AGC15_ARATH
ID AGC15_ARATH Reviewed; 577 AA.
AC Q9LTW5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase AGC1-5 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:16973627};
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 1 member 5 {ECO:0000303|PubMed:13678909};
GN Name=AGC1-5 {ECO:0000303|PubMed:13678909};
GN Synonyms=AGC1.5 {ECO:0000303|PubMed:19144004};
GN OrderedLocusNames=At3g12690 {ECO:0000312|Araport:AT3G12690};
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=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 [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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19144004; DOI=10.1111/j.1365-313x.2009.03792.x;
RA Zhang Y., He J., McCormick S.;
RT "Two Arabidopsis AGC kinases are critical for the polarized growth of
RT pollen tubes.";
RL Plant J. 58:474-484(2009).
CC -!- FUNCTION: Functions redudantly with AGC1-7 as signaling component in
CC the pollen tube. Required for polarized growth of pollen tubes.
CC {ECO:0000269|PubMed:19144004}.
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 Q9LTW5; Q9XF67: PDPK1; NbExp=3; IntAct=EBI-1103747, EBI-1103587;
CC -!- TISSUE SPECIFICITY: Specifically expressed in pollen grains.
CC {ECO:0000269|PubMed:19144004}.
CC -!- PTM: Autophosphorylated and phosphorylated by PDPK1/PDK1.
CC {ECO:0000269|PubMed:16973627}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but pollen of the double mutants agc1.5 and agc1.7 is
CC impaired in polarized growth of pollen tube.
CC {ECO:0000269|PubMed:19144004}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB024033; BAB02413.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75233.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75234.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75235.1; -; Genomic_DNA.
DR EMBL; BT011689; AAS49052.1; -; mRNA.
DR EMBL; BT020332; AAV85687.1; -; mRNA.
DR EMBL; AK229198; BAF01068.1; -; mRNA.
DR RefSeq; NP_187875.1; NM_112105.5.
DR RefSeq; NP_974295.1; NM_202566.2.
DR RefSeq; NP_974296.1; NM_202567.2.
DR AlphaFoldDB; Q9LTW5; -.
DR SMR; Q9LTW5; -.
DR BioGRID; 5784; 1.
DR IntAct; Q9LTW5; 1.
DR STRING; 3702.AT3G12690.2; -.
DR iPTMnet; Q9LTW5; -.
DR PaxDb; Q9LTW5; -.
DR PRIDE; Q9LTW5; -.
DR ProteomicsDB; 244883; -.
DR EnsemblPlants; AT3G12690.1; AT3G12690.1; AT3G12690.
DR EnsemblPlants; AT3G12690.2; AT3G12690.2; AT3G12690.
DR EnsemblPlants; AT3G12690.3; AT3G12690.3; AT3G12690.
DR GeneID; 820450; -.
DR Gramene; AT3G12690.1; AT3G12690.1; AT3G12690.
DR Gramene; AT3G12690.2; AT3G12690.2; AT3G12690.
DR Gramene; AT3G12690.3; AT3G12690.3; AT3G12690.
DR KEGG; ath:AT3G12690; -.
DR Araport; AT3G12690; -.
DR TAIR; locus:2087785; AT3G12690.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9LTW5; -.
DR OMA; ADFHSSW; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q9LTW5; -.
DR PRO; PR:Q9LTW5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTW5; baseline and differential.
DR Genevisible; Q9LTW5; 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; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
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..577
FT /note="Serine/threonine-protein kinase AGC1-5"
FT /id="PRO_0000431358"
FT DOMAIN 185..509
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 510..577
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000305"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 191..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 577 AA; 63768 MW; 2CD2C7C30FAFA9A2 CRC64;
MDLASKKNTA NVGSKEIDPI KPKSPRSSLS PFSLKLGDNV PRNPHFDPKK MDPLVKHQPP
KSLEPPPSTR GTNSEGDLKH NTYSSDGDSL AMRKNAPKNL HYDPKKIVPL TTSETYSPSA
RNHHHHRTKS PDKKRAPRHN GDYAYGDNLV GPSAQPFKPH TGGDVRWDAI NSIASKGPQI
GLDNFRLLKR LGYGDIGSVY LADLRGTNAV FAMKVMDKAS LASRNKLLRA QTEREILSLL
DHPFLPTLYS YFETDKFYCL VMEFCSGGNL HSLRQKQPSR RFTEEAARFY ASEVLLALEY
LHMLGVVYRD LKPENILVRD EGHIMLSDFD LSLRCTFNPT LVKSSSVCSG GGAILNEEFA
VNGCMHPSAF LPRLLPSKKT RKAKSDSGLG GLSMPELMAE PTDVRSMSFV GTHEYLAPEI
IRGEGHGSAV DWWTFGIFLY ELLHGTTPFK GQGNRATLHN VVGQPLKFPD TPHVSSAARD
LIRGLLVKDP HRRIAYTRGA TEIKQHPFFE GVNWALVRSA APPHIPDPVD LGPYAAARGK
TKSHGGGDHC NSMKPEPLVA CAAGPTDDTA YIDFEYF
