ID KIPK2_ARATH Reviewed; 949 AA.
AC Q9SJM3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase KIPK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=KIPK2 {ECO:0000303|PubMed:25262228};
GN OrderedLocusNames=At2g36350 {ECO:0000312|Araport:AT2G36350};
GN ORFNames=F2H17.4 {ECO:0000312|EMBL:AAD21431.1};
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 INTERACTION WITH KCBP; PERK8; PERK9; PERK10 AND PERK13, AND FUNCTION.
RX PubMed=25262228; DOI=10.1093/jxb/eru390;
RA Humphrey T.V., Haasen K.E., Aldea-Brydges M.G., Sun H., Zayed Y.,
RA Indriolo E., Goring D.R.;
RT "PERK-KIPK-KCBP signalling negatively regulates root growth in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 66:71-83(2015).
CC -!- FUNCTION: Serine/threonine-protein kinase that could be involved in the
CC negative regulation of root growth. {ECO:0000269|PubMed:25262228}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with KCBP, PERK8, PERK9, PERK10 and PERK13.
CC {ECO:0000269|PubMed:25262228}.
CC -!- INTERACTION:
CC Q9SJM3; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103882, EBI-1103587;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC006921; AAD21431.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09236.1; -; Genomic_DNA.
DR PIR; F84779; F84779.
DR RefSeq; NP_181176.1; NM_129192.4.
DR AlphaFoldDB; Q9SJM3; -.
DR SMR; Q9SJM3; -.
DR IntAct; Q9SJM3; 6.
DR STRING; 3702.Q9SJM3; -.
DR iPTMnet; Q9SJM3; -.
DR PaxDb; 3702-AT2G36350-1; -.
DR ProteomicsDB; 238220; -.
DR EnsemblPlants; AT2G36350.1; AT2G36350.1; AT2G36350.
DR GeneID; 818208; -.
DR Gramene; AT2G36350.1; AT2G36350.1; AT2G36350.
DR KEGG; ath:AT2G36350; -.
DR Araport; AT2G36350; -.
DR TAIR; AT2G36350; AGC1-9.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_39_0_1; -.
DR InParanoid; Q9SJM3; -.
DR OMA; CEVIDSR; -.
DR OrthoDB; 1218118at2759; -.
DR PhylomeDB; Q9SJM3; -.
DR PRO; PR:Q9SJM3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJM3; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05574; STKc_phototropin_like; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR PANTHER; PTHR45637:SF48; SERINE_THREONINE-PROTEIN KINASE KIPK2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..949
FT /note="Serine/threonine-protein kinase KIPK2"
FT /id="PRO_0000438055"
FT DOMAIN 559..898
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 79..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 684
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 565..573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 949 AA; 104521 MW; A6A581987C69F2BE CRC64;
MESFAGSCEI VEEKDAVRLA KHSSRYCMSP LGSSKDMEQR PALKSGYQGS MEYDIDQLFQ
SITIKPSPRR VMGSSFHHLE TSASAGTSRS TSPSNKGAMK KPFPMGTPRS PRVGPSDSIS
LKQALRDLCI SKASEMASQK RLSKSAAASP RVSEADRIKT LYRQVLNESA GKPGLPVDKG
KSLVEISLTP VVDIPSSSQS VPQRYDVLET EPSNFISEPS QAEILLHVLG NGSGIKTVGY
GMLETVSLCK SNKSGSCLSS GSGDYEIEID ENHTSPPHMV IEDQLVEIDK HVTSLPSCSG
SKVDTEELDK SIVSSARVKS EPTALSSGLK GKLDNFPGSG TEKSKLVSKV TRNIPRPKPR
PKKKILLKKK LKIVVNSATK MVEEVDTSLE PSASQLLCQK CHCAVKSTST ENHPPSNTSH
TTDKNVSIEA DQESLASPRL IRIVKCNKEA SKGSSDSCEV SDSGEAVIVM KQEVSPSNYS
GKGDADEQIR ANPTSSEKFD FSLSSKNSLG DYSSSTSMSE ESNLSRFSCG NKPHMSMDVR
WEAVKHVKLQ YGSLGLRHFN LLKKLGCGDI GTVYLAELVG TNCLFAIKVM DNEFLARRKK
TPRAQAERAI LKMLDHPFLP TLYAQFTSDN LSCLVMEYCP GGDLHVLRQK QLSRCFSEPA
TRFYVAEILL ALEYLHMLGV IYRDLKPENI LVREDGHIML TDFDLSLRCA VNPTLLRSTS
PPEKDPARMS GPYSTSNCIQ PLCIEPSCRV PCFSPRLLST QARNQKPRKP KRPDLLTQQF
RSLPQLVAEP TEARSNSFVG THEYLAPEII KGEGHGAAVD WWTFGVLLYE LLYGKTPFKG
YDNEETLSNV VYQNLKFPDS PLVSFQAKEL IRRLLVKDPE SRLGSEKGAA EIKRHPFFEG
LNWALIRCAI PPELPDIYDN GATEATSPEG NNRYLECKAI GDHLEFELF
//
