ID   P2C04_ARATH             Reviewed;         662 AA.
AC   Q9LQN6; Q8LFF0; Q9ASX4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Probable protein phosphatase 2C 4;
DE            Short=AtPP2C04;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein POLTERGEIST-LIKE 5;
DE   AltName: Full=Protein phosphatase 2C PLL5;
DE            Short=PP2C PLL5;
GN   Name=PLL5; OrderedLocusNames=At1g07630; ORFNames=F24B9.25, F24B9.31;
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=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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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 (250-651) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK32783.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAM91433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC007583; AAF75095.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28151.1; -; Genomic_DNA.
DR   EMBL; AF361615; AAK32783.1; ALT_FRAME; mRNA.
DR   EMBL; AY133603; AAM91433.1; ALT_FRAME; mRNA.
DR   EMBL; AY084887; AAM61450.1; -; mRNA.
DR   PIR; G86210; G86210.
DR   RefSeq; NP_563791.1; NM_100636.3.
DR   AlphaFoldDB; Q9LQN6; -.
DR   SMR; Q9LQN6; -.
DR   STRING; 3702.Q9LQN6; -.
DR   iPTMnet; Q9LQN6; -.
DR   PaxDb; 3702-AT1G07630-1; -.
DR   ProteomicsDB; 248699; -.
DR   EnsemblPlants; AT1G07630.1; AT1G07630.1; AT1G07630.
DR   GeneID; 837276; -.
DR   Gramene; AT1G07630.1; AT1G07630.1; AT1G07630.
DR   KEGG; ath:AT1G07630; -.
DR   Araport; AT1G07630; -.
DR   TAIR; AT1G07630; PLL5.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_12_1_1; -.
DR   InParanoid; Q9LQN6; -.
DR   OMA; CEWEREK; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; Q9LQN6; -.
DR   PRO; PR:Q9LQN6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQN6; baseline and differential.
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   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF228; PROTEIN PHOSPHATASE 2C 4-RELATED; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q9LQN6; AT.
PE   2: Evidence at transcript level;
KW   Developmental protein; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..662
FT                   /note="Probable protein phosphatase 2C 4"
FT                   /id="PRO_0000301263"
FT   DOMAIN          249..653
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         644
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RWN7"
FT   CONFLICT        368
FT                   /note="S -> G (in Ref. 4; AAM61450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  74274 MW;  B1A3670D06B1B94E CRC64;
     MGNGVTKLSI CFTGGGGERL RPKDISVLLP DPLDEGLGHS FCYVRPDPTL ISSSKVHSEE
     DTTTTTFRTI SGASVSANTA TPLSTSLYDP YGHIDRAAAF ESTTSFSSIP LQPIPKSSGP
     IVLGSGPIER GFLSGPIERG FMSGPLDRVG LFSGPLDKPN SDHHHQFQRS FSHGLALRVG
     SRKRSLVRIL RRAISKTMSR GQNSIVAPIK SVKDSDNWGI RSEKSRNLHN ENLTVNSLNF
     SSEVSLDDDV SLENQNLQWA QGKAGEDRVH VVVSEEHGWL FVGIYDGFNG PDAPDYLLSH
     LYPVVHRELK GLLWDDSNVE SKSQDLERSN GDESCSNQEK DETCERWWRC EWDRESQDLD
     RRLKEQISRR SGSDRLTNHS EVLEALSQAL RKTEEAYLDT ADKMLDENPE LALMGSCVLV
     MLMKGEDIYV MNVGDSRAVL GQKSEPDYWL AKIRQDLERI NEETMMNDLE GCEGDQSSLV
     PNLSAFQLTV DHSTNIEEEV ERIRNEHPDD VTAVTNERVK GSLKVTRAFG AGFLKQPKWN
     NALLEMFQID YVGKSPYINC LPSLYHHRLG SKDRFLILSS DGLYQYFTNE EAVSEVELFI
     TLQPEGDPAQ HLVQELLFRA AKKAGMDFHE LLEIPQGERR RYHDDVSIVV ISLEGRMWKS
     CV
//