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CIPKG_ARATH
ID   CIPKG_ARATH             Reviewed;         469 AA.
AC   Q9SEZ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=CBL-interacting serine/threonine-protein kinase 16;
DE            EC=2.7.11.1;
DE   AltName: Full=SNF1-related kinase 3.18;
DE   AltName: Full=SOS2-like protein kinase PKS15;
GN   Name=CIPK16; Synonyms=PKS15, SnRK3.18; OrderedLocusNames=At2g25090;
GN   ORFNames=F13D4.161;
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 (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   FUNCTION, AND INTERACTION WITH AKT1; CBL1; CBL2; CBL3 AND CBL9.
RX   PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA   Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA   Buchanan B.B., Luan S.;
RT   "A protein phosphorylation/dephosphorylation network regulates a plant
RT   potassium channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
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. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by
CC       phosphorylation the K(+) conductance and uptake of AKT1.
CC       {ECO:0000269|PubMed:17898163}.
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: Part of a K(+)-channel calcium-sensing kinase/phosphatase
CC       complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a
CC       kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a
CC       K(+)-channel (AKT1). Interacts with AKT1, CBL1, CBL2, CBL3 and CBL9.
CC       {ECO:0000269|PubMed:17898163}.
CC   -!- INTERACTION:
CC       Q9SEZ7; Q17TI5: BRX; NbExp=3; IntAct=EBI-1573415, EBI-4426649;
CC       Q9SEZ7; Q9LTB8: CBL9; NbExp=7; IntAct=EBI-1573415, EBI-637381;
CC       Q9SEZ7; O22179: MYB70; NbExp=4; IntAct=EBI-1573415, EBI-1238013;
CC       Q9SEZ7; O23160: MYB73; NbExp=3; IntAct=EBI-1573415, EBI-25506855;
CC       Q9SEZ7; Q38845: PP2AA1; NbExp=3; IntAct=EBI-1573415, EBI-1645478;
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}.
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DR   EMBL; AY030304; AAK50348.1; -; mRNA.
DR   EMBL; CP002685; AEC07656.1; -; Genomic_DNA.
DR   EMBL; BT029241; ABJ98573.1; -; mRNA.
DR   PIR; B84644; B84644.
DR   RefSeq; NP_180081.1; NM_128066.4.
DR   AlphaFoldDB; Q9SEZ7; -.
DR   SMR; Q9SEZ7; -.
DR   BioGRID; 2399; 15.
DR   DIP; DIP-40199N; -.
DR   IntAct; Q9SEZ7; 9.
DR   STRING; 3702.AT2G25090.1; -.
DR   PaxDb; Q9SEZ7; -.
DR   PRIDE; Q9SEZ7; -.
DR   EnsemblPlants; AT2G25090.1; AT2G25090.1; AT2G25090.
DR   GeneID; 817047; -.
DR   Gramene; AT2G25090.1; AT2G25090.1; AT2G25090.
DR   KEGG; ath:AT2G25090; -.
DR   Araport; AT2G25090; -.
DR   TAIR; locus:2040219; AT2G25090.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q9SEZ7; -.
DR   OMA; YLFCEDD; -.
DR   OrthoDB; 1127668at2759; -.
DR   PhylomeDB; Q9SEZ7; -.
DR   PRO; PR:Q9SEZ7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SEZ7; baseline and differential.
DR   Genevisible; Q9SEZ7; 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:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; IMP:TAIR.
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..469
FT                   /note="CBL-interacting serine/threonine-protein kinase 16"
FT                   /id="PRO_0000337217"
FT   DOMAIN          15..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          317..342
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          157..193
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          290..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..376
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   REGION          447..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         21..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93V58"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q38997"
SQ   SEQUENCE   469 AA;  53551 MW;  460E17225D6A7A7A CRC64;
     MEESNRSSTV LFDKYNIGRL LGTGNFAKVY HGTEISTGDD VAIKVIKKDH VFKRRGMMEQ
     IEREIAVMRL LRHPNVVELR EVMATKKKIF FVMEYVNGGE LFEMIDRDGK LPEDLARKYF
     QQLISAVDFC HSRGVFHRDI KPENLLLDGE GDLKVTDFGL SALMMPEGLG GRRGSSDDLL
     HTRCGTPAYV APEVLRNKGY DGAMADIWSC GIVLYALLAG FLPFIDENVM TLYTKIFKAE
     CEFPPWFSLE SKELLSRLLV PDPEQRISMS EIKMIPWFRK NFTPSVAFSI DETIPSPPEP
     PTKKKKKDLN EKEDDGASPR SFNAFQFITS MSSGFDLSNL FEIKRKPKRM FTSKFPAKSV
     KERLETAARE MDMRVKHVKD CKMKLQRRTE GRKGRLSVTA EVFEVAPEVS VVEFCKTSGD
     TLEYYLFCED DVRPALKDIV WSWQGDDDED DVTTNDNVDT NDNKINNVS
 
 
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