D6KL2_ARATH
ID D6KL2_ARATH Reviewed; 586 AA.
AC Q39183; Q8W4K8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase D6PKL2;
DE EC=2.7.11.1;
DE AltName: Full=D6 protein kinase-like 2;
DE AltName: Full=Serine/threonine-protein kinase AtPK5;
GN Name=D6PKL2; Synonyms=PK5; OrderedLocusNames=At5g47750; ORFNames=MCA23.7;
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=8444349; DOI=10.1016/0378-1119(93)90401-n;
RA Hayashida N., Mizoguchi T., Shinozaki K.;
RT "Cloning and characterization of a plant gene encoding a protein kinase.";
RL Gene 124:251-255(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 [6]
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 Q39183; Q9XF67: PDPK1; NbExp=4; IntAct=EBI-1103628, 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 -!- 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}.
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DR EMBL; D10909; BAA01715.1; -; Genomic_DNA.
DR EMBL; AB016886; BAB11322.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95568.1; -; Genomic_DNA.
DR EMBL; AY054227; AAL06887.1; -; mRNA.
DR EMBL; AY062501; AAL32579.1; -; mRNA.
DR EMBL; AY093303; AAM13302.1; -; mRNA.
DR EMBL; AY113177; AAM47480.1; -; mRNA.
DR PIR; JN0505; JN0505.
DR RefSeq; NP_199586.1; NM_124149.4.
DR AlphaFoldDB; Q39183; -.
DR SMR; Q39183; -.
DR IntAct; Q39183; 1.
DR STRING; 3702.AT5G47750.1; -.
DR iPTMnet; Q39183; -.
DR PaxDb; Q39183; -.
DR PRIDE; Q39183; -.
DR ProteomicsDB; 222599; -.
DR EnsemblPlants; AT5G47750.1; AT5G47750.1; AT5G47750.
DR GeneID; 834826; -.
DR Gramene; AT5G47750.1; AT5G47750.1; AT5G47750.
DR KEGG; ath:AT5G47750; -.
DR Araport; AT5G47750; -.
DR TAIR; locus:2160922; AT5G47750.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q39183; -.
DR OMA; TNDVRWE; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q39183; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:Q39183; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39183; baseline and differential.
DR Genevisible; Q39183; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; TAS:UniProtKB.
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:0010540; P:basipetal auxin transport; TAS:UniProtKB.
DR GO; GO:0009638; P:phototropism; 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..586
FT /note="Serine/threonine-protein kinase D6PKL2"
FT /id="PRO_0000430037"
FT DOMAIN 191..527
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 418
FT /note="E -> K (in Ref. 4; AAL32579/AAM13302)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 64557 MW; 6F0F287E2AE970C9 CRC64;
MASTRKPSGH GAEVEAQKRS SSNSSTKSAK AETFEPMQLQ RSVTNPRAVG IPESKRLPES
FRKRSSDPAV CKPDFSSLST VLEHVDSLTI DEKKTSGFGS VKTSSASAKL SDGTSSLGKT
SGSAKLSGRL DFMESGKSSI CRGSTSSDVS DESSCSSFSS TVNKPHKAND LRWEAIQAVR
VRDGLLGLSH FRLLKRLGCG DIGSVYLSEL SGTKCYFAMK VMDKTSLASR KKLLRAQTER
EILQSLDHPF LPTLYTHFET EKFSCLVMEF CPGGDLHTLR QRQPGKHFSE QAVKFYIAES
LLALEYLHML GIVYRDLKPE NVLVREDGHI MLSDFDLSLR CLVSPTLVKS AAIESDPLRK
NVYCVQPACI EPSCIQPSCT VPTTCFSPRL FSSKSKKDRK PKNDTANQVR PLPELVAEPT
DARSMSFVGT HEYLAPEIIK GEGHGSAVDW WTFGIFLYEL LFGRTPFKGS GNRQTLFNVV
GQPLRFPETP VVSFAARDLI RGLLMKEPQQ RLGFKRGATE VKQHPFFEGV NWALIRCATP
PEIPKPVELE KGAVSVAEAP SSQKTAAGLV LNAQKGSDNY LEFDFF
