O09043
Gene name |
Napsa (Kdap, Nap) |
Protein name |
Napsin-A |
Names |
KDAP-1, Kidney-derived aspartic protease-like protein, KAP |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:16541 |
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
1 structures for O09043
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O09043-F1 | Predicted | AlphaFoldDB |
22 variants for O09043
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs260907547 | 4 | L>P | No | EVA | |
| rs239105084 | 36 | R>S | No | EVA | |
| rs3388907015 | 42 | N>K | No | EVA | |
| rs260190239 | 47 | L>V | No | EVA | |
| rs3388867010 | 57 | G>D | No | EVA | |
| rs3388866979 | 61 | S>A | No | EVA | |
| rs3388907072 | 81 | T>M | No | EVA | |
| rs3388907002 | 96 | N>Y | No | EVA | |
| rs3388904530 | 99 | V>A | No | EVA | |
| rs16785952 | 127 | P>T | No | EVA | |
| rs16785953 | 134 | I>V | No | EVA | |
| rs16785954 | 151 | T>N | No | EVA | |
| rs3388897016 | 153 | G>V | No | EVA | |
| rs16785967 | 222 | G>V | No | EVA | |
| rs16785968 | 243 | T>I | No | EVA | |
| rs3388906511 | 309 | F>L | No | EVA | |
| rs16793446 | 324 | H>R | No | EVA | |
| rs3388907042 | 355 | A>V | No | EVA | |
| rs217999864 | 375 | P>S | No | EVA | |
| rs3388904526 | 382 | R>C | No | EVA | |
| rs31476421 | 400 | S>A | No | EVA | |
| rs3388899211 | 403 | R>W | No | EVA |
No associated diseases with O09043
3 regional properties for O09043
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Aspartic peptidase, active site | 88 - 99 | IPR001969-1 |
| active_site | Aspartic peptidase, active site | 275 - 286 | IPR001969-2 |
| domain | Peptidase family A1 domain | 72 - 394 | IPR033121 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| alveolar lamellar body | A specialized secretory organelle found in type II pneumocytes and involved in the synthesis, secretion, and reutilization of pulmonary surfactant. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| lysosome | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartic-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. |
| endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| membrane protein proteolysis | The proteolytic cleavage of a transmembrane protein leading to the release of its intracellular or ecto-domains. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| surfactant homeostasis | Any process involved in the maintenance of a steady-state level of the surface-active lipoprotein mixture which coats the alveoli. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSPLLLLLLC | LLLGNLEPEE | AKLIRVPLQR | IHLGHRILNP | LNGWEQLAEL | SRTSTSGGNP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SFVPLSKFMN | TQYFGTIGLG | TPPQNFTVVF | DTGSSNLWVP | STRCHFFSLA | CWFHHRFNPK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ASSSFRPNGT | KFAIQYGTGR | LSGILSQDNL | TIGGIHDAFV | TFGEALWEPS | LIFALAHFDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ILGLGFPTLA | VGGVQPPLDA | MVEQGLLEKP | VFSFYLNRDS | EGSDGGELVL | GGSDPAHYVP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PLTFIPVTIP | AYWQVHMESV | KVGTGLSLCA | QGCSAILDTG | TSLITGPSEE | IRALNKAIGG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YPFLNGQYFI | QCSKTPTLPP | VSFHLGGVWF | NLTGQDYVIK | ILQSDVGLCL | LGFQALDIPK |
| 370 | 380 | 390 | 400 | 410 | |
| PAGPLWILGD | VFLGPYVAVF | DRGDKNVGPR | VGLARAQSRS | TDRAERRTTQ | AQFFKRRPG |