ID   P2C74_ARATH             Reviewed;         448 AA.
AC   Q9FG61; Q8W4Q9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=Probable protein phosphatase 2C 74;
DE            Short=AtPP2C74;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=At5g36250; ORFNames=T30G6.11;
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [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).
RN   [6]
RP   INTERACTION WITH KIN10, TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF GLY-2.
RX   PubMed=22449965; DOI=10.1016/j.febslet.2012.02.019;
RA   Tsugama D., Liu S., Takano T.;
RT   "A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts
RT   with SnRK1 in Arabidopsis.";
RL   FEBS Lett. 586:693-698(2012).
CC   -!- FUNCTION: Acts as a protein phosphatase. {ECO:0000269|PubMed:19021904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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   -!- SUBUNIT: Interacts with KIN10. {ECO:0000269|PubMed:19021904}.
CC   -!- INTERACTION:
CC       Q9FG61; B9DFC1: At3g01090; NbExp=2; IntAct=EBI-4437407, EBI-7801898;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19021904}.
CC   -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC       {ECO:0000269|PubMed:19021904}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AB026661; BAB09365.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94062.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7054145.1; -; Genomic_DNA.
DR   EMBL; AY061752; AAL31255.1; -; mRNA.
DR   EMBL; AY113035; AAM47343.1; -; mRNA.
DR   AlphaFoldDB; Q9FG61; -.
DR   SMR; Q9FG61; -.
DR   BioGRID; 18873; 1.
DR   FunCoup; Q9FG61; 540.
DR   IntAct; Q9FG61; 4.
DR   MINT; Q9FG61; -.
DR   STRING; 3702.Q9FG61; -.
DR   iPTMnet; Q9FG61; -.
DR   PaxDb; 3702-Q9FG61; -.
DR   ProteomicsDB; 250917; -.
DR   GeneID; 833622; -.
DR   KEGG; ath:AT5G36250; -.
DR   Araport; AT5G36250; -.
DR   TAIR; AT5G36250; PP2C74.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_6_0_1; -.
DR   InParanoid; Q9FG61; -.
DR   OMA; TYESAMS; -.
DR   OrthoDB; 1065853at2759; -.
DR   PhylomeDB; Q9FG61; -.
DR   PRO; PR:Q9FG61; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FG61; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; ISM:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:TAIR.
DR   GO; GO:1902531; P:regulation of intracellular signal transduction; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   FunFam; 3.60.40.10:FF:000024; probable protein phosphatase 2C 33; 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   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Lipoprotein; Magnesium; Manganese; Membrane;
KW   Metal-binding; Myristate; Protein phosphatase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..448
FT                   /note="Probable protein phosphatase 2C 74"
FT                   /id="PRO_0000367994"
FT   DOMAIN          67..384
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..37
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..426
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         2
FT                   /note="G->A: Abolishes cell membrane localization."
FT                   /evidence="ECO:0000269|PubMed:19021904"
FT   CONFLICT        57
FT                   /note="G -> E (in Ref. 4; AAM47343/AAL31255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  49314 MW;  F60D6EA773B718C9 CRC64;
     MGSCLSSSGG GGSRRSLHGS PHVPGPGRRK RPPKRRPGSC SSSFDNTEEP LLHRIPGRMF
     LNGSTDTVSL FSQQGKKGPN QDAMIVWENF GSMEDTVFCG VFDGHGPYGH IVAKRVRDLL
     PLKLGSHLES YVSPEEVLKE ISLNTDDRKI SEDLVHISAN GESRVYNKDY VKDQDMIQML
     IGSIVKAYRF MDKELKMQVD VDCFCSGTTA VTMVKQGQHL VIGNIGDSRA VLGVRNKDNK
     LVPFQLTEDL KPDVPAEAER IKRCRGRIFA LRDEPGVARL WLPNHNSPGL AMARAFGDFC
     LKDFGLISVP DVSYRRLTEK DEFVVLATDG IWDALTNEEV VKIVAKAPTR SSAGRALVEA
     AVRNWRWKFP TSKVDDCAVV CLFLDSEPNR LSTASFSKEK HINNGVTEPE PDTASSSTPD
     SGTGSPELNG VNRIDTLVNL PVYVPTKE
//