STU_ARATH
ID STU_ARATH Reviewed; 617 AA.
AC B5X4Z9; A0A178VX47; Q67Z29; Q9SLE3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein kinase STUNTED {ECO:0000303|PubMed:22492352};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=STU {ECO:0000303|PubMed:22492352};
GN OrderedLocusNames=At2g16750 {ECO:0000312|Araport:AT2G16750};
GN ORFNames=T24I21.16 {ECO:0000312|EMBL:AAD24608.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY GIBBERELLINS, REPRESSION BY RGA, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22492352; DOI=10.1242/dev.079426;
RA Lee L.Y.C., Hou X., Fang L., Fan S., Kumar P.P., Yu H.;
RT "STUNTED mediates the control of cell proliferation by GA in Arabidopsis.";
RL Development 139:1568-1576(2012).
CC -!- FUNCTION: Promotes cell proliferation in the gibberellic acid (GA)
CC signaling pathway, acting downstream of RGA, and possibly through a
CC negative regulation of two cyclin-dependent kinase inhibitors SIM and
CC SMR1. {ECO:0000269|PubMed:22492352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22492352}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B5X4Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B5X4Z9-2; Sequence=VSP_061267;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, mostly in roots, to a lower
CC extent in leaves, floral buds and stems, and, at low levels, in flowers
CC and siliques. {ECO:0000269|PubMed:22492352}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, observed in shoot apices and
CC roots and accumulates gradually in the leaf vasculature
CC (PubMed:22492352). Later expressed in inflorescence apices, especially
CC in the center, and in secondary inflorescence meristems
CC (PubMed:22492352). In floral buds and flowers, strongly present in
CC anthers (specifically in the tapetum), ovules and pollen
CC (PubMed:22492352). {ECO:0000269|PubMed:22492352}.
CC -!- INDUCTION: Induced by gibberellins (GA) in seedlings shoot apices, in
CC tissues containing actively dividing cells (PubMed:22492352). Down-
CC regulated by RGA in the GA signaling pathway (PubMed:22492352).
CC {ECO:0000269|PubMed:22492352}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: General retarded growth with small curled leaves
CC and short roots in seedlings, as well as delayed floral transition and
CC lower fertility; these phenotypes are partly due to a reduced cell
CC proliferation. {ECO:0000269|PubMed:22492352}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24608.1; Type=Erroneous gene model prediction; Evidence={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; AC005825; AAD24608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06534.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61982.1; -; Genomic_DNA.
DR EMBL; AK176289; BAD44052.1; -; mRNA.
DR EMBL; BT046118; ACI46506.1; -; mRNA.
DR PIR; G84543; G84543.
DR RefSeq; NP_001318232.1; NM_001335488.1.
DR RefSeq; NP_179266.2; NM_127227.6.
DR AlphaFoldDB; B5X4Z9; -.
DR SMR; B5X4Z9; -.
DR STRING; 3702.AT2G16750.1; -.
DR PaxDb; B5X4Z9; -.
DR PRIDE; B5X4Z9; -.
DR ProteomicsDB; 181274; -.
DR EnsemblPlants; AT2G16750.1; AT2G16750.1; AT2G16750. [B5X4Z9-1]
DR EnsemblPlants; AT2G16750.2; AT2G16750.2; AT2G16750. [B5X4Z9-1]
DR GeneID; 816176; -.
DR Gramene; AT2G16750.1; AT2G16750.1; AT2G16750. [B5X4Z9-1]
DR Gramene; AT2G16750.2; AT2G16750.2; AT2G16750. [B5X4Z9-1]
DR KEGG; ath:AT2G16750; -.
DR Araport; AT2G16750; -.
DR TAIR; locus:2059919; AT2G16750.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_155_2_1; -.
DR InParanoid; B5X4Z9; -.
DR OMA; IHETREM; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; B5X4Z9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; B5X4Z9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF00069; Pkinase; 1.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm;
KW Gibberellin signaling pathway; Hydrolase; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..617
FT /note="Protein kinase STUNTED"
FT /id="PRO_0000454232"
FT DOMAIN 277..555
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 162..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 283..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 350
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 447
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT VAR_SEQ 1..493
FT /note="Missing (in isoform 2)"
FT /id="VSP_061267"
SQ SEQUENCE 617 AA; 68877 MW; 8DF18CBC98784613 CRC64;
MAVDKVIVKQ RNIILVGIPI DESGVEVLKW ALEEVAKHGD CVVVVHVCFT YYRALKSKSS
LDRYLKPYIE FCSTKKIELK GEVLKGNSVL GVLVKEAKRY NAMSVVVGVK QQSKLSLKIA
KGCAKELPST TDILAIHRGN IVFRRSNHYQ LPLAQKISSR PSSELSEGFS DKDLAKTTGQ
EKRKISGRSL SLPSVEVVDQ TPGWPLLRTS TLATPMVQHQ TRKISVVNWV MSLPERFPHH
PNQTCQQSFC DKQLKDILKD INRWFSYDVL KTATSDFSLE NLIGKGGCNE VYKGFLEDGK
GVAVKILKPS VKEAVKEFVH EVSIVSSLSH SNISPLIGVC VHYNDLISVY NLSSKGSLEE
TLQGKHVLRW EERLKIAIGL GEALDYLHNQ CSNPVIHRDV KSSNVLLSDE FEPQLSDFGL
SMWGSKSCRY TIQRDVVGTF GYLAPEYFMY GKVSDKVDVY AFGVVLLELI SGRTSISSDS
PRGQESLVMW AKPMIEKGNA KELLDPNIAG TFDEDQFHKM VLAATHCLTR AATYRPNIKE
ILKLLRGEDD VSKWVKIEED DEDGFDDEVY PNSNTELHLS LAMVDVEDND SVSNSSLERS
NNSLFSSSSS SSQELQS
