PPCK1_ARATH
ID PPCK1_ARATH Reviewed; 284 AA.
AC Q9SPK4; Q9FRS0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphoenolpyruvate carboxylase kinase 1;
DE Short=AtPPCK1;
DE EC=2.7.11.1;
GN Name=PPCK1; OrderedLocusNames=At1g08650; ORFNames=F22O13.13;
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], FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10571893; DOI=10.1046/j.1365-313x.1999.t01-1-00609.x;
RA Hartwell J., Gill A., Nimmo G.A., Wilkins M.B., Jenkins G.I., Nimmo H.G.;
RT "Phosphoenolpyruvate carboxylase kinase is a novel protein kinase regulated
RT at the level of expression.";
RL Plant J. 20:333-342(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT
RP AND CYCLOHEXIMIDE.
RC STRAIN=cv. Landsberg erecta;
RX DOI=10.1046/j.0016-8025.2001.00805.x;
RA Fontaine V., Hartwell J., Jenkins G.I., Nimmo H.G.;
RT "Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase
RT genes with different expression patterns.";
RL Plant Cell Environ. 25:115-122(2002).
RN [6]
RP INDUCTION BY CARBON; NITROGEN AND PHOSPHITE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18771573; DOI=10.1111/j.1365-3040.2008.01885.x;
RA Chen Z.H., Jenkins G.I., Nimmo H.G.;
RT "pH and carbon supply control the expression of phosphoenolpyruvate
RT carboxylase kinase genes in Arabidopsis thaliana.";
RL Plant Cell Environ. 31:1844-1850(2008).
RN [7]
RP INDUCTION BY PHOSPHATE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19228119; DOI=10.1042/bj20082397;
RA Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M.,
RA Knowles V.L., Plaxton W.C.;
RT "In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase
RT AtPPC1 in phosphate-starved Arabidopsis thaliana.";
RL Biochem. J. 420:57-65(2009).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19397910; DOI=10.1016/j.febslet.2009.04.030;
RA Meimoun P., Gousset-Dupont A., Lebouteiller B., Ambard-Bretteville F.,
RA Besin E., Lelarge C., Mauve C., Hodges M., Vidal J.;
RT "The impact of PEPC phosphorylation on growth and development of
RT Arabidopsis thaliana: molecular and physiological characterization of PEPC
RT kinase mutants.";
RL FEBS Lett. 583:1649-1652(2009).
CC -!- FUNCTION: Calcium-independent kinase involved in light-dependent
CC phosphoenolpyruvate carboxylase phosphorylation.
CC {ECO:0000269|PubMed:10571893, ECO:0000269|Ref.5}.
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 Evidence={ECO:0000269|Ref.5};
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; Evidence={ECO:0000269|Ref.5};
CC -!- ACTIVITY REGULATION: Constitutively active and not activated by
CC phosphorylation. {ECO:0000269|PubMed:10571893}.
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=Q9SPK4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, and to lower levels in
CC flowers and roots. Barely detectable in siliques, cauline leaves and
CC stems. {ECO:0000269|Ref.5}.
CC -!- INDUCTION: Up-regulated by light, cycloheximide, phosphate starvation,
CC carbon availability and high pH. Down-regulated by phosphate and
CC phosphite. Not under circadian control and not affected by nitrogen
CC supply. {ECO:0000269|PubMed:18771573, ECO:0000269|PubMed:19228119,
CC ECO:0000269|Ref.5}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and loss of light-induced
CC phosphoenolpyruvate carboxylase phosphorylation, but little or no
CC effect on the metabolic flux through the anaplerotic pathway.
CC {ECO:0000269|PubMed:19397910}.
CC -!- MISCELLANEOUS: Lacks the autoinhibitory region and EF hands found in
CC calcium-dependent protein kinases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF162660; AAF06968.1; -; mRNA.
DR EMBL; AC003981; AAF99758.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28326.1; -; Genomic_DNA.
DR EMBL; AY065297; AAL38773.1; -; mRNA.
DR EMBL; AY150461; AAN12902.1; -; mRNA.
DR PIR; T00718; T00718.
DR RefSeq; NP_172341.1; NM_100738.3. [Q9SPK4-1]
DR AlphaFoldDB; Q9SPK4; -.
DR SMR; Q9SPK4; -.
DR BioGRID; 22628; 4.
DR IntAct; Q9SPK4; 1.
DR STRING; 3702.AT1G08650.1; -.
DR PaxDb; Q9SPK4; -.
DR PRIDE; Q9SPK4; -.
DR ProteomicsDB; 249038; -. [Q9SPK4-1]
DR EnsemblPlants; AT1G08650.1; AT1G08650.1; AT1G08650. [Q9SPK4-1]
DR GeneID; 837387; -.
DR Gramene; AT1G08650.1; AT1G08650.1; AT1G08650. [Q9SPK4-1]
DR KEGG; ath:AT1G08650; -.
DR Araport; AT1G08650; -.
DR TAIR; locus:2025520; AT1G08650.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9SPK4; -.
DR OMA; DRECLEN; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9SPK4; -.
DR PRO; PR:Q9SPK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SPK4; baseline and differential.
DR Genevisible; Q9SPK4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0046898; P:response to cycloheximide; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Pyruvate;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..284
FT /note="Phosphoenolpyruvate carboxylase kinase 1"
FT /id="PRO_0000403718"
FT DOMAIN 15..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 140
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"
SQ SEQUENCE 284 AA; 31829 MW; F1CBEAB69983D859 CRC64;
MTCSQTLGNN NTNKYQICEE IGRGRFGTVS RVYAPATGDF FACKTIDKAS LSDDLDRACL
DNEPKLMALL SYHPNIVQIH DLIDTDSTLS IFMELVHPSV SIYDRLVSSG TFFEPQTASF
AKQILQALSH CHRYGVVHRD IKPENILVDL RNDTVKICDF GSGIWLGEGE TTEGVVGTPY
YVAPEVLMGY SYGEKVDLWS AGVVLYTMLA GTPPFYGETA EEIFEAVLRG NLRFPTKIFR
GVSSMAKDFL RKLICKDASR RFSAEQALRH PWIQRAGETE ERFI
