RHS3_ARATH
ID RHS3_ARATH Reviewed; 499 AA.
AC F4I4F2; A0ME72; Q1PFV6; Q9SA43;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine-protein kinase RHS3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:16973627};
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 1 member 6 {ECO:0000303|PubMed:13678909};
DE AltName: Full=Protein ROOT HAIR SPECIFIC 3 {ECO:0000303|PubMed:19448035};
GN Name=RHS3 {ECO:0000303|PubMed:19448035};
GN Synonyms=AGC1-6 {ECO:0000303|PubMed:13678909};
GN OrderedLocusNames=At1g16440 {ECO:0000312|Araport:AT1G16440};
GN ORFNames=F3O9.24 {ECO:0000312|EMBL:AAD34696.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 69-499.
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 [4]
RP GENE FAMILY.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH PDPK1/PDK1,
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION BY PDPK1/PDK1.
RX PubMed=16973627; DOI=10.1074/jbc.m605167200;
RA Zegzouti H., Li W., Lorenz T.C., Xie M., Payne C.T., Smith K., Glenny S.,
RA Payne G.S., Christensen S.K.;
RT "Structural and functional insights into the regulation of Arabidopsis AGC
RT VIIIa kinases.";
RL J. Biol. Chem. 281:35520-35530(2006).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19448035; DOI=10.1104/pp.109.140905;
RA Won S.-K., Lee Y.-J., Lee H.-Y., Heo Y.-K., Cho M., Cho H.-T.;
RT "Cis-element- and transcriptome-based screening of root hair-specific genes
RT and their functional characterization in Arabidopsis.";
RL Plant Physiol. 150:1459-1473(2009).
CC -!- FUNCTION: Involved in root hair growth and morphogenesis.
CC {ECO:0000269|PubMed:19448035}.
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:16973627};
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:16973627};
CC -!- ACTIVITY REGULATION: Activated by PDPK1/PDK1.
CC {ECO:0000269|PubMed:16973627}.
CC -!- SUBUNIT: Interacts with PDPK1/PDK1. {ECO:0000269|PubMed:16973627}.
CC -!- INTERACTION:
CC F4I4F2; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103713, EBI-1103587;
CC -!- TISSUE SPECIFICITY: Specifically expressed in root hair cells.
CC {ECO:0000269|PubMed:19448035}.
CC -!- PTM: Autophosphorylated and phosphorylated by PDPK1/PDK1.
CC {ECO:0000269|PubMed:16973627}.
CC -!- MISCELLANEOUS: Plants over-expressing RHS3 show altered root hair
CC morphology, such as spiral, bent or branched hairs.
CC {ECO:0000269|PubMed:19448035}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABK28399.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006341; AAD34696.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29451.1; -; Genomic_DNA.
DR EMBL; DQ446257; ABE65627.1; -; mRNA.
DR EMBL; DQ652840; ABK28399.1; ALT_SEQ; mRNA.
DR PIR; G86299; G86299.
DR RefSeq; NP_173094.4; NM_101510.6.
DR AlphaFoldDB; F4I4F2; -.
DR SMR; F4I4F2; -.
DR IntAct; F4I4F2; 1.
DR STRING; 3702.AT1G16440.1; -.
DR iPTMnet; F4I4F2; -.
DR PaxDb; F4I4F2; -.
DR PRIDE; F4I4F2; -.
DR ProteomicsDB; 236918; -.
DR EnsemblPlants; AT1G16440.1; AT1G16440.1; AT1G16440.
DR GeneID; 838214; -.
DR Gramene; AT1G16440.1; AT1G16440.1; AT1G16440.
DR KEGG; ath:AT1G16440; -.
DR Araport; AT1G16440; -.
DR TAIR; locus:2032785; AT1G16440.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; F4I4F2; -.
DR OMA; CYQPSAF; -.
DR OrthoDB; 799520at2759; -.
DR PRO; PR:F4I4F2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I4F2; baseline and differential.
DR Genevisible; F4I4F2; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0080147; P:root hair cell development; IMP:UniProtKB.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..499
FT /note="Serine/threonine-protein kinase RHS3"
FT /id="PRO_0000431359"
FT DOMAIN 113..436
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 437..499
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000305"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 499 AA; 56130 MW; AB39C980201CDFD7 CRC64;
MLLKPGNKLV SPETSHHRDS ASNSSNHKCQ QQKPRKDKQK QVEQNTKKIE EHQIKSESTL
LISNHNVNMS SQSNNSESTS TNNSSKPHTG GDIRWDAVNS LKSRGIKLGI SDFRVLKRLG
YGDIGSVYLV ELKGANPTTY FAMKVMDKAS LVSRNKLLRA QTEREILSQL DHPFLPTLYS
HFETDKFYCL VMEFCSGGNL YSLRQKQPNK CFTEDAARFF ASEVLLALEY LHMLGIVYRD
LKPENVLVRD DGHIMLSDFD LSLRCSVNPT LVKSFNGGGT TGIIDDNAAV QGCYQPSAFF
PRMLQSSKKN RKSKSDFDGS LPELMAEPTN VKSMSFVGTH EYLAPEIIKN EGHGSAVDWW
TFGIFIYELL HGATPFKGQG NKATLYNVIG QPLRFPEYSQ VSSTAKDLIK GLLVKEPQNR
IAYKRGATEI KQHPFFEGVN WALIRGETPP HLPEPVDFSC YVKKEKESLP PAATEKKSKM
FDEANKSGSD PDYIVFEYF
