P2C19_ARATH
ID P2C19_ARATH Reviewed; 1094 AA.
AC Q9SL76; B5KQ16; B5KQ17; Q0WLT6; Q9SL77;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein;
DE Includes:
DE RecName: Full=Probable protein phosphatase 2C 19;
DE Short=AtPP2C19;
DE EC=3.1.3.16;
DE Includes:
DE RecName: Full=Probable inactive cyclic nucleotide-dependent protein kinase At2g20050;
GN OrderedLocusNames=At2g20050/At2g20040; ORFNames=T2G17.15/T2G17.16;
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 Van Ingelgem C., Azmi A., Inze D., Van Onckelen H., Roef L.;
RT "Involvement of a putative cyclic nucleotide dependent hybrid phosphatase
RT 2C/protein kinase gene in stress responses in higher plants.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pascaud F., Corratge C., Thibaud J.-B., Lacombe B.;
RT "Plants have cyclic nucleotide dependent kinases.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-1090.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 743-1090.
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SL76-1; Sequence=Displayed;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PP2C family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. AGC Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24391.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20040 and At2g20050.; Evidence={ECO:0000305};
CC Sequence=AAD24392.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20040 and At2g20050.; Evidence={ECO:0000305};
CC Sequence=AAY27059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EU101468; ABU68673.1; -; mRNA.
DR EMBL; EU101469; ABU68674.1; -; mRNA.
DR EMBL; EU591510; ACF05481.1; -; mRNA.
DR EMBL; AC006081; AAD24391.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006081; AAD24392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06958.1; -; Genomic_DNA.
DR EMBL; AK230102; BAF01921.1; -; mRNA.
DR EMBL; BT022072; AAY27059.1; ALT_INIT; mRNA.
DR EMBL; BT023477; AAY57316.1; -; mRNA.
DR PIR; D84584; D84584.
DR RefSeq; NP_179595.5; NM_127563.6. [Q9SL76-1]
DR AlphaFoldDB; Q9SL76; -.
DR SMR; Q9SL76; -.
DR STRING; 3702.AT2G20050.1; -.
DR iPTMnet; Q9SL76; -.
DR PaxDb; Q9SL76; -.
DR PRIDE; Q9SL76; -.
DR ProteomicsDB; 248703; -. [Q9SL76-1]
DR EnsemblPlants; AT2G20050.1; AT2G20050.1; AT2G20050. [Q9SL76-1]
DR GeneID; 816524; -.
DR Gramene; AT2G20050.1; AT2G20050.1; AT2G20050. [Q9SL76-1]
DR KEGG; ath:AT2G20050; -.
DR Araport; AT2G20050; -.
DR TAIR; locus:2061673; AT2G20050.
DR eggNOG; KOG0616; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR eggNOG; KOG1113; Eukaryota.
DR InParanoid; Q9SL76; -.
DR OMA; NPSEACH; -.
DR OrthoDB; 1344250at2759; -.
DR PhylomeDB; Q9SL76; -.
DR PRO; PR:Q9SL76; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL76; baseline and differential.
DR Genevisible; Q9SL76; AT.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Hydrolase; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Protein phosphatase; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1094
FT /note="Protein phosphatase 2C and cyclic nucleotide-
FT binding/kinase domain-containing protein"
FT /id="PRO_0000367949"
FT DOMAIN 107..397
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 785..1038
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 491..616
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 617..758
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 791..799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 811
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1094 AA; 121389 MW; 89C6347D846297AC CRC64;
MGCAYSKTCI GQICATKENS IRQTHQQAPS RGGTRATAAA AAVEEDNPVF NFSSDAVDDV
DNDEIHQLGL SRDQEWGITR LSRVSSQFLP PDGSRVVKVP SCNYELRCSF LSQRGYYPDA
LDKANQDSFA IHTPFGSNSD DHFFGVFDGH GEFGAQCSQF VKRRLCENLL RHGRFRVDPA
EACNSAFLTT NSQLHADLVD DSMSGTTAIT VMVRGRTIYV ANAGDSRAVL AEKRDGDLVA
VDLSIDQTPF RPDELERVKL CGARVLTLDQ IEGLKNPDVQ CWGTEEDDDG DPPRLWVPNG
MYPGTAFTRS IGDSIAETIG VVANPEIAVV ELTPDNPFFV VASDGVFEFI SSQTVVDMVA
KHKDPRDACA AIVAESYRLW LQYETRTDDI TIIVVHIDGL KDDAPRQLSS TGTQLQPPIP
QVVELTGSES PSTFGWNSKN QRVRHDLSRA RIRAIENSLE NGHAWVPPSP AHRKTWEEEA
HIERVLRDHF LFRKLTDSQC QVLLDCMQRL EANPGDIVVK QGGEGDCFYV VGSGEFEVLA
TQDGKNGEVP RILQRYTAEK QSSFGELALM HNKPLQASVR AVDHGTLWAL KREDFRGILM
SEFSNLASLK LLRSVDLLSR LTILQLSHVA ESLSEACFSD GQTIVTKDQK LQGLYVIQKG
RVKISFCTEV LESQNVSSLT TGITNEYDNL EIGTEVSIEK HEGSYFGEWA LLGELKDSLS
VVAVGEVVCV VLTKENFESA VGPLTNISDD GPKTRHSSFE LSKESAKVTD TTALAKATLA
DLEWTTCLST TDCSEIGLVH LKDKENLLSL KRFSKQKVKK LGKEAQVLKE RNLMKNVIKP
SAIVPEILCT CVDQTFAAIL LNTTLACPIS SLLHSPLDES SVRFITGSLV SAIEDIHKNE
ILFRGSSPEL LMLDQSGYLQ IVDFRFAKKL SGERTFTICG NADYLAPEIV QGKGHGYAAD
WWALGVLIYY MLEGEMPFGS WRESELDTFQ KIAKGQLTFP RVLSSEAEDL ITKLLEVDEN
LRFGSQGGPE SIKKHPWFNG LKWEAISNRE FQVPQEIISR IHHHLENDNV LPLETSKSLD
TTEDQDAQNW LEEW
