位置:首页 > 蛋白库 > CIPKK_ARATH
CIPKK_ARATH
ID   CIPKK_ARATH             Reviewed;         439 AA.
AC   Q9FJ54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=CBL-interacting serine/threonine-protein kinase 20;
DE            EC=2.7.11.1;
DE   AltName: Full=SNF1-related kinase 3.6;
DE   AltName: Full=SOS2-like protein kinase PKS18;
GN   Name=CIPK20; Synonyms=PKS18, SnRK3.6; OrderedLocusNames=At5g45820;
GN   ORFNames=K15I22.2;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
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   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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, MUTAGENESIS OF THR-170, AUTOPHOSPHORYLATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12198122; DOI=10.1074/jbc.m205504200;
RA   Gong D., Zhang C., Chen X., Gong Z., Zhu J.-K.;
RT   "Constitutive activation and transgenic evaluation of the function of an
RT   arabidopsis PKS protein kinase.";
RL   J. Biol. Chem. 277:42088-42096(2002).
RN   [7]
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).
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). Required for the abscisic acid-mediated (ABA)
CC       signaling pathway involved in seed germination and growth elongation
CC       inhibition. {ECO:0000250, ECO:0000269|PubMed:12198122}.
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   -!- INTERACTION:
CC       Q9FJ54; Q9LTB8: CBL9; NbExp=5; IntAct=EBI-25514480, EBI-637381;
CC   -!- TISSUE SPECIFICITY: Confined to mature leaves.
CC       {ECO:0000269|PubMed:12198122}.
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   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {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; AY035225; AAK61493.1; -; mRNA.
DR   EMBL; AB016870; BAB09310.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95303.1; -; Genomic_DNA.
DR   EMBL; AK221510; BAD94760.1; -; mRNA.
DR   EMBL; BT028970; ABI54345.1; -; mRNA.
DR   RefSeq; NP_199394.1; NM_123950.4.
DR   AlphaFoldDB; Q9FJ54; -.
DR   SMR; Q9FJ54; -.
DR   BioGRID; 19871; 3.
DR   IntAct; Q9FJ54; 1.
DR   STRING; 3702.AT5G45820.1; -.
DR   PaxDb; Q9FJ54; -.
DR   PRIDE; Q9FJ54; -.
DR   ProteomicsDB; 246518; -.
DR   EnsemblPlants; AT5G45820.1; AT5G45820.1; AT5G45820.
DR   GeneID; 834622; -.
DR   Gramene; AT5G45820.1; AT5G45820.1; AT5G45820.
DR   KEGG; ath:AT5G45820; -.
DR   Araport; AT5G45820; -.
DR   TAIR; locus:2152380; AT5G45820.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q9FJ54; -.
DR   OMA; GSINTKH; -.
DR   OrthoDB; 1127668at2759; -.
DR   PhylomeDB; Q9FJ54; -.
DR   PRO; PR:Q9FJ54; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJ54; baseline and differential.
DR   Genevisible; Q9FJ54; 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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0007165; P:signal transduction; 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..439
FT                   /note="CBL-interacting serine/threonine-protein kinase 20"
FT                   /id="PRO_0000337221"
FT   DOMAIN          12..266
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          297..322
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          152..181
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          326..356
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         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         41
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"
FT   MUTAGEN         170
FT                   /note="T->D: Strongly enhanced kinase activity, and higher
FT                   autophosphorylation, with an optimal pH of 7.5."
FT                   /evidence="ECO:0000269|PubMed:12198122"
FT   MUTAGEN         303..323
FT                   /note="Missing: Enhanced kinase activity, and higher
FT                   autophosphorylation."
SQ   SEQUENCE   439 AA;  50168 MW;  AE9FB6C013192D20 CRC64;
     MDKNGIVLMR KYELGRLLGQ GTFAKVYHAR NIKTGESVAI KVIDKQKVAK VGLIDQIKRE
     ISVMRLVRHP HVVFLHEVMA SKTKIYFAME YVKGGELFDK VSKGKLKENI ARKYFQQLIG
     AIDYCHSRGV YHRDLKPENL LLDENGDLKI SDFGLSALRE SKQQDGLLHT TCGTPAYVAP
     EVIGKKGYDG AKADVWSCGV VLYVLLAGFL PFHEQNLVEM YRKITKGEFK CPNWFPPEVK
     KLLSRILDPN PNSRIKIEKI MENSWFQKGF KKIETPKSPE SHQIDSLISD VHAAFSVKPM
     SYNAFDLISS LSQGFDLSGL FEKEERSESK FTTKKDAKEI VSKFEEIATS SERFNLTKSD
     VGVKMEDKRE GRKGHLAIDV EIFEVTNSFH MVEFKKSGGD TMEYKQFCDR ELRPSLKDIV
     WKWQGNNNNS NNEKIEVIH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024