPTLVR FAAITLESKS SSYCIQPTCV
DQSSCIVQPD CIQPVCFTPR FLSKGKHRKK SNDMSRQIRP LPELIAEPTS ARSMSFVGTH
EYLAPEIIKG EGHGSAVDWW TFGIFLYELL FGITPFRGGD NRATLFNVVG QPLRFPEHPN
VSFAARDLIR GLLVKEPQHR LAYRRGATEI KQHPFFQSVN WALIRCTSPP QIPQPVKPMD
QAHSVRHGFS QGHGHVGYDK PPTVDVKPSG NYLEIDFF
