Q2QY12
SS
Gene name |
ACA9 |
Protein name |
Probable calcium-transporting ATPase 9, plasma membrane-type |
Names |
OsACA9, Ca(2+)-ATPase isoform 9 |
Species |
Oryza sativa subsp japonica (Rice) |
KEGG Pathway |
osa:4351449 |
EC number |
7.2.2.10: Linked to the hydrolysis of a nucleoside triphosphate |
Protein Class |
|
Descriptions
Calcium-transporting ATPases (ACAs) catalyze the hydrolysis of ATP coupled with the translocation of calcium. The N-terminal region interacts with calmodulin in the same protein and it contains a known autoinhibitory region at N-terminus.
Autoinhibitory domains (AIDs)
Target domain |
436-808 (ATPase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Singh A et al. (2014) "Genome-wide expressional and functional analysis of calcium transport elements during abiotic stress and development in rice", The FEBS journal, 281, 894-915
- Luoni L et al. (2004) "Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop", FEBS letters, 574, 20-4
- Tidow H et al. (2010) "Expression, purification, crystallization and preliminary X-ray analysis of calmodulin in complex with the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8", Acta crystallographica. Section F, Structural biology and crystallization communications, 66, 361-3
- Harper JF et al. (1998) "A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain", The Journal of biological chemistry, 273, 1099-106
- Calì T et al. (2017) "The ataxia related G1107D mutation of the plasma membrane Ca(2+) ATPase isoform 3 affects its interplay with calmodulin and the autoinhibition process", Biochimica et biophysica acta. Molecular basis of disease, 1863, 165-173
- Carafoli E (1994) "Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme", FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 8, 993-1002
- Saffioti NA et al. (2021) "Conformational changes during the reaction cycle of plasma membrane Ca2+-ATPase in the autoinhibited and activated states", The Biochemical journal, 478, 2019-2034
- Calì T et al. (2018) "The PMCA pumps in genetically determined neuronal pathologies", Neuroscience letters, 663, 2-11
- Corradi GR et al. (2007) "Intramolecular fluorescence resonance energy transfer between fused autofluorescent proteins reveals rearrangements of the N- and C-terminal segments of the plasma membrane Ca2+ pump involved in the activation", The Journal of biological chemistry, 282, 35440-8
- Osborn KD et al. (2005) "Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase", Biochemistry, 44, 11074-81
- Lopreiato R et al. (2014) "The plasma membrane calcium pump: new ways to look at an old enzyme", The Journal of biological chemistry, 289, 10261-10268
- Bredeston LM et al. (2004) "Loss of autoinhibition of the plasma membrane Ca(2+) pump by substitution of aspartic 170 by asparagin. A ctivation of plasma membrane calcium ATPase 4 without disruption of the interaction between the catalytic core and the C-terminal regulatory domain", The Journal of biological chemistry, 279, 41619-25
- Pinto Fde T et al. (2002) "Deletions in the acidic lipid-binding region of the plasma membrane Ca2+ pump. A mutant with high affinity for Ca2+ resembling the acidic lipid-activated enzyme", The Journal of biological chemistry, 277, 12784-9
Autoinhibited structure
Activated structure
1 structures for Q2QY12
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2QY12-F1 | Predicted | AlphaFoldDB |
No variants for Q2QY12
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2QY12 | |||||
No associated diseases with Q2QY12
5 regional properties for Q2QY12
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cation-transporting P-type ATPase, N-terminal | 96 - 191 | IPR004014 |
| domain | Cation-transporting P-type ATPase, C-terminal | 841 - 1014 | IPR006068 |
| ptm | P-type ATPase, phosphorylation site | 456 - 462 | IPR018303 |
| domain | Calcium-transporting P-type ATPase, N-terminal autoinhibitory domain | 8 - 52 | IPR024750 |
| domain | P-type ATPase, haloacid dehalogenase domain | 436 - 808 | IPR044492 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.2.2.10 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of plasma membrane | The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATPase-coupled cation transmembrane transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + cation(out) = ADP + phosphate + cation(in). |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| metal ion binding | Binding to a metal ion. |
| P-type calcium transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Ca2+(in) = ADP + phosphate + Ca2+(out). |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
31 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P38929 | PMC1 | Calcium-transporting ATPase 2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| D3K0R6 | ATP2B4 | Plasma membrane calcium-transporting ATPase 4 | Bos taurus (Bovine) | SS |
| Q01814 | ATP2B2 | Plasma membrane calcium-transporting ATPase 2 | Homo sapiens (Human) | SS |
| P23634 | ATP2B4 | Plasma membrane calcium-transporting ATPase 4 | Homo sapiens (Human) | EV |
| P20020 | ATP2B1 | Plasma membrane calcium-transporting ATPase 1 | Homo sapiens (Human) | SS |
| Q16720 | ATP2B3 | Plasma membrane calcium-transporting ATPase 3 | Homo sapiens (Human) | EV |
| G5E829 | Atp2b1 | Plasma membrane calcium-transporting ATPase 1 | Mus musculus (Mouse) | SS |
| Q9R0K7 | Atp2b2 | Plasma membrane calcium-transporting ATPase 2 | Mus musculus (Mouse) | SS |
| Q6Q477 | Atp2b4 | Plasma membrane calcium-transporting ATPase 4 | Mus musculus (Mouse) | SS |
| P23220 | ATP2B1 | Plasma membrane calcium-transporting ATPase 1 | Sus scrofa (Pig) | SS |
| P11506 | Atp2b2 | Plasma membrane calcium-transporting ATPase 2 | Rattus norvegicus (Rat) | SS |
| Q64542 | Atp2b4 | Plasma membrane calcium-transporting ATPase 4 | Rattus norvegicus (Rat) | SS |
| P11505 | Atp2b1 | Plasma membrane calcium-transporting ATPase 1 | Rattus norvegicus (Rat) | SS |
| Q64568 | Atp2b3 | Plasma membrane calcium-transporting ATPase 3 | Rattus norvegicus (Rat) | SS |
| Q2QMX9 | ACA10 | Calcium-transporting ATPase 10, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q6ATV4 | ACA3 | Calcium-transporting ATPase 3, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q7X8B5 | ACA5 | Calcium-transporting ATPase 5, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q7XEK4 | ACA7 | Calcium-transporting ATPase 7, plasma membrane-type | Oryza sativa subsp japonica (Rice) | EV |
| Q8RUN1 | ACA1 | Calcium-transporting ATPase 1, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q65X71 | ACA6 | Probable calcium-transporting ATPase 6, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q2RAS0 | ACA8 | Probable calcium-transporting ATPase 8, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
| Q37145 | ACA1 | Calcium-transporting ATPase 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| O64806 | ACA7 | Putative calcium-transporting ATPase 7, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LU41 | ACA9 | Calcium-transporting ATPase 9, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LIK7 | ACA13 | Putative calcium-transporting ATPase 13, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LY77 | ACA12 | Calcium-transporting ATPase 12, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9SZR1 | ACA10 | Calcium-transporting ATPase 10, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| O81108 | ACA2 | Calcium-transporting ATPase 2, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | EV |
| Q9LF79 | ACA8 | Calcium-transporting ATPase 8, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | EV |
| O22218 | ACA4 | Calcium-transporting ATPase 4, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9M2L4 | ACA11 | Putative calcium-transporting ATPase 11, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEKLDRYLQE | NFDVPAKNPS | EEAQRRWRQA | VGTIVKNRRR | RFRWVPDLER | RSLDKAKVRS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TQEKIRVALY | VQQAALIFSD | GAKKKEYKLT | GDIIKAGYAI | NPDELALITS | KHDSKALKMH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GGVDGISIKV | RSSFDHGIYA | SELDTRQNIY | GVNRYAEKPS | RSFWMFVWDA | LQDMTLIILM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VCALLSVAVG | LATEGWPKGM | YDGLGIILSI | FLVVMVTAVS | DYKQSLQFKE | LDNEKKKIFI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HVTRDGRRQK | ISIYDLVVGD | IVHLSIGDQV | PADGLYIHGY | SLLIDESSLS | GESDPVYVSQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DKPFILAGTK | VQDGSAKMIV | TAVGMRTEWG | KLMSTLSEGG | EDETPLQVKL | NGVATIIGKI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLVFAILTFL | VLLVRFLIDK | GMTVGLLKWY | STDALTIVNY | FATAVTIIVV | AVPEGLPLAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TLSLAFAMKK | LMNDKALVRH | LSACETMGSA | GTICTDKTGT | LTTNHMVVDK | IWISEVSKSV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TSNTISGELN | SVVSSSTLSL | LLQGIFENTS | AEVVKEKDGK | QTVLGTPTER | AILEFGLGLK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GDHDAEYRAC | TKVKVEPFNS | VKKKMAVLIS | LPNGTSRWFC | KGASEIILQM | CDMMVDGDGN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AIPLSEAQRK | NILDTINSFA | SDALRTLCLA | YKEVDDDIDD | NADSPTSGFT | LIAIFGIKDP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VRPGVKDAVK | TCMSAGITVR | MVTGDNINTA | KAIAKECGIL | TEDGVAIEGP | EFHSKSTEEM |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RDLILNIQVM | ARSLPLDKHT | LVTNLRGMFD | EVVSVTGDGT | NDAPALHEAD | IGLAMGIAGT |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EVAKESADVI | VLDDNFTTII | NVARWGRAVY | INIQKFVQFQ | LTVNIVALVI | NFVSACIIGS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| APLTAVQLLW | VNMIMDTLGA | LALATEPPND | EMMKRPPVRK | GESFITKFMW | RNIMGQSLYQ |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LFVLGALMFG | GERLLNIKGA | DSKSIINTLI | FNSFVFCQVF | NEINSREMQK | INVFRGIISN |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| WIFIAVIAAT | VAFQVVIIEF | LGTFASTVPL | NWQHWLLSVG | LGSISLIVGV | ILKCIPVGSG |
| 1030 | |||||
| ETSATPNGYR | PLANGPDDI |