PPP5_SOLLC
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 03-AUG-2022, entry version 120.
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 PRIDE; Q84K11; -.
DR GeneID; 543849; -.
DR KEGG; sly:543849; -.
DR InParanoid; Q84K11; -.
DR OrthoDB; 671536at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.25.40.10; -; 1.
DR Gene3D; 3.60.21.10; -; 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 Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56300; SSF56300; 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
