D6PK_ARATH
ID D6PK_ARATH Reviewed; 498 AA.
AC Q9FG74; Q39031;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine/threonine-protein kinase D6PK {ECO:0000303|PubMed:19168677, ECO:0000303|PubMed:23709629};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19168677};
DE AltName: Full=D6 protein kinase {ECO:0000303|PubMed:19168677, ECO:0000303|PubMed:23709629};
DE AltName: Full=Serine/threonine-protein kinase 64 {ECO:0000303|PubMed:1558955};
DE Short=AtPK64 {ECO:0000303|PubMed:1558955};
DE AltName: Full=Serine/threonine-protein kinase AGC1-1 {ECO:0000303|PubMed:14749726};
GN Name=D6PK {ECO:0000303|PubMed:19168677, ECO:0000303|PubMed:23709629};
GN Synonyms=PK64 {ECO:0000303|PubMed:1558955};
GN OrderedLocusNames=At5g55910 {ECO:0000312|Araport:AT5G55910};
GN ORFNames=MYN21.2 {ECO:0000312|EMBL:BAB08656.1};
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 [MRNA].
RX PubMed=1558955; DOI=10.1007/bf00020025;
RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Harada H.,
RA Shinozaki K.;
RT "Nucleotide sequence of a cDNA encoding a protein kinase homologue in
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 18:809-812(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH PDPK1.
RX PubMed=14749726; DOI=10.1038/sj.emboj.7600068;
RA Anthony R.G., Henriques R., Helfer A., Meszaros T., Rios G., Testerink C.,
RA Munnik T., Deak M., Koncz C., Boegre L.;
RT "A protein kinase target of a PDK1 signalling pathway is involved in root
RT hair growth in Arabidopsis.";
RL EMBO J. 23:572-581(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
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. Phosphorylates
CC PIN1, PIN2, PIN3, PIN4 and PIN7 in vitro and PIN1 in vivo. Acts as a
CC lipid domain-dependent mediator of root epidermal planar polarity via
CC the binding to phosphatidylinositol phosphates (e.g. PtdIns(3)P,
CC PtdIns(4)P, PtdIns(5)P, PtdIns(3,5)P(2), PtdIns(4,5)P(2),
CC PtdIns(3,4,5)P(3) and phosphatidic acid) (PubMed:27251533).
CC {ECO:0000269|PubMed:19168677, ECO:0000269|PubMed:23709629,
CC ECO:0000269|PubMed:27251533}.
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 Evidence={ECO:0000269|PubMed:19168677};
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; Evidence={ECO:0000269|PubMed:19168677};
CC -!- SUBUNIT: Interacts (via C-terminal PIF domain) with PDPK1.
CC {ECO:0000269|PubMed:14749726}.
CC -!- INTERACTION:
CC Q9FG74; Q17TI5: BRX; NbExp=3; IntAct=EBI-1103570, EBI-4426649;
CC Q9FG74; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103570, EBI-1103587;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19168677,
CC ECO:0000269|PubMed:27251533}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19168677}. Note=Colocalizes with PIN1 to the basal
CC (lower) membrane of root stele, cortex, epidermis and lateral root cap
CC cells (PubMed:19168677). Undergoes a phosphatidylinositol-4,5-
CC bisphosphate- and sterol-dependent basal-to-planar polarity switching
CC into the polar, lipid-enriched domain of root hair-forming cells just
CC before hair formation; this process is mediated by DRP1A and PIP5K3
CC (PubMed:27251533). {ECO:0000269|PubMed:19168677,
CC ECO:0000269|PubMed:27251533}.
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, exhibits basal shift in root hairs positioning, are
CC almost infertile and impaired in phototropic hypocotyl bending when
CC exposed to lateral white light. {ECO:0000269|PubMed:19168677,
CC ECO:0000269|PubMed:23709629, ECO:0000269|PubMed:27251533}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; D10937; BAA01731.1; -; mRNA.
DR EMBL; AB026659; BAB08656.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96698.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70679.1; -; Genomic_DNA.
DR PIR; S20918; S20918.
DR RefSeq; NP_001332267.1; NM_001345171.1.
DR RefSeq; NP_200402.1; NM_124973.5.
DR AlphaFoldDB; Q9FG74; -.
DR SMR; Q9FG74; -.
DR BioGRID; 20933; 7.
DR IntAct; Q9FG74; 3.
DR STRING; 3702.AT5G55910.1; -.
DR PaxDb; Q9FG74; -.
DR PRIDE; Q9FG74; -.
DR ProteomicsDB; 222600; -.
DR EnsemblPlants; AT5G55910.1; AT5G55910.1; AT5G55910.
DR EnsemblPlants; AT5G55910.2; AT5G55910.2; AT5G55910.
DR GeneID; 835689; -.
DR Gramene; AT5G55910.1; AT5G55910.1; AT5G55910.
DR Gramene; AT5G55910.2; AT5G55910.2; AT5G55910.
DR KEGG; ath:AT5G55910; -.
DR Araport; AT5G55910; -.
DR TAIR; locus:2178388; AT5G55910.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9FG74; -.
DR OMA; VPAHQVK; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q9FG74; -.
DR PRO; PR:Q9FG74; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG74; baseline and differential.
DR Genevisible; Q9FG74; AT.
DR GO; GO:0009925; C:basal plasma membrane; IDA:TAIR.
DR GO; GO:0071944; C:cell periphery; IDA:TAIR.
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:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:TAIR.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
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; Lipid-binding;
KW Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..498
FT /note="Serine/threonine-protein kinase D6PK"
FT /id="PRO_0000430035"
FT DOMAIN 109..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 246
FT /note="G -> R (in Ref. 1; BAA01731)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..470
FT /note="DLEA -> ILKL (in Ref. 1; BAA01731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 54816 MW; 54990F44790BADB8 CRC64;
MMASKTPEGS LTNSSQSMSI NTLADQVSSS LSFADPSSDG KTGNSKINEQ GESGKSSTCR
PSTSSDISDE STCSSFSSSI NKPHKANDVR WEAIQAVRTK HGGLGLNHFR LLKRLGCGDI
GTVHLAELNG TRCYFAMKVM DKTALASRKK LLRAQTEREI LQCLDHPFLP TLYSHFETEK
FSCLVMEFCP GGDLHTLRQR QPGKRFTEQA AKFYVAEVLL AMEYLHMLGI IYRDLKPENV
LVRDDGHVML SDFDLSLRCT VSLSIVRSAN VGSEGLSKNS VSCSQQPACI QQPSCISMAP
TSCFGPRFFS SKSKKDKKPK TENGNHQVTP LPELVAEPTG ARSMSFVGTH EYLAPEIIKG
EGHGSAVDWW TFGIFLYELL FGKTPFKGSG NRATLFNVVG QPLRFPESPV VSFAARDLIR
SLLVKEPQHR LAYKRGATEI KQHPFFEGVN WALVRCASPP EIPKPVDLEA LNPTPTVPAA
ASSSVRSDQS NYLEFDFF
