ID   P2C41_ARATH             Reviewed;         351 AA.
AC   Q9LRZ4; Q8LPG8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Probable protein phosphatase 2C 41;
DE            Short=AtPP2C41;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=At3g16800; ORFNames=K20I9.2;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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] (ISOFORM 2).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [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   -!- 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=2;
CC       Name=1;
CC         IsoId=Q9LRZ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LRZ4-2; Sequence=VSP_036767, VSP_036768, VSP_036769;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AB028608; BAA95773.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75866.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75867.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75868.2; -; Genomic_DNA.
DR   EMBL; AY099831; AAM20682.1; -; mRNA.
DR   EMBL; BT000321; AAN15640.1; -; mRNA.
DR   EMBL; AK317121; BAH19809.1; -; mRNA.
DR   EMBL; AY088376; AAM65915.1; -; mRNA.
DR   RefSeq; NP_001319572.1; NM_001338260.1. [Q9LRZ4-1]
DR   RefSeq; NP_188303.1; NM_112554.3. [Q9LRZ4-1]
DR   RefSeq; NP_850599.2; NM_180268.4. [Q9LRZ4-1]
DR   AlphaFoldDB; Q9LRZ4; -.
DR   SMR; Q9LRZ4; -.
DR   BioGRID; 6267; 1.
DR   IntAct; Q9LRZ4; 1.
DR   STRING; 3702.Q9LRZ4; -.
DR   PaxDb; 3702-AT3G16800-2; -.
DR   ProteomicsDB; 248711; -. [Q9LRZ4-1]
DR   EnsemblPlants; AT3G16800.1; AT3G16800.1; AT3G16800. [Q9LRZ4-1]
DR   EnsemblPlants; AT3G16800.2; AT3G16800.2; AT3G16800. [Q9LRZ4-1]
DR   EnsemblPlants; AT3G16800.3; AT3G16800.3; AT3G16800. [Q9LRZ4-1]
DR   GeneID; 820933; -.
DR   Gramene; AT3G16800.1; AT3G16800.1; AT3G16800. [Q9LRZ4-1]
DR   Gramene; AT3G16800.2; AT3G16800.2; AT3G16800. [Q9LRZ4-1]
DR   Gramene; AT3G16800.3; AT3G16800.3; AT3G16800. [Q9LRZ4-1]
DR   KEGG; ath:AT3G16800; -.
DR   Araport; AT3G16800; -.
DR   TAIR; AT3G16800; EGR3.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_6_0_1; -.
DR   InParanoid; Q9LRZ4; -.
DR   OMA; SMMKNSK; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; Q9LRZ4; -.
DR   PRO; PR:Q9LRZ4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRZ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0009819; P:drought recovery; IMP:TAIR.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR   GO; GO:0045926; P:negative regulation of growth; IMP:TAIR.
DR   GO; GO:0006470; P:protein dephosphorylation; 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; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF47; PROTEIN PHOSPHATASE 2C 41-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q9LRZ4; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Probable protein phosphatase 2C 41"
FT                   /id="PRO_0000367965"
FT   DOMAIN          62..348
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..95
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_036767"
FT   VAR_SEQ         295..315
FT                   /note="MWDVMTNNEAVEIVRGVKERR -> VIYQTYSAFKSKSRLINHIIV (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_036768"
FT   VAR_SEQ         316..351
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_036769"
SQ   SEQUENCE   351 AA;  38601 MW;  5161F2EA4314BFD6 CRC64;
     MVLLPAFLDG LARTVSTKKG KKLSEDEDGG REIAKSMIKD SKKNSTLLGT SGFVSSESSK
     RFTSICSNRG EKGINQDRAI VWEGFGCQED ITFCGMFDGH GPWGHVIAKR VKKSFPSSLL
     CQWQQTLASL SSSPECSSPF DLWKQACLKT FSIIDLDLKI SPSIDSYCSG CTALTAVLQG
     DHLVIANAGD SRAVIATTSD DGNGLVPVQL SVDFKPNIPE EAERIKQSDG RLFCLDDEPG
     VYRVGMPNGG SLGLAVSRAF GDYCLKDFGL VSEPEVTYRK ITDKDQFLIL ATDGMWDVMT
     NNEAVEIVRG VKERRKSAKR LVERAVTLWR RKRRSIAMDD ISVLCLFFRP S
//