CDG1_ARATH
ID CDG1_ARATH Reviewed; 432 AA.
AC Q9LSE1; A0MEY6; Q84UJ3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Serine/threonine-protein kinase CDG1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:21855796};
DE AltName: Full=Protein CONSTITUTIVE DIFFERENTIAL GROWTH 1 {ECO:0000303|PubMed:15466232};
GN Name=CDG1 {ECO:0000303|PubMed:15466232};
GN OrderedLocusNames=At3g26940 {ECO:0000312|Araport:AT3G26940};
GN ORFNames=MOJ10.2 {ECO:0000312|EMBL:BAB01076.1};
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], TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15466232; DOI=10.1104/pp.104.046805;
RA Muto H., Yabe N., Asami T., Hasunuma K., Yamamoto K.T.;
RT "Overexpression of constitutive differential growth 1 gene, which encodes a
RT RLCKVII-subfamily protein kinase, causes abnormal differential and
RT elongation growth after organ differentiation in Arabidopsis.";
RL Plant Physiol. 136:3124-3133(2004).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH BSU1; BSL1 AND BRI1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-44; SER-47
RP AND SER-234, PALMITOYLATION AT CYS-4 AND CYS-6, MUTAGENESIS OF CYS-4; CYS-6
RP AND TYR-147, AND DISRUPTION PHENOTYPE.
RX PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
RA Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
RT "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1
RT receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
RL Mol. Cell 43:561-571(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the positive
CC regulation of brassinosteroid (BR) signaling and plant growth. Mediates
CC BR signal transduction from BRI1 receptor kinase to BSU1 phosphatase.
CC After activation by phosphorylation at Ser-234 by BRI1, CDG1
CC phosphorylates BSU1 at 'Ser-764' in the phosphatase domain, increasing
CC the ability of BSU1 to inactivate the negative regulator of BR
CC signaling ASK7/BIN2 by dephosphorylation at 'Tyr-200'. The full kinase
CC activity of CDG1 is required for its biological function.
CC {ECO:0000269|PubMed:21855796}.
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:21855796};
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:21855796};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-234.
CC {ECO:0000269|PubMed:21855796}.
CC -!- SUBUNIT: Interacts with BSU1, BSL1 and BRI1.
CC {ECO:0000269|PubMed:21855796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21855796};
CC Lipid-anchor {ECO:0000303|PubMed:21855796}. Note=Plasma membrane
CC localization is required for CDG1 to function in BR signaling.
CC {ECO:0000269|PubMed:21855796}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the stamen and pollen
CC grains (PubMed:21855796). Expressed at a very low level in vegetative
CC tissues (PubMed:15466232, PubMed:21855796).
CC {ECO:0000269|PubMed:15466232, ECO:0000269|PubMed:21855796}.
CC -!- PTM: Phosphorylated at Ser-44, Ser-47 and Ser-234 by BRI1.
CC {ECO:0000269|PubMed:21855796}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:15466232, ECO:0000269|PubMed:21855796}.
CC -!- MISCELLANEOUS: The gain of function mutants cdg1-D (T-DNA tagging) show
CC pleiotropic phenotype such as dwarfism, exaggerated leaf epinasty and
CC twisted or spiral growth in hypocotyl, inflorescence stem, and petiole.
CC {ECO:0000269|PubMed:15466232}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28574.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB099698; BAC67214.1; -; mRNA.
DR EMBL; AB026649; BAB01076.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77248.1; -; Genomic_DNA.
DR EMBL; DQ446706; ABE65973.1; -; mRNA.
DR EMBL; DQ653109; ABK28574.1; ALT_SEQ; mRNA.
DR RefSeq; NP_189330.1; NM_113608.3.
DR AlphaFoldDB; Q9LSE1; -.
DR SMR; Q9LSE1; -.
DR BioGRID; 7642; 6.
DR STRING; 3702.AT3G26940.1; -.
DR iPTMnet; Q9LSE1; -.
DR PaxDb; Q9LSE1; -.
DR PRIDE; Q9LSE1; -.
DR EnsemblPlants; AT3G26940.1; AT3G26940.1; AT3G26940.
DR GeneID; 822312; -.
DR Gramene; AT3G26940.1; AT3G26940.1; AT3G26940.
DR KEGG; ath:AT3G26940; -.
DR Araport; AT3G26940; -.
DR TAIR; locus:2091980; AT3G26940.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q9LSE1; -.
DR OMA; IQGHHYL; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LSE1; -.
DR PRO; PR:Q9LSE1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSE1; baseline and differential.
DR Genevisible; Q9LSE1; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane; Kinase;
KW Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..432
FT /note="Serine/threonine-protein kinase CDG1"
FT /id="PRO_0000431232"
FT DOMAIN 74..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 15..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 147
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 248
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000303|PubMed:21855796"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000303|PubMed:21855796"
FT MUTAGEN 4
FT /note="C->A: Loss of plasma membrane localization; when
FT associated with Ala-6."
FT /evidence="ECO:0000269|PubMed:21855796"
FT MUTAGEN 6
FT /note="C->A: Loss of plasma membrane localization; when
FT associated with Ala-4."
FT /evidence="ECO:0000269|PubMed:21855796"
FT MUTAGEN 147
FT /note="Y->G: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:21855796"
FT CONFLICT 38
FT /note="T -> A (in Ref. 1; BAC67214)"
FT CONFLICT 424
FT /note="Missing (in Ref. 1; BAC67214)"
SQ SEQUENCE 432 AA; 48507 MW; 05084EF1E951A70A CRC64;
MVSCLCFRPS RKTKLKDKSH KRSIRNQTSS SSAQPAGTAK EVDSSSSQTV VQDSSRYRCQ
IFSYRELAIA TNSFRNESLI GRGGFGTVYK GRLSTGQNIA VKMLDQSGIQ GDKEFLVEVL
MLSLLHHRNL VHLFGYCAEG DQRLVVYEYM PLGSVEDHLY DLSEGQEALD WKTRMKIALG
AAKGLAFLHN EAQPPVIYRD LKTSNILLDH DYKPKLSDFG LAKFGPSDDM SHVSTRVMGT
HGYCAPEYAN TGKLTLKSDI YSFGVVLLEL ISGRKALMPS SECVGNQSRY LVHWARPLFL
NGRIRQIVDP RLARKGGFSN ILLYRGIEVA FLCLAEEANA RPSISQVVEC LKYIIDHTIR
KERRTRRRLL GGNKDGAGTS RSPDETMMRM LEEEEEYVTS EEAIERRRVI VDDARTWAGM
NRRGATPPTP TP
