ID   PPP5_SOLLC              Reviewed;         556 AA.
AC   Q84K11; Q8H1H4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Serine/threonine-protein phosphatase 5;
DE            EC=3.1.3.16;
DE   AltName: Full=LePP5;
GN   Name=PP5;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF
RP   GLY-411, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE
RP   PRODUCTS, AND ACTIVATION BY FATTY ACIDS.
RC   STRAIN=cv. GCR161, and cv. VFN8;
RX   PubMed=12972652; DOI=10.1104/pp.103.026617;
RA   de la Fuente van Bentem S., Vossen J.H., Vermeer J.E.M., de Vroomen M.J.,
RA   Gadella T.W.J. Jr., Haring M.A., Cornelissen B.J.C.;
RT   "The subcellular localization of plant protein phosphatase 5 isoforms is
RT   determined by alternative splicing.";
RL   Plant Physiol. 133:702-712(2003).
CC   -!- FUNCTION: Isoform 2 dephosphorylates phosphorylated phytochromes, with
CC       a preference toward Pfr forms, and enhances phytochrome-mediated
CC       photoresponses (By similarity). Can use para-nitrophenylphosphate
CC       (pNPP) and phosphorylated casein as substrate at pH 7.5 and 5.0.
CC       {ECO:0000250, ECO:0000269|PubMed:12972652}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by linoleic acid, linolenic acid, oleic
CC       acid, and arachidonic acid (AA).
CC   -!- SUBUNIT: Interacts with PHYA and PHYB, mostly when they are
CC       phosphorylated and in Pfr forms. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane;
CC       Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus, nucleoplasm.
CC       Nucleus speckle. Note=Cytoplasmic in darkness, but translocated to the
CC       nucleus upon illumination, when associated with phytochromes into
CC       speckles. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=62 kDa isoform;
CC         IsoId=Q84K11-1; Sequence=Displayed;
CC       Name=2; Synonyms=55 kDa isoform;
CC         IsoId=Q84K11-2; Sequence=VSP_029090;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers, and
CC       fruits. {ECO:0000269|PubMed:12972652}.
CC   -!- DOMAIN: TPR repeats are required for the binding with phytochromes.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Partial isoform 2 (148-485) lacking TPR
CC       repeats exhibits enhanced activity at pH 7.5 but not at pH 5.0 with
CC       phosphocasein as substrate. This partial protein is in addition
CC       inhibited by okadaic acid. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY150041; AAN64317.1; -; mRNA.
DR   EMBL; AY182777; AAO26213.1; -; mRNA.
DR   EMBL; AY182778; AAO26214.1; -; Genomic_DNA.
DR   EMBL; AY182778; AAO26215.1; -; Genomic_DNA.
DR   RefSeq; NP_001234232.2; NM_001247303.2.
DR   AlphaFoldDB; Q84K11; -.
DR   SMR; Q84K11; -.
DR   STRING; 4081.Q84K11; -.
DR   GeneID; 543849; -.
DR   KEGG; sly:543849; -.
DR   InParanoid; Q84K11; -.
DR   OrthoDB; 1107740at2759; -.
DR   BRENDA; 3.1.3.16; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q84K11; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW   Manganese; Membrane; Metal-binding; Nucleus; Protein phosphatase;
KW   Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..556
FT                   /note="Serine/threonine-protein phosphatase 5"
FT                   /id="PRO_0000308995"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          14..47
FT                   /note="TPR 1"
FT   REPEAT          49..81
FT                   /note="TPR 2"
FT   REPEAT          82..115
FT                   /note="TPR 3"
FT   ACT_SITE        362
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
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="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         361
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         410
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         485
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         158..228
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12972652"
FT                   /id="VSP_029090"
FT   MUTAGEN         411
FT                   /note="G->R: Loss of activity; in isoform 2."
FT                   /evidence="ECO:0000269|PubMed:12972652"
SQ   SEQUENCE   556 AA;  61860 MW;  39262299C9B27866 CRC64;
     MPGMEAENSN ASRAEELKQL ANEAFKGHKY SQAIDLYTQA IELNGENAVY YANRAFAHTK
     LEEYGSAIQD GTRAIEIDPR YSKGYYRRGA AYLAMGKFKD ALKDFQQVKK LCPNDPDATK
     KLKECEKAVM KLKFEEAISV PESQRRSVAD SIDYRSVGSG PGSSYVPTKT TAVSAAAALM
     GVLVVYMGTK AATMVAAAAS AALLVVLITF LWGRCSDGFF TKSRTLELEV EPQYAGARIE
     GDVVTLDFVK KMLDDFKNQK NLHKRYAYQI VLQTREMLRA LPSLVDIVVP EGKHFTVCGD
     VHGQFYDLLN IFELNGLPSE DNPYLFNGDF VDRGSFSLEV ILTLFAFKCM CPSAIHLARG
     NHESKSMNKI YGFEGEVRSK LSEIFVELFA EVFCCLPLAH VINEKVFVVH GGLFSVDGVK
     LSDIRAIDRF CEPPEEGLMC ELLWSDPQPQ PGRGPSKRGV GLSFGGDVTK RFLQENNLDL
     VVRSHEVKDE GYEIEHDGKL ITVFSAPNYC DQMGNKGAFI RFEAPDMKPN IVTFSAVPHP
     DVKPMAYANN FLRMFS
//