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KIPK2_ARATH
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   03-AUG-2022, entry version 155.
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.AT2G36350.1; -.
DR   iPTMnet; Q9SJM3; -.
DR   PaxDb; Q9SJM3; -.
DR   PRIDE; Q9SJM3; -.
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; locus:2049485; AT2G36350.
DR   eggNOG; KOG0610; Eukaryota.
DR   HOGENOM; CLU_000288_39_0_1; -.
DR   InParanoid; Q9SJM3; -.
DR   OMA; KHSSRYC; -.
DR   OrthoDB; 272753at2759; -.
DR   PhylomeDB; Q9SJM3; -.
DR   PRO; PR:Q9SJM3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJM3; baseline and differential.
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: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; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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..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
 
 
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