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 16-SEP-2015, entry version 82. 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|TAIR:AT1G79250}; GN ORFNames=YUP8H12R.15 {ECO:0000312|EMBL:AAC17041.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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 RT kinases."; RL Trends Plant Sci. 8:424-431(2003). RN [5] RP CATALYTIC ACTIVITY, ENZYME 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., RA Glenny S., Payne G.S., Christensen S.K.; RT "Structural and functional insights into the regulation of Arabidopsis RT AGC 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 CC in the pollen tube. Required for polarized growth of pollen tubes. CC {ECO:0000269|PubMed:19144004}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000269|PubMed:16973627}. CC -!- ENZYME REGULATION: Activated by PDPK1/PDK1. CC {ECO:0000269|PubMed:16973627}. CC -!- SUBUNIT: Interacts with PDPK1/PDK1. {ECO:0000269|PubMed:16973627}. CC -!- INTERACTION: CC 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 -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC17041.1; 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; AC002986; AAC17041.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE36222.1; -; Genomic_DNA. DR EMBL; CP002684; AEE36223.1; -; Genomic_DNA. DR EMBL; DQ446444; ABE65785.1; -; mRNA. DR PIR; T01032; T01032. DR RefSeq; NP_001185434.1; NM_001198505.1. DR RefSeq; NP_178045.2; NM_106575.3. DR UniGene; At.50049; -. DR ProteinModelPortal; Q1PFB9; -. DR SMR; Q1PFB9; 94-513. DR BioGrid; 29484; 1. DR IntAct; Q1PFB9; 1. DR STRING; 3702.AT1G79250.1; -. DR PRIDE; Q1PFB9; -. DR EnsemblPlants; AT1G79250.1; AT1G79250.1; AT1G79250. DR EnsemblPlants; AT1G79250.2; AT1G79250.2; AT1G79250. DR GeneID; 844265; -. DR KEGG; ath:AT1G79250; -. DR TAIR; AT1G79250; -. DR HOGENOM; HOG000233027; -. DR InParanoid; Q1PFB9; -. DR OMA; STHHTTS; -. DR PhylomeDB; Q1PFB9; -. DR BioCyc; ARA:AT1G79250-MONOMER; -. DR BioCyc; ARA:GQT-1460-MONOMER; -. DR PRO; PR:Q1PFB9; -. DR Proteomes; UP000006548; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; 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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR011993; PH/PTB_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Growth regulation; Kinase; KW Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 555 Serine/threonine-protein kinase AGC1-7. FT /FTId=PRO_0000431357. FT DOMAIN 146 480 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 481 555 AGC-kinase C-terminal. {ECO:0000305}. FT NP_BIND 152 160 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT COMPBIAS 87 102 Asn-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00003}. FT ACT_SITE 271 271 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 175 175 ATP. {ECO:0000255|PROSITE- FT 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 //