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 22-FEB-2023, entry version 115. 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. [B5X4Z9-1] DR RefSeq; NP_179266.2; NM_127227.6. [B5X4Z9-1] DR AlphaFoldDB; B5X4Z9; -. DR SMR; B5X4Z9; -. DR STRING; 3702.AT2G16750.1; -. DR PaxDb; 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; 1210882at2759; -. DR PhylomeDB; B5X4Z9; -. DR PRO; PR: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: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 CDD; cd00293; USP_Like; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR046958; RBK1/2/STUNTED. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR47987; OS08G0249100 PROTEIN; 1. DR PANTHER; PTHR47987:SF11; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //