PP13_ARATH
ID PP13_ARATH Reviewed; 322 AA.
AC P48483; Q9SH54;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 3 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE AltName: Full=Type one protein phosphatase 3 {ECO:0000303|PubMed:17368080};
GN Name=TOPP3 {ECO:0000303|PubMed:17368080};
GN OrderedLocusNames=At1g64040 {ECO:0000312|Araport:AT1G64040};
GN ORFNames=F22C12.20 {ECO:0000312|EMBL:AAF24566.1};
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 [MRNA].
RX PubMed=7678768; DOI=10.1007/bf00019946;
RA Smith R.D., Walker J.C.;
RT "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 21:307-316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [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=17368080; DOI=10.1016/j.tplants.2007.03.003;
RA Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
RT "Arabidopsis PPP family of serine/threonine phosphatases.";
RL Trends Plant Sci. 12:169-176(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19329567; DOI=10.1104/pp.109.135335;
RA Takemiya A., Ariyoshi C., Shimazaki K.;
RT "Identification and functional characterization of inhibitor-3, a
RT regulatory subunit of protein phosphatase 1 in plants.";
RL Plant Physiol. 150:144-156(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=21222654; DOI=10.1042/bj20101035;
RA Templeton G.W., Nimick M., Morrice N., Campbell D., Goudreault M.,
RA Gingras A.C., Takemiya A., Shimazaki K., Moorhead G.B.;
RT "Identification and characterization of AtI-2, an Arabidopsis homologue of
RT an ancient protein phosphatase 1 (PP1) regulatory subunit.";
RL Biochem. J. 435:73-83(2011).
CC -!- FUNCTION: Serine/threonine-protein phosphatase that possesses
CC phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
CC {ECO:0000269|PubMed:21222654}.
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 Evidence={ECO:0000269|PubMed:21222654};
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 Evidence={ECO:0000269|PubMed:21222654};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Phosphatase activity is strongly reduced by the
CC protein phosphatase inhibitor 2 (I-2). {ECO:0000269|PubMed:21222654}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm
CC {ECO:0000269|PubMed:19329567}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M93410; AAA32838.1; -; mRNA.
DR EMBL; AC007764; AAF24566.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34183.1; -; Genomic_DNA.
DR EMBL; AY081338; AAL91227.1; -; mRNA.
DR EMBL; AY128830; AAM91230.1; -; mRNA.
DR PIR; C96665; C96665.
DR PIR; S31087; S31087.
DR RefSeq; NP_176587.1; NM_105077.4.
DR AlphaFoldDB; P48483; -.
DR SMR; P48483; -.
DR BioGRID; 27929; 2.
DR STRING; 3702.AT1G64040.1; -.
DR iPTMnet; P48483; -.
DR PaxDb; P48483; -.
DR PRIDE; P48483; -.
DR ProteomicsDB; 249133; -.
DR EnsemblPlants; AT1G64040.1; AT1G64040.1; AT1G64040.
DR GeneID; 842708; -.
DR Gramene; AT1G64040.1; AT1G64040.1; AT1G64040.
DR KEGG; ath:AT1G64040; -.
DR Araport; AT1G64040; -.
DR TAIR; locus:2024507; AT1G64040.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P48483; -.
DR OMA; RYSVRVW; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P48483; -.
DR PRO; PR:P48483; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P48483; baseline and differential.
DR Genevisible; P48483; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISS: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; IDA:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:TAIR.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..322
FT /note="Serine/threonine-protein phosphatase PP1 isozyme 3"
FT /id="PRO_0000058799"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P48486"
SQ SEQUENCE 322 AA; 36215 MW; 644A70BB9F63215C CRC64;
MEDSVVDDVI KRLLGAKNGK TTKQVQLTEA EIKHLCSTAK QIFLTQPNLL ELEAPIKICG
DTHGQFSDLL RLFEYGGYPP AANYLFLGDY VDRGKQSVET ICLLLAYKIK YKENFFLLRG
NHECASINRI YGFYDECKKR YSVRVWKIFT DCFNCLPVAA LIDEKILCMH GGLSPELKHL
DEIRNIPRPA DIPDHGLLCD LLWSDPDKDI EGWGENDRGV SYTFGADKVE EFLQTHDLDL
ICRAHQVVED GYEFFANRQL VTIFSAPNYC GEFDNAGAMM SVDDSLTCSF QILKASEKKG
NFGFGKNAGR RGTPPRKGGG KG
