KIPK1_ARATH
ID KIPK1_ARATH Reviewed; 934 AA.
AC Q9LFA2; A0A1I9LSZ2; Q9M590;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase KIPK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=KCBP-interacting protein kinase {ECO:0000303|PubMed:10788494};
GN Name=KIPK1 {ECO:0000303|PubMed:25262228};
GN Synonyms=KIPK {ECO:0000303|PubMed:10788494};
GN OrderedLocusNames=At3g52890 {ECO:0000312|Araport:AT3G52890};
GN ORFNames=F8J2_60 {ECO:0000312|EMBL:CAB86893.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-934, TISSUE SPECIFICITY, INTERACTION WITH
RP KCBP, AND AUTOPHOSPHORYLATION.
RX PubMed=10788494; DOI=10.1074/jbc.275.18.13737;
RA Day I.S., Miller C., Golovkin M., Reddy A.S.;
RT "Interaction of a kinesin-like calmodulin-binding protein with a protein
RT kinase.";
RL J. Biol. Chem. 275:13737-13745(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 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: Could be involved in the negative regulation of root growth.
CC {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 (PubMed:10788494, PubMed:25262228).
CC Interacts with PERK8, PERK9, PERK10 AND PERK13 (PubMed:25262228).
CC {ECO:0000269|PubMed:10788494, ECO:0000269|PubMed:25262228}.
CC -!- INTERACTION:
CC Q9LFA2; Q9FHN8: KIN14E; NbExp=4; IntAct=EBI-1103859, EBI-1749651;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16973627}. Nucleus
CC {ECO:0000305|PubMed:16973627}. Note=Predominantly in the nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline leaves, flowers and
CC siliques. {ECO:0000269|PubMed:10788494, ECO:0000269|PubMed:16973627}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL132969; CAB86893.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79005.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79006.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65700.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65701.1; -; Genomic_DNA.
DR EMBL; AY124003; AAM74511.1; -; mRNA.
DR EMBL; BT001910; AAN71909.1; -; mRNA.
DR EMBL; BT002286; AAN72297.1; -; mRNA.
DR EMBL; AF236104; AAF68383.1; ALT_INIT; mRNA.
DR PIR; T47546; T47546.
DR RefSeq; NP_001319733.1; NM_001339591.1.
DR RefSeq; NP_001327649.1; NM_001339592.1.
DR RefSeq; NP_566973.2; NM_115149.3.
DR RefSeq; NP_850687.1; NM_180356.2.
DR AlphaFoldDB; Q9LFA2; -.
DR SMR; Q9LFA2; -.
DR BioGRID; 9772; 7.
DR IntAct; Q9LFA2; 7.
DR STRING; 3702.AT3G52890.1; -.
DR iPTMnet; Q9LFA2; -.
DR PaxDb; Q9LFA2; -.
DR PRIDE; Q9LFA2; -.
DR ProteomicsDB; 250692; -.
DR EnsemblPlants; AT3G52890.1; AT3G52890.1; AT3G52890.
DR EnsemblPlants; AT3G52890.2; AT3G52890.2; AT3G52890.
DR EnsemblPlants; AT3G52890.3; AT3G52890.3; AT3G52890.
DR EnsemblPlants; AT3G52890.4; AT3G52890.4; AT3G52890.
DR GeneID; 824455; -.
DR Gramene; AT3G52890.1; AT3G52890.1; AT3G52890.
DR Gramene; AT3G52890.2; AT3G52890.2; AT3G52890.
DR Gramene; AT3G52890.3; AT3G52890.3; AT3G52890.
DR Gramene; AT3G52890.4; AT3G52890.4; AT3G52890.
DR KEGG; ath:AT3G52890; -.
DR Araport; AT3G52890; -.
DR TAIR; locus:2085191; AT3G52890.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_39_0_1; -.
DR InParanoid; Q9LFA2; -.
DR OMA; WKEEHSS; -.
DR OrthoDB; 272753at2759; -.
DR PhylomeDB; Q9LFA2; -.
DR PRO; PR:Q9LFA2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFA2; baseline and differential.
DR Genevisible; Q9LFA2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0004672; F:protein kinase activity; IDA: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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..934
FT /note="Serine/threonine-protein kinase KIPK1"
FT /id="PRO_0000403275"
FT DOMAIN 538..879
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 663
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 544..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 934 AA; 102694 MW; 42B1CD30CA8B9BDE CRC64;
MGSFAGACEI VEEKDDEVRL PKHSGRYGKS VMGSSSKDLV ERKQREYHGS LEYDIDMLFQ
SISVKPSTTR LMSSSFHHHE TSASAGPSRT TSPSKRIASM KKPGTPQSPR FVGLSDSVSL
KQALRDRCIS KASEMAAQKR LSKSAAASPR VSEADRIKSL YNQVSNESTS SRSGLVPVDK
GKGSLVEIPL MPVNDKPSSS KSVPQRFEDP SNPISEPSQA GTSFGLQGVG NQTREIKLLH
RSNKPGSCLS SGSGDYEIEL DENVASPSTH AFVEDDVIEI DKHVTSLPSH SSKKVNATEL
DKNISSSAVD SEQKGKLDDA PNSGTENGKT VRKVTRMIPR PKQPKKKILL KKKLKIGVVS
ATYPTKDDEE IVPSLDSSAN QLLCQRCHCS LKSTSIDDNP PSYTSSHNPK ICTDSLSSVS
NKEAHQGSDE NSSGSCNVSQ SSEADIVIMK QDVSSSNNSG IGAMVEKETE NPTSSEKFEF
SLSSKDSLGD YSRSTSISEE SNLSRFSCGN KPHMSMDVRW EAIKHIKVQY GSLGLRHFNL
LKKLGCGDIG TVYLAELIGT NCLFAIKVMD NEFLARRKKS PRAQAEREIL KMLDHPFLPT
LYAQFTSDNL SCLVMEYCPG GDLHVLRQKQ LGRCFPEPAA RFYVAEILLA LEYLHMLGII
YRDLKPENIL VREDGHIMLT DFDLSLRCAV NPTLVRSNSP PGKDPARISG PYNTSNCIQP
FCITEPSCQV SCFSPRLSSN QQQGRKPKRG DHLSKTQQHL SRSLPQLVAE PTEARSNSFV
GTHEYLAPEI IKGEGHGAAV DWWTFGVLLY ELLYGKTPFK GYNNDETLAN VVLQNLKFPD
SPLVSFQAKD LIRGLLVKEP ENRLGSEKGS VEIKRHPFFE GLNWALIRCA IPPELPDFYE
YGGGPEAAAD SPGGSNNRYL ECKAIGDHLE FELF
