(data stored in SCRATCH zone)

SWISSPROT: D6KL1_ARATH

ID   D6KL1_ARATH             Reviewed;         506 AA.
AC   Q9SUA3; Q0WL51;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 139.
DE   RecName: Full=Serine/threonine-protein kinase D6PKL1;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase AGC1-2;
GN   Name=D6PKL1; OrderedLocusNames=At4g26610; ORFNames=T15N24.60;
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   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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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       Q9XF67:PDPK1; NbExp=3; IntAct=EBI-1103605, 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}.
DR   EMBL; AL078465; CAB43857.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79516.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85226.1; -; Genomic_DNA.
DR   EMBL; AY063923; AAL36279.1; -; mRNA.
DR   EMBL; AY091248; AAM14187.1; -; mRNA.
DR   EMBL; AK230357; BAF02156.1; -; mRNA.
DR   PIR; T08927; T08927.
DR   RefSeq; NP_194391.1; NM_118795.4.
DR   SMR; Q9SUA3; -.
DR   BioGrid; 14055; 1.
DR   IntAct; Q9SUA3; 1.
DR   STRING; 3702.AT4G26610.1; -.
DR   iPTMnet; Q9SUA3; -.
DR   PaxDb; Q9SUA3; -.
DR   PRIDE; Q9SUA3; -.
DR   EnsemblPlants; AT4G26610.1; AT4G26610.1; AT4G26610.
DR   GeneID; 828768; -.
DR   Gramene; AT4G26610.1; AT4G26610.1; AT4G26610.
DR   KEGG; ath:AT4G26610; -.
DR   Araport; AT4G26610; -.
DR   TAIR; locus:2133837; AT4G26610.
DR   eggNOG; KOG0610; Eukaryota.
DR   eggNOG; ENOG410XQ0C; LUCA.
DR   HOGENOM; HOG000233027; -.
DR   InParanoid; Q9SUA3; -.
DR   OMA; QNLDCNG; -.
DR   OrthoDB; 799520at2759; -.
DR   PhylomeDB; Q9SUA3; -.
DR   PRO; PR:Q9SUA3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SUA3; baseline and differential.
DR   Genevisible; Q9SUA3; 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; 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: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;
DR   PRODOM; Q9SUA3.
DR   SWISS-2DPAGE; Q9SUA3.
KW   ATP-binding; Auxin signaling pathway; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..506
FT                   /note="Serine/threonine-protein kinase D6PKL1"
FT                   /id="PRO_0000430036"
FT   DOMAIN          123..456
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         129..137
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        26..92
FT                   /note="Ser-rich"
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         152
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        95
FT                   /note="N -> D (in Ref. 4; BAF02156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  55947 MW;  AC55C73EDC85557F CRC64;
     MASKYGSGVL PENKKEKGDK ETPETSYSSQ SVSVNTLADQ VSSTLSFAPS SDSKTGGEVK
     FNEKSDQSGK SNTCRPSTSS DISDESTCSS FSGNNKPHKA NDVRWEAIQA VRTKHGVLGL
     NHFRLLKRLG CGDIGTVHLA ELHGTRCFFA MKVMDKGALA SRKKLLRAQT EREILQCLDH
     PFLPTLYSHF ETEKFSCLVM EFCPGGDLHT LRQRQPGKRF SEQAAKFYVA EVLLAMEYLH
     MLGIIYRDLK PENVLVRDDG HVMLSDFDLS LRCTVSPTVV RSTVLASEGQ KNSGYCAQPA
     CIQQPSCISA PTTCFSPRYF SSKSKKDKKM KNETGNQVSP LPELVAEPTS ARSMSFVGTH
     EYLAPEIIKG EGHGSAVDWW TFGIFLYELL FGKTPFKGSG NRATLFNVVG QPLRFPESPV
     VSFAARDLIR SLLVKEPQHR LAYKRGATEM KQHPFFEGVN WALVRCASPP EIPKPVDYES
     APATPAAATS TSVKSDQSNY LEFDFF
//

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