P2C74_ARATH
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 03-AUG-2022, entry version 125.
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 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).
RN [5]
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=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 -!- 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; AY061752; AAL31255.1; -; mRNA.
DR EMBL; AY113035; AAM47343.1; -; mRNA.
DR RefSeq; NP_198474.1; NM_123016.2.
DR AlphaFoldDB; Q9FG61; -.
DR SMR; Q9FG61; -.
DR BioGRID; 18873; 1.
DR IntAct; Q9FG61; 4.
DR MINT; Q9FG61; -.
DR STRING; 3702.AT5G36250.1; -.
DR iPTMnet; Q9FG61; -.
DR PaxDb; Q9FG61; -.
DR PRIDE; Q9FG61; -.
DR ProteomicsDB; 250917; -.
DR EnsemblPlants; AT5G36250.1; AT5G36250.1; AT5G36250.
DR GeneID; 833622; -.
DR Gramene; AT5G36250.1; AT5G36250.1; AT5G36250.
DR KEGG; ath:AT5G36250; -.
DR Araport; AT5G36250; -.
DR TAIR; locus:2183612; AT5G36250.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_6_0_1; -.
DR InParanoid; Q9FG61; -.
DR OMA; YMAVEMS; -.
DR PhylomeDB; Q9FG61; -.
DR PRO; PR:Q9FG61; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG61; baseline and differential.
DR Genevisible; Q9FG61; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IDA: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 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 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. 3; 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
