CIPKH_ARATH
ID CIPKH_ARATH Reviewed; 432 AA.
AC Q94C40; Q9LNH7; Q9SX61;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=CBL-interacting serine/threonine-protein kinase 17;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase 3.21;
DE AltName: Full=SOS2-like protein kinase PKS20;
GN Name=CIPK17; Synonyms=PKS20, SnRK3.21; OrderedLocusNames=At1g48260;
GN ORFNames=F11A17.18, F21D18.2;
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].
RA Weinl S., Albrecht V., Kudla J.;
RT "Molecular characterization of the CIPK gene family from Arabidopsis
RT thaliana.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP INTERACTION WITH CBL1.
RX PubMed=14730064; DOI=10.1104/pp.103.033068;
RA Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT "Calcium sensors and their interacting protein kinases: genomics of the
RT Arabidopsis and rice CBL-CIPK signaling networks.";
RL Plant Physiol. 134:43-58(2004).
CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC protein lead to the activation of the kinase in a calcium-dependent
CC manner (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with CBL1. {ECO:0000269|PubMed:14730064}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation/activation by upstream protein kinases. The PPI motif
CC mediates the interaction with the ABI (abscisic acid-insensitive)
CC phosphatases (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49770.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79514.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY036958; AAK64513.1; -; mRNA.
DR EMBL; AC007932; AAD49770.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC023673; AAF79514.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32269.1; -; Genomic_DNA.
DR EMBL; BT029240; ABJ98572.1; -; mRNA.
DR PIR; E96522; E96522.
DR RefSeq; NP_175260.1; NM_103723.4.
DR AlphaFoldDB; Q94C40; -.
DR SMR; Q94C40; -.
DR BioGRID; 26471; 6.
DR IntAct; Q94C40; 4.
DR STRING; 3702.AT1G48260.1; -.
DR PaxDb; Q94C40; -.
DR PRIDE; Q94C40; -.
DR EnsemblPlants; AT1G48260.1; AT1G48260.1; AT1G48260.
DR GeneID; 841246; -.
DR Gramene; AT1G48260.1; AT1G48260.1; AT1G48260.
DR KEGG; ath:AT1G48260; -.
DR Araport; AT1G48260; -.
DR TAIR; locus:2007685; AT1G48260.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_0_1; -.
DR InParanoid; Q94C40; -.
DR OMA; GAQNMIK; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q94C40; -.
DR PRO; PR:Q94C40; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94C40; baseline and differential.
DR Genevisible; Q94C40; AT.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018451; NAF/FISL_domain.
DR InterPro; IPR004041; NAF_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03822; NAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50816; NAF; 1.
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 ATP-binding; Kinase; Manganese; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..432
FT /note="CBL-interacting serine/threonine-protein kinase 17"
FT /id="PRO_0000337218"
FT DOMAIN 11..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 301..325
FT /note="NAF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT REGION 152..181
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 331..360
FT /note="PPI"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 432 AA; 48663 MW; E1C2521D0CCAD53E CRC64;
MVIKGMRVGK YELGRTLGEG NSAKVKFAID TLTGESFAIK IIEKSCITRL NVSFQIKREI
RTLKVLKHPN IVRLHEVLAS KTKIYMVLEC VTGGDLFDRI VSKGKLSETQ GRKMFQQLID
GVSYCHNKGV FHRDLKLENV LLDAKGHIKI TDFGLSALSQ HYREDGLLHT TCGSPNYVAP
EVLANEGYDG AASDIWSCGV ILYVILTGCL PFDDANLAVI CRKIFKGDPP IPRWISLGAK
TMIKRMLDPN PVTRVTIAGI KAHDWFKHDY TPSNYDDDDD VYLIQEDVFM MKEYEEEKSP
DSPTIINAFQ LIGMSSFLDL SGFFETEKLS ERQIRFTSNS LAKDLLENIE TIFTEMGFCL
QKKHAKLKAI KEESTQKRQC GLSVTAEVFE ISPSLNVVEL RKSHGDSSLY KQLYERLLNE
LGSSSQVQEL LA
