O22218
Gene name |
ACA4 |
Protein name |
Calcium-transporting ATPase 4, plasma membrane-type |
Names |
Ca(2+)-ATPase isoform 4 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT2G41560 |
EC number |
7.2.2.10: Linked to the hydrolysis of a nucleoside triphosphate |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
431-799 (ATPase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- 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
- 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
- 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
- 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 O22218
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-O22218-F1 | Predicted | AlphaFoldDB |
44 variants for O22218
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
ENSVATH05698078 | 3 | N>S | No | 1000Genomes | |
tmp_2_17337147_C_A | 11 | E>D | No | 1000Genomes | |
ENSVATH00269329 | 33 | R>P | No | 1000Genomes | |
ENSVATH01977474 | 41 | R>Q | No | 1000Genomes | |
tmp_2_17337036_G_T | 48 | D>E | No | 1000Genomes | |
ENSVATH14605682 | 77 | A>P | No | 1000Genomes | |
tmp_2_17335465_G_A | 78 | A>V | No | 1000Genomes | |
ENSVATH14605681 | 79 | R>K | No | 1000Genomes | |
tmp_2_17335417_G_C | 94 | S>C | No | 1000Genomes | |
tmp_2_17335313_G_A | 129 | L>F | No | 1000Genomes | |
ENSVATH01977453 | 134 | R>C | No | 1000Genomes | |
ENSVATH01977452 | 151 | T>S | No | 1000Genomes | |
ENSVATH05698032 | 273 | S>C | No | 1000Genomes | |
tmp_2_17334851_T_C | 283 | S>G | No | 1000Genomes | |
ENSVATH13608885 | 313 | M>V | No | 1000Genomes | |
ENSVATH05698029 | 358 | S>N | No | 1000Genomes | |
tmp_2_17334556_A_G | 381 | F>S | No | 1000Genomes | |
ENSVATH14605680 | 392 | L>V | No | 1000Genomes | |
ENSVATH05698028 | 494 | T>I | No | 1000Genomes | |
ENSVATH05698027 | 512 | D>Y | No | 1000Genomes | |
tmp_2_17334048_C_G | 550 | E>D | No | 1000Genomes | |
tmp_2_17333950_T_C | 583 | K>R | No | 1000Genomes | |
tmp_2_17333914_G_A | 595 | S>L | No | 1000Genomes | |
tmp_2_17333909_G_A | 597 | P>S | No | 1000Genomes | |
ENSVATH01977446 | 611 | E>V | No | 1000Genomes | |
ENSVATH05698024 | 624 | V>G | No | 1000Genomes | |
tmp_2_17333774_T_A | 642 | T>S | No | 1000Genomes | |
tmp_2_17333734_G_A | 655 | P>L | No | 1000Genomes | |
ENSVATH13608873 | 660 | A>S | No | 1000Genomes | |
tmp_2_17333639_T_G | 687 | K>Q | No | 1000Genomes | |
ENSVATH13608872 | 694 | E>Q | No | 1000Genomes | |
ENSVATH13608871 | 712 | M>K | No | 1000Genomes | |
tmp_2_17333042_C_A | 824 | V>F | No | 1000Genomes | |
ENSVATH05698010 | 869 | I>L | No | 1000Genomes | |
ENSVATH01977442 | 873 | A>T | No | 1000Genomes | |
ENSVATH14605676 | 879 | T>I | No | 1000Genomes | |
tmp_2_17332773_G_A | 885 | A>V | No | 1000Genomes | |
ENSVATH05698008 | 903 | K>N | No | 1000Genomes | |
tmp_2_17332681_C_T | 916 | V>I | No | 1000Genomes | |
ENSVATH14605675 | 917 | L>R | No | 1000Genomes | |
ENSVATH13608849 | 948 | M>L | No | 1000Genomes | |
tmp_2_17332422_G_A | 976 | A>V | No | 1000Genomes | |
ENSVATH00269318 | 996 | N>S | No | 1000Genomes | |
ENSVATH05698001 | 1006 | V>I | No | 1000Genomes |
No associated diseases with O22218
10 regional properties for O22218
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Protein kinase domain | 670 - 919 | IPR000719 |
domain | Ephrin receptor ligand binding domain | 33 - 237 | IPR001090 |
domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 670 - 914 | IPR001245 |
conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 213 - 233 | IPR001426-1 |
conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 286 - 306 | IPR001426-2 |
domain | Sterile alpha motif domain | 945 - 1012 | IPR001660 |
domain | Fibronectin type III | 369 - 486 | IPR003961-1 |
domain | Fibronectin type III | 487 - 582 | IPR003961-2 |
domain | Tyrosine-protein kinase ephrin type A/B receptor-like | 306 - 345 | IPR011641 |
domain | Ephrin receptor, transmembrane domain | 596 - 667 | IPR027936 |
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 |
8 GO annotations of cellular component
Name | Definition |
---|---|
chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
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. |
plant-type vacuole | A closed structure that is completely surrounded by a unit membrane, contains liquid, and retains the same shape regardless of cell cycle phase. An example of this structure is found in Arabidopsis thaliana. |
plant-type vacuole membrane | The lipid bilayer surrounding a vacuole that retains the same shape regardless of cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this component is found in Arabidopsis thaliana. |
vacuolar membrane | The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell. |
vacuole | A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol. |
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). |
4 GO annotations of biological process
Name | Definition |
---|---|
anion homeostasis | Any process involved in the maintenance of an internal steady state of anions within an organism or cell. |
defense response to bacterium | Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. |
negative regulation of programmed cell death | Any process that stops, prevents, or reduces the frequency, rate or extent of programmed cell death, cell death resulting from activation of endogenous cellular processes. |
response to nematode | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a nematode. |
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 |
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 |
Q2QMX9 | ACA10 | Calcium-transporting ATPase 10, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
Q2QY12 | ACA9 | Probable calcium-transporting ATPase 9, plasma membrane-type | Oryza sativa subsp japonica (Rice) | SS |
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 |
O64806 | ACA7 | Putative calcium-transporting ATPase 7, 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 |
Q9LIK7 | ACA13 | Putative calcium-transporting ATPase 13, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q9LU41 | ACA9 | Calcium-transporting ATPase 9, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q9LY77 | ACA12 | Calcium-transporting ATPase 12, 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 |
Q9SZR1 | ACA10 | Calcium-transporting ATPase 10, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q37145 | ACA1 | Calcium-transporting ATPase 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MSNLLRDFEV | EAKNPSLEAR | QRWRSSVSIV | KNRTRRFRNI | RDLDKLADYE | NKKHQIQEKI |
70 | 80 | 90 | 100 | 110 | 120 |
RVAFFVQKAA | LHFIDAAARP | EYKLTDEVKK | AGFSIEADEL | ASMVRKNDTK | SLAQKGGVEE |
130 | 140 | 150 | 160 | 170 | 180 |
LAKKVSVSLS | EGIRSSEVPI | REKIFGENRY | TEKPARSFLM | FVWEALHDIT | LIILMVCAVV |
190 | 200 | 210 | 220 | 230 | 240 |
SIGVGVATEG | FPRGMYDGTG | ILLSILLVVM | VTAISDYKQS | LQFRDLDREK | KKIIVQVTRD |
250 | 260 | 270 | 280 | 290 | 300 |
GSRQEISIHD | LVVGDVVHLS | IGDQVPADGI | FISGYNLEID | ESSLSGESEP | SHVNKEKPFL |
310 | 320 | 330 | 340 | 350 | 360 |
LSGTKVQNGS | AKMLVTTVGM | RTEWGKLMET | LVDGGEDETP | LQVKLNGVAT | IIGKIGLSFA |
370 | 380 | 390 | 400 | 410 | 420 |
VLTFVVLCIR | FVLDKATSGS | FTNWSSEDAL | TLLDYFAISV | TIIVVAVPEG | LPLAVTLSLA |
430 | 440 | 450 | 460 | 470 | 480 |
FAMKKLMSDR | ALVRHLAACE | TMGSSTCICT | DKTGTLTTNH | MVVNKVWICD | KVQERQEGSK |
490 | 500 | 510 | 520 | 530 | 540 |
ESFELELSEE | VQSTLLQGIF | QNTGSEVVKD | KDGNTQILGS | PTERAILEFG | LLLGGDFNTQ |
550 | 560 | 570 | 580 | 590 | 600 |
RKEHKILKIE | PFNSDKKKMS | VLIALPGGGA | RAFCKGASEI | VLKMCENVVD | SNGESVPLTE |
610 | 620 | 630 | 640 | 650 | 660 |
ERITSISDII | EGFASEALRT | LCLVYKDLDE | APSGELPDGG | YTMVAVVGIK | DPVRPGVREA |
670 | 680 | 690 | 700 | 710 | 720 |
VQTCQAAGIT | VRMVTGDNIS | TAKAIAKECG | IYTEGGLAIE | GSEFRDLSPH | EMRAIIPKIQ |
730 | 740 | 750 | 760 | 770 | 780 |
VMARSLPLDK | HTLVSNLRKI | GEVVAVTGDG | TNDAPALHEA | DIGLAMGIAG | TEVAKENADV |
790 | 800 | 810 | 820 | 830 | 840 |
IIMDDNFKTI | VNVARWGRAV | YINIQKFVQF | QLTVNVVALI | INFVSACITG | SAPLTAVQLL |
850 | 860 | 870 | 880 | 890 | 900 |
WVNMIMDTLG | ALALATEPPN | EGLMKRAPIA | RTASFITKTM | WRNIAGQSVY | QLIVLGILNF |
910 | 920 | 930 | 940 | 950 | 960 |
AGKSLLKLDG | PDSTAVLNTV | IFNSFVFCQV | FNEINSREIE | KINVFKGMFN | SWVFTWVMTV |
970 | 980 | 990 | 1000 | 1010 | 1020 |
TVVFQVIIVE | FLGAFASTVP | LSWQHWLLSI | LIGSLNMIVA | VILKCVPVES | RHHHDGYDLL |
PSGPSSSNSA |