A7L9Z8
PR
Gene name |
Atp2c2 |
Protein name |
Calcium-transporting ATPase type 2C member 2 |
Names |
ATPase 2C2, Ca(2+)/Mn(2+)-ATPase 2C2, Secretory pathway Ca(2+)-transporting ATPase type 2, SPCA2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:69047 |
EC number |
7.2.2.10: Linked to the hydrolysis of a nucleoside triphosphate |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A7L9Z8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A7L9Z8-F1 | Predicted | AlphaFoldDB |
65 variants for A7L9Z8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs45857488 | 48 | A>T | No | EVA | |
| rs3389013664 | 73 | S>N | No | EVA | |
| rs3389013266 | 77 | E>D | No | EVA | |
| rs243926091 | 86 | V>I | No | EVA | |
| rs3389017068 | 90 | N>S | No | EVA | |
| rs3389013675 | 100 | V>A | No | EVA | |
| rs212034026 | 110 | N>S | No | EVA | |
| rs3399386620 | 167 | E>G | No | EVA | |
| rs3388996832 | 186 | P>Q | No | EVA | |
| rs3388965722 | 213 | D>N | No | EVA | |
| rs233354915 | 229 | S>N | No | EVA | |
| rs260500945 | 233 | D>G | No | EVA | |
| rs227865386 | 249 | L>M | No | EVA | |
| rs3389021971 | 261 | G>* | No | EVA | |
| rs3389008688 | 334 | P>L | No | EVA | |
| rs3388991259 | 343 | V>M | No | EVA | |
| rs3389013692 | 349 | V>M | No | EVA | |
| rs3388996844 | 352 | M>L | No | EVA | |
| rs3388984839 | 361 | K>R | No | EVA | |
| rs3389013467 | 390 | T>P | No | EVA | |
| rs3399661406 | 413 | V>E | No | EVA | |
| rs3399758964 | 413 | V>L | No | EVA | |
| rs3399677202 | 414 | C>S | No | EVA | |
| rs3389002496 | 434 | V>M | No | EVA | |
| rs3413084253 | 454 | P>L | No | EVA | |
| rs3388984829 | 463 | A>T | No | EVA | |
| rs51409418 | 470 | S>G | No | EVA | |
| rs3389013465 | 476 | V>I | No | EVA | |
| rs3389010164 | 479 | K>* | No | EVA | |
| rs48799094 | 481 | I>V | No | EVA | |
| rs3389010221 | 508 | K>* | No | EVA | |
| rs3388965719 | 542 | E>V | No | EVA | |
| rs3389010223 | 561 | L>M | No | EVA | |
| rs3389013499 | 568 | G>S | No | EVA | |
| rs3389002547 | 600 | D>G | No | EVA | |
| rs3389013294 | 609 | G>* | No | EVA | |
| rs3389013618 | 650 | P>L | No | EVA | |
| rs3389013443 | 669 | M>L | No | EVA | |
| rs3388996807 | 676 | D>H | No | EVA | |
| rs3399661421 | 686 | G>W | No | EVA | |
| rs3389017028 | 696 | V>L | No | EVA | |
| rs46407037 | 707 | D>A | No | EVA | |
| rs3399759839 | 713 | I>N | No | EVA | |
| rs3399781868 | 713 | I>V | No | EVA | |
| rs3389009270 | 716 | A>T | No | EVA | |
| rs3399759846 | 719 | E>G | No | EVA | |
| rs3389013427 | 726 | N>D | No | EVA | |
| rs3389013634 | 731 | V>I | No | EVA | |
| rs3388965718 | 741 | A>T | No | EVA | |
| rs13474595 | 765 | V>A | No | EVA | |
| rs3389010193 | 767 | I>V | No | EVA | |
| rs3389010160 | 768 | I>F | No | EVA | |
| rs46818414 | 770 | D>E | No | EVA | |
| rs258549032 | 794 | V>I | No | EVA | |
| rs3388991234 | 795 | G>W | No | EVA | |
| rs3389009309 | 796 | D>N | No | EVA | |
| rs3399692101 | 820 | F>C | No | EVA | |
| rs3399692073 | 820 | F>L | No | EVA | |
| rs3389010163 | 867 | F>L | No | EVA | |
| rs3389015503 | 899 | T>I | No | EVA | |
| rs3389010184 | 917 | V>I | No | EVA | |
| rs3388996814 | 922 | E>K | No | EVA | |
| rs3388996846 | 923 | L>R | No | EVA | |
| rs3388965788 | 924 | L>V | No | EVA | |
| rs3389002569 | 933 | R>K | No | EVA |
No associated diseases with A7L9Z8
4 regional properties for A7L9Z8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cation-transporting P-type ATPase, N-terminal | 54 - 128 | IPR004014 |
| domain | Cation-transporting P-type ATPase, C-terminal | 754 - 926 | IPR006068 |
| ptm | P-type ATPase, phosphorylation site | 377 - 383 | IPR018303 |
| domain | P-type ATPase, haloacid dehalogenase domain | 357 - 721 | 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 | |
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| basolateral plasma membrane | The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis. |
| cytoplasmic side of plasma membrane | The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
| cytoplasmic vesicle | A vesicle found in the cytoplasm of a cell. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| integral component of membrane | The component of a 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. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| trans-Golgi network membrane | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| 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). |
| P-type ion 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 = ADP + phosphate, to directly drive the transport of ions across a membrane. The reaction is characterized by the transient formation of a high-energy aspartyl-phosphoryl-enzyme intermediate. |
| P-type manganese 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 + Mn2+(in) = ADP + H+ + Mn2+(out) + phosphate. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| calcium ion transmembrane transport | A process in which a calcium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. |
| cellular calcium ion homeostasis | Any process involved in the maintenance of an internal steady state of calcium ions at the level of a cell. |
| ion transmembrane transport | A process in which an ion is transported across a membrane. |
| mammary gland epithelium development | The process whose specific outcome is the progression of the mammary gland epithelium over time, from its formation to the mature structure. The mammary gland is a large compound sebaceous gland that in female mammals is modified to secrete milk. |
| manganese ion transport | The directed movement of manganese (Mn) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| positive regulation of calcium ion import | Any process that increases the rate, frequency, or extent of the directed movement of calcium ions into a cell or organelle. |
| protein localization to plasma membrane | A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane. |
10 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P57709 | ATP2C1 | Calcium-transporting ATPase type 2C member 1 | Bos taurus (Bovine) | PR |
| Q80XR2 | Atp2c1 | Calcium-transporting ATPase type 2C member 1 | Mus musculus (Mouse) | PR |
| P20431 | AHA3 | ATPase 3, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LY32 | AHA7 | ATPase 7, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9SU58 | AHA4 | ATPase 4, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q43128 | AHA10 | ATPase 10, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9SH76 | AHA6 | ATPase 6, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P20649 | AHA1 | ATPase 1, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9M2A0 | AHA8 | ATPase 8, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LV11 | AHA11 | ATPase 11, plasma membrane-type | Arabidopsis thaliana (Mouse-ear cress) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGRRLKFLQK | LAFLGQNHRY | KALERDEVET | LIDEQCELKA | IEREKTVAAL | PPGEACKCSR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EELARAFHVD | LDSGLSEFAV | AQRRLVHGWN | EFVTDNAEPV | WKKYLDQFRN | PLILLLLGSS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VVSVLTKEYE | DAVSIALAVL | IVVTVGFIQE | YRSEKSLEEL | TKLVPPECNC | LRDGKLRHML |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ARDLVPGDIV | SLSMGDRIPA | DIRLTEVTDL | LVDESSFTGE | VEPCGKTDSP | LADGGDLSTL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SNVVFMGTLV | QCGKGQGVVI | GTGEQSQFGE | VFKMMRAEET | PKTPLQKSMD | KLGKQLTIFS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FGIIGLLMLV | GWVQGKPFLS | MFTVGVSLAV | AAIPEGLPIV | VMVTLVLGVL | RMAKKRVIVK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLPIVETLGC | CNVICSDKTG | TLTANEMTAT | QLVTSDGFHA | EVSGVGYSGE | GTVCLLPSKE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VIKGFDNVSV | GKLVEAGCVA | NNAVIRKNAV | MGQPTEGALV | VLAMKMNLGS | IKDSYVRKKE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IPFSSEQKWM | AVRCGPKSED | GEDIYFMKGA | FEEVIHHCSM | YNNGGIPLPL | TPQQKSYCQQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EEKKMGSLGL | RVLALASGPE | LGRLTFLGLV | GIIDPPRAGV | KEAVQVLSES | GVSVKMVTGD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ALETALAIGR | TIGLCNEKLK | AMSGEEVEGT | EQGALAARVR | QVSVFFRTSP | KHKVKIIKAL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QESGAIVAMT | GDGVNDSVAL | KSADIGIAMG | QTGTDVSKEA | ANMILVDDDF | SAIMSAVEEG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KGIFYNIKNF | VRFQLSTSIA | ALSLITLSTV | CNLPSPLNAM | QILWVNIIMD | GPPAQSLGVE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PVDRDALRRP | PRSVGDTILN | RALILRVLMS | AAVIIGGTLF | IFWREIPANG | TSTPRTTTMA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FTCFVFFDLF | NALSCRSQTK | LIFEIGFFRN | RMFLYSVLGS | LLGQLAVIYA | PPLQKVFQTE |
| 910 | 920 | 930 | 940 | ||
| NLSALDLLLL | TGLASSVFIL | SELLKLWEKF | LSRARPTQML | PEAV |