AGC17_ARATH
ID AGC17_ARATH Reviewed; 555 AA.
AC Q1PFB9; O64528;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine/threonine-protein kinase AGC1-7 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:16973627};
DE AltName: Full=AGC serine/threonine-protein kinase subfamily 1 member 7 {ECO:0000303|PubMed:13678909};
GN Name=AGC1-7 {ECO:0000303|PubMed:13678909};
GN Synonyms=AGC1.7 {ECO:0000303|PubMed:19144004};
GN OrderedLocusNames=At1g79250 {ECO:0000312|Araport:AT1G79250};
GN ORFNames=YUP8H12R.15 {ECO:0000312|EMBL:AAC17041.1};
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].
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 SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND PHOSPHORYLATION BY
RP 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, 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 AGC1-5 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 Q1PFB9; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103730, EBI-1103587;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16973627}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002986; AAC17041.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36222.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36223.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59156.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59157.1; -; Genomic_DNA.
DR EMBL; DQ446444; ABE65785.1; -; mRNA.
DR PIR; T01032; T01032.
DR RefSeq; NP_001185434.1; NM_001198505.1.
DR RefSeq; NP_001319411.1; NM_001334875.1.
DR RefSeq; NP_001319412.1; NM_001334876.1.
DR RefSeq; NP_178045.2; NM_106575.4.
DR AlphaFoldDB; Q1PFB9; -.
DR SMR; Q1PFB9; -.
DR BioGRID; 29484; 1.
DR IntAct; Q1PFB9; 1.
DR STRING; 3702.AT1G79250.2; -.
DR PaxDb; Q1PFB9; -.
DR PRIDE; Q1PFB9; -.
DR ProteomicsDB; 244660; -.
DR EnsemblPlants; AT1G79250.1; AT1G79250.1; AT1G79250.
DR EnsemblPlants; AT1G79250.2; AT1G79250.2; AT1G79250.
DR EnsemblPlants; AT1G79250.3; AT1G79250.3; AT1G79250.
DR EnsemblPlants; AT1G79250.4; AT1G79250.4; AT1G79250.
DR GeneID; 844265; -.
DR Gramene; AT1G79250.1; AT1G79250.1; AT1G79250.
DR Gramene; AT1G79250.2; AT1G79250.2; AT1G79250.
DR Gramene; AT1G79250.3; AT1G79250.3; AT1G79250.
DR Gramene; AT1G79250.4; AT1G79250.4; AT1G79250.
DR KEGG; ath:AT1G79250; -.
DR Araport; AT1G79250; -.
DR TAIR; locus:2207470; AT1G79250.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q1PFB9; -.
DR OMA; EMQKPLF; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q1PFB9; -.
DR PRO; PR:Q1PFB9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1PFB9; baseline and differential.
DR Genevisible; Q1PFB9; 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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; Cytoplasm; Growth regulation; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..555
FT /note="Serine/threonine-protein kinase AGC1-7"
FT /id="PRO_0000431357"
FT DOMAIN 146..480
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 481..555
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000305"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 152..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 555 AA; 61069 MW; 94CF9E1B15DB3496 CRC64;
MLTKPGKKLD SSESTHHTTS SNYPPLDIVH QTPQPRKEMQ QKPLFDPKKM DNLIKPEPAG
FTNHHRPNPS PKIPSSPGSN MTESQSNLNT KPNNNNSNNN SNMSSRSNSI ESTSSNPSKP
HTGGDIRWDA VNTLTSKGVQ LGISDFRLLK RLGYGDIGSV YLVELRGTIT YFAMKVMDKA
SLASRNKLLR AQTEREILSQ LDHPFLPTLY SHFETDKFYC LVMEFCGGGN LYSLRQKQPN
KCFTEDAARF FASEVLLALE YLHMLGIVYR DLKPENVLVR DDGHIMLSDF DLSLRCSVSP
TLVKSSSVHA AGGGSGSSRP VGLIDEDAAV QGCIQPSTFF PRILQSSKKN RKAKSDFGLF
VNGSMPELMA EPTNVKSMSF VGTHEYLAPE IIRGEGHGSA VDWWTFGIFI YELLYGATPF
KGQGNRATLH NVIGQALRFP EVPHVSSAAR DLIKGLLVKE PQKRIAYKRG ATEIKQHPFF
EGVNWALIRS ATPPHVPEPV DFSCYASKDK ESMAAVDGGG KKNNNGAGGG CSTGGGDNKP
NGDCNDPDYI DFEYF
