CDPKS_ARATH
ID CDPKS_ARATH Reviewed; 523 AA.
AC Q9FKW4; A8MQP5; Q0WNW9; Q8LDS1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Calcium-dependent protein kinase 28 {ECO:0000303|Ref.6};
DE EC=2.7.11.1 {ECO:0000269|PubMed:25525792};
GN Name=CPK28 {ECO:0000303|Ref.6}; OrderedLocusNames=At5g66210;
GN ORFNames=K2A18.29;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RA Harmon A.C., Gribskov M., Gubrium E., Harper J.F.;
RT "The CDPK superfamily of protein kinases.";
RL New Phytol. 151:175-183(2001).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12068094; DOI=10.1104/pp.005645;
RA Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J.;
RT "Calcium signaling through protein kinases. The Arabidopsis calcium-
RT dependent protein kinase gene family.";
RL Plant Physiol. 129:469-485(2002).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12913141; DOI=10.1104/pp.103.020008;
RA Dammann C., Ichida A., Hong B., Romanowsky S.M., Hrabak E.M., Harmon A.C.,
RA Pickard B.G., Harper J.F.;
RT "Subcellular targeting of nine calcium-dependent protein kinase isoforms
RT from Arabidopsis.";
RL Plant Physiol. 132:1840-1848(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-228; SER-318 AND
RP SER-495, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23252373; DOI=10.1111/tpj.12090;
RA Matschi S., Werner S., Schulze W.X., Legen J., Hilger H.H., Romeis T.;
RT "Function of calcium-dependent protein kinase CPK28 of Arabidopsis thaliana
RT in plant stem elongation and vascular development.";
RL Plant J. 73:883-896(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BIK1, AND MUTAGENESIS OF
RP SER-245 AND ALA-295.
RX PubMed=25525792; DOI=10.1016/j.chom.2014.10.007;
RA Monaghan J., Matschi S., Shorinola O., Rovenich H., Matei A., Segonzac C.,
RA Malinovsky F.G., Rathjen J.P., MacLean D., Romeis T., Zipfel C.;
RT "The calcium-dependent protein kinase CPK28 buffers plant immunity and
RT regulates BIK1 turnover.";
RL Cell Host Microbe 16:605-615(2014).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger (Probable). Acts as developmentally
CC controlled regulator for coordinated stem elongation and vascular
CC development. Acts as key component which contributes to the
CC developmental switch that establishes the transition from vegetative to
CC reproductive growth (PubMed:23252373). Involved in pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI) signaling. Interacts
CC with and phosphorylates the kinase BIK1, a central rate-limiting kinase
CC in PTI signaling. Facilitates BIK1 turnover and negatively regulates
CC BIK1-mediated immune responses triggered by several PAMPs. Its kinase
CC activity is necessary and sufficient for its function in PTI signaling
CC (PubMed:25525792). {ECO:0000269|PubMed:23252373,
CC ECO:0000269|PubMed:25525792, ECO:0000305|PubMed:23252373}.
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:25525792};
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:25525792};
CC -!- ACTIVITY REGULATION: Activated by calcium (PubMed:23252373).
CC Autophosphorylation plays an important role in the regulation of the
CC kinase activity (PubMed:23252373). {ECO:0000269|PubMed:23252373}.
CC -!- SUBUNIT: Interacts with BIK1. {ECO:0000269|PubMed:25525792}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12913141};
CC Lipid-anchor {ECO:0000269|PubMed:12913141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FKW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKW4-2; Sequence=VSP_036294, VSP_036295;
CC Name=3;
CC IsoId=Q9FKW4-3; Sequence=VSP_036292, VSP_036293;
CC -!- TISSUE SPECIFICITY: Expressed in vascular and meristematic tissues
CC throughout plant development. {ECO:0000269|PubMed:23252373}.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (328-358) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Severe growth defect in shoot elongation. Severe
CC growth defect of flowering stem. {ECO:0000269|PubMed:23252373}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB011474; BAB10426.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98177.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98178.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98179.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98180.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69530.1; -; Genomic_DNA.
DR EMBL; AY139991; AAM98133.1; -; mRNA.
DR EMBL; BT010380; AAQ56823.1; -; mRNA.
DR EMBL; AK227052; BAE99112.1; -; mRNA.
DR EMBL; AK229317; BAF01180.1; -; mRNA.
DR EMBL; AY085837; AAM63052.1; -; mRNA.
DR RefSeq; NP_001078806.1; NM_001085337.1. [Q9FKW4-2]
DR RefSeq; NP_001119508.1; NM_001126036.2. [Q9FKW4-3]
DR RefSeq; NP_001331200.1; NM_001345752.1. [Q9FKW4-3]
DR RefSeq; NP_201422.1; NM_126019.4. [Q9FKW4-1]
DR RefSeq; NP_851280.1; NM_180949.3. [Q9FKW4-1]
DR AlphaFoldDB; Q9FKW4; -.
DR SMR; Q9FKW4; -.
DR STRING; 3702.AT5G66210.1; -.
DR iPTMnet; Q9FKW4; -.
DR SwissPalm; Q9FKW4; -.
DR PaxDb; Q9FKW4; -.
DR PRIDE; Q9FKW4; -.
DR ProteomicsDB; 224395; -. [Q9FKW4-1]
DR EnsemblPlants; AT5G66210.1; AT5G66210.1; AT5G66210. [Q9FKW4-1]
DR EnsemblPlants; AT5G66210.2; AT5G66210.2; AT5G66210. [Q9FKW4-1]
DR EnsemblPlants; AT5G66210.3; AT5G66210.3; AT5G66210. [Q9FKW4-2]
DR EnsemblPlants; AT5G66210.4; AT5G66210.4; AT5G66210. [Q9FKW4-3]
DR EnsemblPlants; AT5G66210.6; AT5G66210.6; AT5G66210. [Q9FKW4-3]
DR GeneID; 836753; -.
DR Gramene; AT5G66210.1; AT5G66210.1; AT5G66210. [Q9FKW4-1]
DR Gramene; AT5G66210.2; AT5G66210.2; AT5G66210. [Q9FKW4-1]
DR Gramene; AT5G66210.3; AT5G66210.3; AT5G66210. [Q9FKW4-2]
DR Gramene; AT5G66210.4; AT5G66210.4; AT5G66210. [Q9FKW4-3]
DR Gramene; AT5G66210.6; AT5G66210.6; AT5G66210. [Q9FKW4-3]
DR KEGG; ath:AT5G66210; -.
DR Araport; AT5G66210; -.
DR TAIR; locus:2156947; AT5G66210.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_2_1; -.
DR InParanoid; Q9FKW4; -.
DR OMA; CKKPTEN; -.
DR PhylomeDB; Q9FKW4; -.
DR PRO; PR:Q9FKW4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW4; baseline and differential.
DR Genevisible; Q9FKW4; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Cell membrane;
KW Developmental protein; Growth regulation; Kinase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Plant defense; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..523
FT /note="Calcium-dependent protein kinase 28"
FT /id="PRO_0000363350"
FT DOMAIN 62..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 365..400
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 402..437
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 444..479
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 482..509
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 15..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..358
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 487
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23252373"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23252373"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23252373"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT VAR_SEQ 414..435
FT /note="IDSNTDGLVDFTEFVAAALHVH -> VVIFLFSIAIASLGVSEGDVVS (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_036292"
FT VAR_SEQ 436..523
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_036293"
FT VAR_SEQ 472..488
FT /note="HTGLRGSIDPLLDEADI -> AQQNKERKWSENPIDEI (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036294"
FT VAR_SEQ 489..523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036295"
FT MUTAGEN 188
FT /note="D->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:25525792"
FT MUTAGEN 245
FT /note="S->L: In mod1; abolishes kinase activity; when
FT associated with V-295."
FT /evidence="ECO:0000269|PubMed:25525792"
FT MUTAGEN 295
FT /note="A->V: In mod1; abolishes kinase activity; when
FT associated with L-245."
FT /evidence="ECO:0000269|PubMed:25525792"
FT CONFLICT 34
FT /note="K -> E (in Ref. 4; BAF01180)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="G -> D (in Ref. 5; AAM63052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 58972 MW; C4211CAA1F22619D CRC64;
MGVCFSAIRV TGASSSRRSS QTKSKAAPTP IDTKASTKRR TGSIPCGKRT DFGYSKDFHD
HYTIGKLLGH GQFGYTYVAI HRPNGDRVAV KRLDKSKMVL PIAVEDVKRE VQILIALSGH
ENVVQFHNAF EDDDYVYIVM ELCEGGELLD RILSKKGNRY SEKDAAVVVR QMLKVAGECH
LHGLVHRDMK PENFLFKSAQ LDSPLKATDF GLSDFIKPGK RFHDIVGSAY YVAPEVLKRR
SGPESDVWSI GVITYILLCG RRPFWDRTED GIFKEVLRNK PDFSRKPWAT ISDSAKDFVK
KLLVKDPRAR LTAAQALSHA WVREGGNATD IPVDISVLNN LRQFVRYSRL KQFALRALAS
TLDEAEISDL RDQFDAIDVD KNGVISLEEM RQALAKDLPW KLKDSRVAEI LEAIDSNTDG
LVDFTEFVAA ALHVHQLEEH DSEKWQLRSR AAFEKFDLDK DGYITPEELR MHTGLRGSID
PLLDEADIDR DGKISLHEFR RLLRTASISS QRAPSPAGHR NLR
