P15920
Gene name |
Atp6v0a2 (Atp6n1b, Tj6) |
Protein name |
V-type proton ATPase 116 kDa subunit a 2 |
Names |
V-ATPase 116 kDa subunit a 2, Immune suppressor factor J6B7, ISF, Lysosomal H(+)-transporting ATPase V0 subunit a 2, ShIF, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:21871 |
EC number |
|
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
2 structures for P15920
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2LX4 | NMR | - | A | 1-17 | PDB |
| AF-P15920-F1 | Predicted | AlphaFoldDB |
36 variants for P15920
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388786852 | 25 | C>Y | No | EVA | |
| rs3388800151 | 88 | A>T | No | EVA | |
| rs3388793813 | 117 | K>M | No | EVA | |
| rs3388779431 | 126 | V>E | No | EVA | |
| rs3388786876 | 126 | V>M | No | EVA | |
| rs3388764142 | 140 | K>R | No | EVA | |
| rs3412941730 | 149 | Y>H | No | EVA | |
| rs3388764117 | 291 | A>T | No | EVA | |
| rs3388784616 | 293 | E>K | No | EVA | |
| rs3388764094 | 299 | V>E | No | EVA | |
| rs3395774864 | 312 | L>F | No | EVA | |
| rs3395774900 | 313 | N>S | No | EVA | |
| rs3388792914 | 321 | N>K | No | EVA | |
| rs3388787676 | 355 | S>L | No | EVA | |
| rs3388784623 | 411 | M>T | No | EVA | |
| rs3388793983 | 470 | D>E | No | EVA | |
| rs3388800211 | 483 | W>S | No | EVA | |
| rs3395782255 | 484 | N>D | No | EVA | |
| rs3388782244 | 511 | H>Y | No | EVA | |
| rs3388793858 | 514 | T>I | No | EVA | |
| rs3388793804 | 515 | L>* | No | EVA | |
| rs227699251 | 526 | R>Q | No | EVA | |
| rs3388792971 | 556 | V>E | No | EVA | |
| rs50427088 | 611 | A>V | No | EVA | |
| rs3388791153 | 625 | I>V | No | EVA | |
| rs253879767 | 635 | T>A | No | EVA | |
| rs3388800181 | 642 | Y>N | No | EVA | |
| rs3388794061 | 669 | L>P | No | EVA | |
| rs3388800226 | 678 | R>P | No | EVA | |
| rs247457573 | 704 | N>S | No | EVA | |
| rs3388784663 | 707 | I>T | No | EVA | |
| rs3388790776 | 711 | N>T | No | EVA | |
| rs3388790759 | 727 | N>K | No | EVA | |
| rs3388787708 | 732 | L>Q | No | EVA | |
| rs3388794007 | 832 | G>C | No | EVA | |
| rs3388794007 | 832 | G>S | No | EVA |
No associated diseases with P15920
1 regional properties for P15920
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | UDP-glycosyltransferase family, conserved site | 341 - 384 | IPR035595 |
10 GO annotations of cellular component
| Name | Definition |
|---|---|
| acrosomal vesicle | A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome. |
| endosome membrane | The lipid bilayer surrounding an endosome. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| 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. |
| 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. |
| intracellular organelle | Organized structure of distinctive morphology and function, occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma 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. |
| vacuolar proton-transporting V-type ATPase complex | A proton-transporting two-sector ATPase complex found in the vacuolar membrane, where it acts as a proton pump to mediate acidification of the vacuolar lumen. |
| vacuolar proton-transporting V-type ATPase, V0 domain | The V0 domain of a proton-transporting V-type ATPase found in the vacuolar membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATPase binding | Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP. |
| proton-transporting ATPase activity, rotational mechanism | Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| cellular response to increased oxygen levels | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting an increase in the level of oxygen. |
| vacuolar acidification | Any process that reduces the pH of the vacuole, measured by the concentration of the hydrogen ion. |
16 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P32563 | VPH1 | V-type proton ATPase subunit a, vacuolar isoform | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q29466 | ATP6V0A1 | V-type proton ATPase 116 kDa subunit a 1 | Bos taurus (Bovine) | PR |
| O97681 | ATP6V0A2 | V-type proton ATPase 116 kDa subunit a 2 | Bos taurus (Bovine) | PR |
| Q9I8D0 | ATP6V0A1 | V-type proton ATPase 116 kDa subunit a 1 | Gallus gallus (Chicken) | PR |
| Q13488 | TCIRG1 | V-type proton ATPase 116 kDa subunit a 3 | Homo sapiens (Human) | PR |
| Q93050 | ATP6V0A1 | V-type proton ATPase 116 kDa subunit a 1 | Homo sapiens (Human) | PR |
| Q9HBG4 | ATP6V0A4 | V-type proton ATPase 116 kDa subunit a 4 | Homo sapiens (Human) | PR |
| Q9Y487 | ATP6V0A2 | V-type proton ATPase 116 kDa subunit a 2 | Homo sapiens (Human) | PR |
| Q920R6 | Atp6v0a4 | V-type proton ATPase 116 kDa subunit a 4 | Mus musculus (Mouse) | PR |
| Q9Z1G4 | Atp6v0a1 | V-type proton ATPase 116 kDa subunit a 1 | Mus musculus (Mouse) | PR |
| P25286 | Atp6v0a1 | V-type proton ATPase 116 kDa subunit a 1 | Rattus norvegicus (Rat) | PR |
| P30628 | unc-32 | V-type proton ATPase 116 kDa subunit a 1 | Caenorhabditis elegans | PR |
| Q8RWZ7 | VHA-a1 | V-type proton ATPase subunit a1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9SJT7 | VHA-a2 | V-type proton ATPase subunit a2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q8W4S4 | VHA-a3 | V-type proton ATPase subunit a3 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| A1A5G6 | atp6v0a1 | V-type proton ATPase 116 kDa subunit a 1 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSLFRSESM | CLAQLFLQSG | TAYECLSALG | EKGLVQFRDL | NQNVSSFQRK | FVGEVKRCEE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LERILVYLVQ | EITRADIPLP | EGEASPPAPP | LKHVLEMQEQ | LQKLEVELRE | VTKNKEKLRK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NLLELVEYTH | MLRVTKTFLK | RNVEFEPTYE | EFPALENDSL | LDYSCMQRLG | AKLGFVSGLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QQGRVEAFER | MLWRACKGYT | IVTYAELDEC | LEDPETGEVI | KWYVFLISFW | GEQIGHKVKK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ICDCYHCHIY | PYPNTAEERR | EIQEGLNTRI | QDLYTVLHKT | EDYLRQVLCK | AAESVCSRVV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QVRKMKAIYH | MLNMCSFDVT | NKCLIAEVWC | PEVDLPGLRR | ALEEGSRESG | ATIPSFMNTI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PTKETPPTLI | RTNKFTEGFQ | NIVDAYGVGS | YREVNPALFT | IITFPFLFAV | MFGDFGHGFV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MFLFALLLVL | NENHPRLSQS | QEILRMFFDG | RYILLLMGLF | SVYTGLIYND | CFSKSVNLFG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SGWNVSAMYS | SSHSPEEQRK | MVLWNDSTIR | HSRTLQLDPN | IPGVFRGPYP | FGIDPIWNLA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TNRLTFLNSF | KMKMSVILGI | FHMTFGVVLG | IFNHLHFRKK | FNVYLVSVPE | ILFMLCIFGY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LIFMIIYKWL | AYSAETSREA | PSILIEFINM | FLFPTSKTHG | LYPGQAHVQR | VLVALTVLAV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PVLFLGKPLF | LLWLHNGRNC | FGMSRSGYTL | VRKDSEEEVS | LLGNQDIEEG | NSRMEEGCRE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VTCEEFNFGE | ILMTQAIHSI | EYCLGCISNT | ASYLRLWALS | LAHAQLSDVL | WAMLMRVGLR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| VDTTYGVLLL | LPVMAFFAVL | TIFILLVMEG | LSAFLHAIRL | HWVEFQNKFY | VGAGTKFVPF |
| 850 | |||||
| SFSLLSSKFS | NDDSIA |