CKL13_ARATH
ID CKL13_ARATH Reviewed; 468 AA.
AC Q5XF24; P93816; Q84WN7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Casein kinase 1-like protein 13 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 13 {ECO:0000303|PubMed:16126836};
GN Name=CKL13 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At1g04440 {ECO:0000312|Araport:AT1G04440};
GN ORFNames=F19P19.10 {ECO:0000312|EMBL:AAB70431.1};
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=16126836; DOI=10.1105/tpc.105.034330;
RA Lee J.-Y., Taoka K., Yoo B.-C., Ben-Nissan G., Kim D.-J., Lucas W.J.;
RT "Plasmodesmal-associated protein kinase in tobacco and Arabidopsis
RT recognizes a subset of non-cell-autonomous proteins.";
RL Plant Cell 17:2817-2831(2005).
RN [2]
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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins.
CC {ECO:0000250|UniProtKB:P48730}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell
CC junction, plasmodesma {ECO:0000269|PubMed:16126836}. Note=Present in
CC punctate particles with granular structure.
CC {ECO:0000269|PubMed:16126836}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY943851; AAY24541.1; -; mRNA.
DR EMBL; AC000104; AAB70431.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27698.1; -; Genomic_DNA.
DR EMBL; BT002960; AAO22771.1; -; mRNA.
DR EMBL; BT015792; AAU90082.1; -; mRNA.
DR EMBL; BT021997; AAY25409.1; -; mRNA.
DR PIR; E86176; E86176.
DR RefSeq; NP_171939.1; NM_100324.3.
DR AlphaFoldDB; Q5XF24; -.
DR SMR; Q5XF24; -.
DR STRING; 3702.AT1G04440.1; -.
DR iPTMnet; Q5XF24; -.
DR PaxDb; Q5XF24; -.
DR PRIDE; Q5XF24; -.
DR ProteomicsDB; 246704; -.
DR EnsemblPlants; AT1G04440.1; AT1G04440.1; AT1G04440.
DR GeneID; 839520; -.
DR Gramene; AT1G04440.1; AT1G04440.1; AT1G04440.
DR KEGG; ath:AT1G04440; -.
DR Araport; AT1G04440; -.
DR TAIR; locus:2018269; AT1G04440.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q5XF24; -.
DR OMA; LMGTGCY; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q5XF24; -.
DR PRO; PR:Q5XF24; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XF24; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..468
FT /note="Casein kinase 1-like protein 13"
FT /id="PRO_0000437152"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 299..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 57
FT /note="M -> V (in Ref. 4; AAO22771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53205 MW; 6D02BF800DA417F7 CRC64;
MDRVVGGKFK LGRKLGSGSF GEIFLGVNVQ TGEEVAVKLE PLRARHPQLH YESKLYMLLQ
GGTGIPHLKW FGVEGEFNCM VIDLLGPSME EFFNYCSRSF SLKTVLMLAD QMINRVEYMH
VKGFLHRDIK PDNFLMGLGR KANQVYIIDY GLAKKYRDLQ THKHIPYREN KNLTGTARYA
SVNTHLGIEQ SRRDDLESLG YLLMYFLRGS LPWQGLRAGT KKQKYDKISE KKRLTPVEVL
CKNFPPEFTS YFLYVRSLRF EDKPDYSYLK RLFRDLFIRE GYQFDYVFDW TILRYPQFGS
SSSSNSKPRP TLRPAMNIPV PSADKAEKPP IGQDSRERFS GVFEAYTRRN GSGTGVQADQ
SSRPRTSENV LASKDTQNQE RPNSLSRNLS SSRKAIAGSS VRATSSADFT ENRLSRLIPN
NDRSSTTLRT QFAPSSSSVA TKAAPTRAAR DITLQSLELL SIGNSKRK
