ID   PP18_ARATH              Reviewed;         324 AA.
AC   O82734; Q8LAG7; Q94B49;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 3.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 8 {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE   AltName: Full=Type one protein phosphatase 8 {ECO:0000303|PubMed:17368080};
GN   Name=TOPP8 {ECO:0000303|PubMed:17368080};
GN   OrderedLocusNames=At5g27840 {ECO:0000312|Araport:AT5G27840};
GN   ORFNames=T1G16.170;
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 [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=9617814; DOI=10.1023/a:1005912413555;
RA   Lin Q., Li J., Smith R.D., Walker J.C.;
RT   "Molecular cloning and chromosomal mapping of type one serine/threonine
RT   protein phosphatases in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 37:471-481(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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] (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   [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=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   [7]
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O82734-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O82734-2; Sequence=VSP_009007;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, rosettes and flowers.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1, Met-2, Met-5 or Met-8 is the
CC       initiator. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM65377.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U80922; AAC39461.1; -; Genomic_DNA.
DR   EMBL; AC069556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93734.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93735.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69190.1; -; Genomic_DNA.
DR   EMBL; AY081492; AAM10054.1; -; mRNA.
DR   EMBL; AY042854; AAK68794.1; -; mRNA.
DR   EMBL; AY087823; AAM65377.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001330890.1; NM_001344042.1. [O82734-1]
DR   RefSeq; NP_568501.3; NM_122666.4. [O82734-1]
DR   RefSeq; NP_851085.1; NM_180754.4. [O82734-2]
DR   AlphaFoldDB; O82734; -.
DR   SMR; O82734; -.
DR   BioGRID; 18120; 6.
DR   IntAct; O82734; 2.
DR   MINT; O82734; -.
DR   STRING; 3702.O82734; -.
DR   PaxDb; 3702-AT5G27840-2; -.
DR   ProteomicsDB; 249152; -. [O82734-1]
DR   EnsemblPlants; AT5G27840.1; AT5G27840.1; AT5G27840. [O82734-2]
DR   EnsemblPlants; AT5G27840.2; AT5G27840.2; AT5G27840. [O82734-1]
DR   EnsemblPlants; AT5G27840.3; AT5G27840.3; AT5G27840. [O82734-1]
DR   GeneID; 832846; -.
DR   Gramene; AT5G27840.1; AT5G27840.1; AT5G27840. [O82734-2]
DR   Gramene; AT5G27840.2; AT5G27840.2; AT5G27840. [O82734-1]
DR   Gramene; AT5G27840.3; AT5G27840.3; AT5G27840. [O82734-1]
DR   KEGG; ath:AT5G27840; -.
DR   Araport; AT5G27840; -.
DR   TAIR; AT5G27840; TOPP8.
DR   eggNOG; KOG0374; Eukaryota.
DR   InParanoid; O82734; -.
DR   OMA; NERIFCC; -.
DR   PhylomeDB; O82734; -.
DR   PRO; PR:O82734; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O82734; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; 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:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
DR   GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR   GO; GO:0048768; P:root hair cell tip growth; IGI:TAIR.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
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   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF432; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 8; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   Genevisible; O82734; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW   Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..324
FT                   /note="Serine/threonine-protein phosphatase PP1 isozyme 8"
FT                   /id="PRO_0000058804"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         312..324
FT                   /note="DFHNRTLGYNLSA -> VPKMGKS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_009007"
FT   CONFLICT        256
FT                   /note="G -> E (in Ref. 1; AAC39461)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  36806 MW;  AD6ECB37F8FBBFE0 CRC64;
     MMTSMEGMVE KGVLDDIIRR LLEGKGGKQV QLSESEIRQL CFNARQIFLS QPNLLDLHAP
     IRICGDIHGQ YQDLLRLFEY GGYPPSANYL FLGDYVDRGK QSLETICLLL AYKIRYPSKI
     YLLRGNHEDA KINRIYGFYD ECKRRFNVRL WKVFTDCFNC LPVAALIDEK ILCMHGGLSP
     DLDNLNQIRE IQRPIEIPDS GLLCDLLWSD PDQKIEGWAD SDRGISCTFG ADKVAEFLDK
     NDLDLICRGH QVVEDGYEFF AKRRLVTIFS APNYGGEFDN AGALLSVDES LVCSFEIMKP
     APASSSHPLK KDFHNRTLGY NLSA
//