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CIPKJ_ARATH
ID   CIPKJ_ARATH             Reviewed;         483 AA.
AC   Q9FJ55;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=CBL-interacting serine/threonine-protein kinase 19;
DE            EC=2.7.11.1;
DE   AltName: Full=SNF1-related kinase 3.5;
DE   AltName: Full=SOS2-like protein kinase PKS21;
GN   Name=CIPK19; Synonyms=PKS21, SnRK3.5; OrderedLocusNames=At5g45810;
GN   ORFNames=K15I22.1;
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].
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=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;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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).
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   -!- INTERACTION:
CC       Q9FJ55; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-16967606, EBI-25512239;
CC       Q9FJ55; Q38845: PP2AA1; NbExp=3; IntAct=EBI-16967606, EBI-1645478;
CC       Q9FJ55; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-16967606, EBI-15192297;
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; AY030303; AAK50347.1; -; mRNA.
DR   EMBL; AB016870; BAB09309.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95302.1; -; Genomic_DNA.
DR   EMBL; DQ447041; ABE66223.1; -; mRNA.
DR   RefSeq; NP_199393.1; NM_123949.2.
DR   AlphaFoldDB; Q9FJ55; -.
DR   SMR; Q9FJ55; -.
DR   BioGRID; 19870; 4.
DR   IntAct; Q9FJ55; 4.
DR   STRING; 3702.AT5G45810.1; -.
DR   PaxDb; Q9FJ55; -.
DR   PRIDE; Q9FJ55; -.
DR   ProteomicsDB; 246861; -.
DR   EnsemblPlants; AT5G45810.1; AT5G45810.1; AT5G45810.
DR   GeneID; 834621; -.
DR   Gramene; AT5G45810.1; AT5G45810.1; AT5G45810.
DR   KEGG; ath:AT5G45810; -.
DR   Araport; AT5G45810; -.
DR   TAIR; locus:2152370; AT5G45810.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q9FJ55; -.
DR   OMA; MEYDEFC; -.
DR   OrthoDB; 1127668at2759; -.
DR   PhylomeDB; Q9FJ55; -.
DR   PRO; PR:Q9FJ55; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJ55; baseline and differential.
DR   Genevisible; Q9FJ55; 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: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..483
FT                   /note="CBL-interacting serine/threonine-protein kinase 19"
FT                   /id="PRO_0000337220"
FT   DOMAIN          28..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          340..364
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          168..197
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          313..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..396
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   REGION          459..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         34..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93V58"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q38997"
SQ   SEQUENCE   483 AA;  54616 MW;  2CF0E948F2A07BF9 CRC64;
     MADLLRKVKS IKKKQDQSNH QALILGKYEM GRLLGHGTFA KVYLARNAQS GESVAIKVID
     KEKVLKSGLI AHIKREISIL RRVRHPNIVQ LFEVMATKSK IYFVMEYVKG GELFNKVAKG
     RLKEEMARKY FQQLISAVSF CHFRGVYHRD LKPENLLLDE NGNLKVSDFG LSAVSDQIRQ
     DGLFHTFCGT PAYVAPEVLA RKGYDGAKVD IWSCGVILFV LMAGFLPFHD RNVMAMYKKI
     YRGDFRCPRW FPVEINRLLI RMLETKPERR FTMPDIMETS WFKKGFKHIK FYVEDDHQLC
     NVADDDEIES IESVSGRSST VSEPEDFESF DGRRRGGSMP RPASLNAFDL ISFSPGFDLS
     GLFEDDGEGS RFVSGAPVGQ IISKLEEIAR IVSFTVRKKD CKVSLEGSRE GSMKGPLSIA
     AEIFELTPAL VVVEVKKKGG DKMEYDEFCN KELKPKLQNL SSENGQRVSG SRSLPSFLLS
     DTD
 
 
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