P2C41_ARATH
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 03-AUG-2022, entry version 131.
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.AT3G16800.2; -.
DR PaxDb; Q9LRZ4; -.
DR PRIDE; Q9LRZ4; -.
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; locus:2086755; AT3G16800.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_6_0_1; -.
DR InParanoid; Q9LRZ4; -.
DR OMA; SMMKNSK; -.
DR PhylomeDB; Q9LRZ4; -.
DR PRO; PR:Q9LRZ4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRZ4; baseline and differential.
DR Genevisible; Q9LRZ4; AT.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:TAIR.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
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 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
