P2C23_ARATH
ID P2C23_ARATH Reviewed; 654 AA.
AC Q9ZV25;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable protein phosphatase 2C 23;
DE Short=AtPP2C23;
DE EC=3.1.3.16;
DE AltName: Full=Protein POLTERGEIST-LIKE 4;
DE AltName: Full=Protein phosphatase 2C PLL4;
DE Short=PP2C PLL4;
GN Name=PLL4; OrderedLocusNames=At2g28890; ORFNames=F8N16.18;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16112663; DOI=10.1016/j.ydbio.2005.06.020;
RA Song S.-K., Clark S.E.;
RT "POL and related phosphatases are dosage-sensitive regulators of meristem
RT and organ development in Arabidopsis.";
RL Dev. Biol. 285:272-284(2005).
RN [5]
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 -!- FUNCTION: Involved in leaf development regulation.
CC {ECO:0000269|PubMed:16112663}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems, young
CC inflorescences, flowers and siliques. {ECO:0000269|PubMed:16112663}.
CC -!- DOMAIN: The conserved PP2C phosphatase domain (244-643) is interrupted
CC by an insertion of approximately 100 amino acids.
CC -!- DISRUPTION PHENOTYPE: Plants show abnormal leaves altered in shape and
CC curling. {ECO:0000269|PubMed:16112663}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC005727; AAC79593.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08185.1; -; Genomic_DNA.
DR EMBL; AY065299; AAL38775.1; -; mRNA.
DR EMBL; AY096450; AAM20090.1; -; mRNA.
DR PIR; B84690; B84690.
DR RefSeq; NP_180455.1; NM_128448.4.
DR AlphaFoldDB; Q9ZV25; -.
DR SMR; Q9ZV25; -.
DR STRING; 3702.AT2G28890.1; -.
DR iPTMnet; Q9ZV25; -.
DR PaxDb; Q9ZV25; -.
DR PRIDE; Q9ZV25; -.
DR ProteomicsDB; 248706; -.
DR EnsemblPlants; AT2G28890.1; AT2G28890.1; AT2G28890.
DR GeneID; 817438; -.
DR Gramene; AT2G28890.1; AT2G28890.1; AT2G28890.
DR KEGG; ath:AT2G28890; -.
DR Araport; AT2G28890; -.
DR TAIR; locus:2053265; AT2G28890.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; Q9ZV25; -.
DR OMA; EDNQRRW; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9ZV25; -.
DR PRO; PR:Q9ZV25; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV25; baseline and differential.
DR Genevisible; Q9ZV25; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..654
FT /note="Probable protein phosphatase 2C 23"
FT /id="PRO_0000301262"
FT DOMAIN 243..645
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 11..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RWN7"
SQ SEQUENCE 654 AA; 72482 MW; 6EEE6628C5AA060A CRC64;
MGNGIGKLSK CLTGGAGRNK KPELSILEPD PLDEGLGHSF CYVRPDPTRV SSSKVHSEEE
TTTFRTISGA SVSANTATPL STSLYDPYGH IDRAAAFEST TSFSSIPLQP IPRSSGPIVP
GSGPLERGFL SGPIERGFMS GPLDGSSGPI DGKTGSDQFQ RSFSHGLANL RVGSRKGSLV
RVLRRAISKT ITRGQNSIVA PIKPVKEPDW VFGSDKTRIH QIENNLTVNS LNFSSEGSLL
DDDVSLESQN LQWAQGKAGE DRVHVVVSEE HGWLFVGIYD GFNGPDAPDY LLSHLYPAVH
RELKGLLWDD PKTDAKSSDE ADVENRDSSS EKKSKNWEES QRRWRCEWDR DLDRLLKDRS
NGLDLDPDPN SSDVLKALSQ ALRKTEEAYL ENADMMLDEN PELALMGSCV LVMLMKGEDV
YLMNVGDSRA VLGQKAESDY WIGKIKQDLE RINEETMNDF DGCGDGEGAS LVPTLSAFQL
TVDHSTNVEE EVNRIRKEHP DDASAVSNER VKGSLKVTRA FGAGFLKQPK WNNALLEMFQ
IDYKGTSPYI NCLPSLYHHR LGSKDQFLIL SSDGLYQYFT NEEAVSEVEL FITLQPEGDP
AQHLVQELLF RAAKKAGMDF HELLEIPQGE RRRYHDDVSI VVISLEGRMW KSCV
