ID P2C76_ARATH Reviewed; 420 AA. AC Q94AT1; Q8VZD9; Q9FGM3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Probable protein phosphatase 2C 76; DE Short=AtPP2C76; DE EC=3.1.3.16; GN OrderedLocusNames=At5g53140; ORFNames=MFH8.8; 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; RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. 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 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 -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB08417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB025622; BAB08417.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002688; AED96312.1; -; Genomic_DNA. DR EMBL; CP002688; ANM68199.1; -; Genomic_DNA. DR EMBL; AY045819; AAK76493.1; -; mRNA. DR EMBL; AY065026; AAL57666.1; -; mRNA. DR EMBL; AY091360; AAM14299.1; -; mRNA. DR EMBL; AY133656; AAM91486.1; -; mRNA. DR RefSeq; NP_001329972.1; NM_001345034.1. DR RefSeq; NP_568786.1; NM_124693.4. DR AlphaFoldDB; Q94AT1; -. DR SMR; Q94AT1; -. DR BioGRID; 20640; 4. DR IntAct; Q94AT1; 2. DR MINT; Q94AT1; -. DR STRING; 3702.Q94AT1; -. DR iPTMnet; Q94AT1; -. DR MetOSite; Q94AT1; -. DR PaxDb; 3702-AT5G53140-1; -. DR ProteomicsDB; 250974; -. DR EnsemblPlants; AT5G53140.1; AT5G53140.1; AT5G53140. DR EnsemblPlants; AT5G53140.2; AT5G53140.2; AT5G53140. DR GeneID; 835395; -. DR Gramene; AT5G53140.1; AT5G53140.1; AT5G53140. DR Gramene; AT5G53140.2; AT5G53140.2; AT5G53140. DR KEGG; ath:AT5G53140; -. DR Araport; AT5G53140; -. DR TAIR; AT5G53140; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_0_6_1; -. DR InParanoid; Q94AT1; -. DR OMA; KHNPSCN; -. DR OrthoDB; 11028at2759; -. DR PhylomeDB; Q94AT1; -. DR PRO; PR:Q94AT1; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q94AT1; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0009536; C:plastid; 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 CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. 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:SF70; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q94AT1; AT. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..420 FT /note="Probable protein phosphatase 2C 76" FT /id="PRO_0000367996" FT DOMAIN 101..347 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 353..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 372..387 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..420 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 137 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 138 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 299 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 338 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 267 FT /note="F -> L (in Ref. 3; AAM91486/AAL57666)" FT /evidence="ECO:0000305" SQ SEQUENCE 420 AA; 45786 MW; C312D84D35159052 CRC64; MVCSSFIRSF IVQAGCRIGV LAQGRHQFIH IKKTLSVGFG FRTSVIGFRT TSGIGFRTSA KMMVDTSAGE KRISLVDMPP EKVDDGGYIG GGWKNDDGSL SCGYCSFRGK RSTMEDFYDI KASTIEGQAV CMFGIFDGHG GSRAAEYLKE HLFNNLMKHP QFLTDTKLAL NETYKQTDVA FLESEKDTYR DDGSTASAAV LVGNHLYVAN VGDSRTIVSK AGKAIALSDD HKPNRSDERK RIESAGGVIM WAGTWRVGGV LAMSRAFGNR MLKQFVVAEP EIQDLEIDHE AELLVLASDG LWDVVPNEDA VALAQSEEEP EAAARKLTDT AFSRGSADNI TCIVVKFRHD KTESPKIETN AMAESEPELN PTTELEPESN PSTALETESI PKAELESEPD AIPDPKPETE PETKGEKAGE //