Q84XU2
SS
Gene name |
PAPP5 (PP5, At2g42810, F7D19.19) |
Protein name |
Serine/threonine-protein phosphatase 5 |
Names |
EC 3.1.3.16 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT2G42810 |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
|
Descriptions
Protein phosphatase 5 is involved in the regulation of kinases and transcription factors. Its dephosphorylation activity is modulated by the C-terminal MEEVD motif of molecular chaperone Hsp90, which binds to the tetratricopeptide repeat (TPR) domain of protein phosphatase 5. The TRP domain is involved in autoinhibition and the addition of a peptide containing the MEEVD motif counteracts the autoinhibition of the TPR domain.
Autoinhibitory domains (AIDs)
Target domain |
142-536 (Phosphatase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Haslbeck V et al. (2015) "The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90", Scientific reports, 5, 17058
- Chen MX et al. (1997) "Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain", FEBS letters, 400, 136-40
- Kang H et al. (2001) "Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation", Biochemistry, 40, 10485-90
- Oberoi J et al. (2016) "Structural and functional basis of protein phosphatase 5 substrate specificity", Proceedings of the National Academy of Sciences of the United States of America, 113, 9009-14
- Cliff MJ et al. (2006) "Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90", Structure (London, England : 1993), 14, 415-26
Autoinhibited structure
Activated structure
3 structures for Q84XU2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5JJT | X-ray | 210 A | A/B | 5-537 | PDB |
| 7OBE | X-ray | 300 A | A/B | 1-484 | PDB |
| AF-Q84XU2-F1 | Predicted | AlphaFoldDB |
26 variants for Q84XU2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| ENSVATH05706096 | 18 | S>N | No | 1000Genomes | |
| tmp_2_17815821_C_A | 26 | G>C | No | 1000Genomes | |
| tmp_2_17815692_T_C | 33 | I>V | No | 1000Genomes | |
| tmp_2_17815623_C_T | 56 | A>T | No | 1000Genomes | |
| tmp_2_17815464_A_G | 84 | Y>H | No | 1000Genomes | |
| tmp_2_17815020_T_C | 113 | N>S | No | 1000Genomes | |
| ENSVATH13621769 | 154 | H>Y | No | 1000Genomes | |
| tmp_2_17814694_C_T | 165 | M>I | No | 1000Genomes | |
| ENSVATH05706047 | 220 | R>G | No | 1000Genomes | |
| ENSVATH05706046 | 227 | T>I | No | 1000Genomes | |
| tmp_2_17813998_T_C | 258 | Q>R | No | 1000Genomes | |
| ENSVATH13621742 | 265 | S>P | No | 1000Genomes | |
| ENSVATH05706039 | 273 | H>N | No | 1000Genomes | |
| tmp_2_17813613_C_G | 295 | E>D | No | 1000Genomes | |
| ENSVATH05706020 | 296 | L>H | No | 1000Genomes | |
| tmp_2_17813520_C_A | 326 | L>F | No | 1000Genomes | |
| ENSVATH05706017 | 333 | C>R | No | 1000Genomes | |
| ENSVATH05706003 | 370 | L>F | No | 1000Genomes | |
| tmp_2_17813226_C_T | 372 | A>T | No | 1000Genomes | |
| ENSVATH00271860 | 400 | G>S | No | 1000Genomes | |
| ENSVATH14609972 | 452 | K>M | No | 1000Genomes | |
| ENSVATH05705999 | 460 | L>I | No | 1000Genomes | |
| ENSVATH05705998 | 461 | D>N | No | 1000Genomes | |
| tmp_2_17812770_C_G | 462 | L>F | No | 1000Genomes | |
| tmp_2_17812772_A_T | 462 | L>M | No | 1000Genomes | |
| tmp_2_17812555_C_T | 506 | A>T | No | 1000Genomes |
No associated diseases with Q84XU2
7 regional properties for Q84XU2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Calcineurin-like phosphoesterase domain, ApaH type | 276 - 470 | IPR004843 |
| domain | Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase | 244 - 520 | IPR006186 |
| domain | PPP domain | 211 - 268 | IPR013235 |
| repeat | Tetratricopeptide repeat | 13 - 46 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 47 - 80 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 81 - 114 | IPR019734-3 |
| domain | PP5, C-terminal metallophosphatase domain | 216 - 531 | IPR041753 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| nuclear envelope | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). |
| nuclear membrane | Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. |
| nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| plasmodesma | A fine cytoplasmic channel, found in all higher plants, that connects the cytoplasm of one cell to that of an adjacent cell. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| myosin phosphatase activity | Catalysis of the reaction |
| phosphoprotein phosphatase activity | Catalysis of the reaction |
| protein serine/threonine phosphatase activity | Catalysis of the reaction |
| tetrapyrrole binding | Binding to a tetrapyrrole, a compound containing four pyrrole nuclei variously substituted and linked to each other through carbons at the alpha position. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chloroplast-nucleus signaling pathway | The process in which a molecular signal is transduced between the chloroplast and nucleus, such that expression of nuclear encoding photosynthetic proteins is coupled with chloroplast biogenesis. |
| negative regulation of chlorophyll biosynthetic process | Any process that stops, prevents or reduces the frequency, rate or extent of chlorophyll biosynthetic process. |
| nucleocytoplasmic transport | The directed movement of molecules between the nucleus and the cytoplasm. |
| red or far-red light signaling pathway | The series of molecular signals initiated upon sensing by photoreceptor molecules of red light or far red light. Red light is electromagnetic radiation of wavelength of 580-700nm. Far red light is electromagnetic radiation of wavelength 700-800nm. An example of this response is seen at the beginning of many plant species developmental stages. These include germination, and the point when cotyledon expansion is triggered. In certain species these processes take place in response to absorption of red light by the pigment molecule phytochrome, but the signal can be reversed by exposure to far red light. During the initial phase the phytochrome molecule is only present in the red light absorbing form, but on absorption of red light it changes to a far red light absorbing form, triggering progress through development. An immediate short period of exposure to far red light entirely returns the pigment to its initial state and prevents triggering of the developmental process. A thirty minute break between red and subsequent far red light exposure renders the red light effect irreversible, and development then occurs regardless of whether far red light exposure subsequently occurs. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P53043 | PPT1 | Serine/threonine-protein phosphatase T | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P53041 | PPP5C | Serine/threonine-protein phosphatase 5 | Homo sapiens (Human) | EV |
| Q60676 | Ppp5c | Serine/threonine-protein phosphatase 5 | Mus musculus (Mouse) | SS |
| P53042 | Ppp5c | Serine/threonine-protein phosphatase 5 | Rattus norvegicus (Rat) | EV |
| Q9NES8 | pph-5 | Serine/threonine-protein phosphatase 5 | Caenorhabditis elegans | EV |
| Q84K11 | PP5 | Serine/threonine-protein phosphatase 5 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| METKNENSDV | SRAEEFKSQA | NEAFKGHKYS | SAIDLYTKAI | ELNSNNAVYW | ANRAFAHTKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EEYGSAIQDA | SKAIEVDSRY | SKGYYRRGAA | YLAMGKFKDA | LKDFQQVKRL | SPNDPDATRK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LKECEKAVMK | LKFEEAISVP | VSERRSVAES | IDFHTIGNKP | RSSSMPTKTA | LAAVVAAVMV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VAVRGFATTE | ILMVLVSVVL | GTFWWGSFSG | KVEPQYSGAR | IEGEEVTLDF | VKTMMEDFKN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QKTLHKRYAY | QIVLQTRQIL | LALPSLVDIS | VPHGKHITVC | GDVHGQFYDL | LNIFELNGLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SEENPYLFNG | DFVDRGSFSV | EIILTLFAFK | CMCPSSIYLA | RGNHESKSMN | KIYGFEGEVR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SKLSEKFVDL | FAEVFCYLPL | AHVINGKVFV | VHGGLFSVDG | VKLSDIRAID | RFCEPPEEGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MCELLWSDPQ | PLPGRGPSKR | GVGLSFGGDV | TKRFLQDNNL | DLLVRSHEVK | DEGYEVEHDG |
| 490 | 500 | 510 | 520 | 530 | |
| KLITVFSAPN | YCDQMGNKGA | FIRFEAPDMK | PNIVTFSAVP | HPDVKPMAYA | NNFLRMFN |