Q5I2A0
PR
Gene name |
Serpina3g (Spi2A) |
Protein name |
Serine protease inhibitor A3G |
Names |
Serpin A3G, Serine protease inhibitor 2A, Serpin 2A |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:20715 |
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 Q5I2A0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5I2A0-F1 | Predicted | AlphaFoldDB |
No variants for Q5I2A0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5I2A0 | |||||
No associated diseases with Q5I2A0
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cysteine-type endopeptidase inhibitor activity | Binds to and stops, prevents or reduces the activity of a cysteine-type endopeptidase, any enzyme that hydrolyzes peptide bonds in polypeptides by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. |
| serine-type endopeptidase inhibitor activity | Binds to and stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| adaptive immune response | An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory). |
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| negative regulation of endopeptidase activity | Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins. |
| response to cytokine | 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 cytokine stimulus. |
| response to peptide hormone | 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 peptide hormone stimulus. A peptide hormone is any of a class of peptides that are secreted into the blood stream and have endocrine functions in living animals. |
37 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9N2I2 | SERPINA5 | Plasma serine protease inhibitor | Bos taurus (Bovine) | PR |
| P41361 | SERPINC1 | Antithrombin-III | Bos taurus (Bovine) | PR |
| Q1JPB0 | SERPINB1 | Leukocyte elastase inhibitor | Bos taurus (Bovine) | PR |
| P13909 | SERPINE1 | Plasminogen activator inhibitor 1 | Bos taurus (Bovine) | PR |
| A2I7N1 | SERPINA3-5 | Serpin A3-5 | Bos taurus (Bovine) | PR |
| A6QPQ2 | SERPINA3-8 | Serpin A3-8 | Bos taurus (Bovine) | PR |
| A2I7N2 | SERPINA3-6 | Serpin A3-6 | Bos taurus (Bovine) | PR |
| A2I7M9 | SERPINA3-2 | Serpin A3-2 | Bos taurus (Bovine) | PR |
| Q9TTE1 | SERPINA3-1 | Serpin A3-1 | Bos taurus (Bovine) | PR |
| O73790 | SERPINB10 | Heterochromatin-associated protein MENT | Gallus gallus (Chicken) | PR |
| P05121 | SERPINE1 | Plasminogen activator inhibitor 1 | Homo sapiens (Human) | PR |
| Q9UK55 | SERPINA10 | Protein Z-dependent protease inhibitor | Homo sapiens (Human) | PR |
| P05155 | SERPING1 | Plasma protease C1 inhibitor | Homo sapiens (Human) | PR |
| P08697 | SERPINF2 | Alpha-2-antiplasmin | Homo sapiens (Human) | PR |
| Q86WD7 | SERPINA9 | Serpin A9 | Homo sapiens (Human) | PR |
| P01008 | SERPINC1 | Antithrombin-III | Homo sapiens (Human) | PR |
| P07093 | SERPINE2 | Glia-derived nexin | Homo sapiens (Human) | PR |
| Q96P15 | SERPINB11 | Serpin B11 | Homo sapiens (Human) | PR |
| P01011 | SERPINA3 | Alpha-1-antichymotrypsin | Homo sapiens (Human) | PR |
| P12388 | Serpinb2 | Plasminogen activator inhibitor 2, macrophage | Mus musculus (Mouse) | PR |
| P22777 | Serpine1 | Plasminogen activator inhibitor 1 | Mus musculus (Mouse) | PR |
| P32261 | Serpinc1 | Antithrombin-III | Mus musculus (Mouse) | PR |
| Q07235 | Serpine2 | Glia-derived nexin | Mus musculus (Mouse) | PR |
| Q5SV42 | Serpinb1c | Leukocyte elastase inhibitor C | Mus musculus (Mouse) | PR |
| Q80X76 | Serpina3f | Serine protease inhibitor A3F | Mus musculus (Mouse) | PR |
| Q8BYY9 | Serpina3b | Serine protease inhibitor A3B | Mus musculus (Mouse) | PR |
| Q8CDC0 | Serpinb13 | Serpin B13 | Mus musculus (Mouse) | PR |
| Q9D154 | Serpinb1a | Leukocyte elastase inhibitor A | Mus musculus (Mouse) | PR |
| Q9JK88 | Serpini2 | Serpin I2 | Mus musculus (Mouse) | PR |
| P29524 | Serpinb2 | Plasminogen activator inhibitor 2 type A | Rattus norvegicus (Rat) | PR |
| Q6P734 | Serping1 | Plasma protease C1 inhibitor | Rattus norvegicus (Rat) | PR |
| P05545 | Serpina3k | Serine protease inhibitor A3K | Rattus norvegicus (Rat) | PR |
| P07092 | Serpine2 | Glia-derived nexin | Rattus norvegicus (Rat) | PR |
| Q62975 | Serpina10 | Protein Z-dependent protease inhibitor | Rattus norvegicus (Rat) | PR |
| O48706 | At2g26390 | Serpin-Z3 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9M1T7 | At3g45220 | Serpin-Z4 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9ZQR6 | At2g14540 | Serpin-Z2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGVSPAVFG | CPDVTLGRNT | AVREVQENVT | SVDSLTLVSS | NTDFAFSLYR | KLVLKNPDEN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVFSPFSICT | ALALLSLGAK | SNTLKEILEG | LKFNLTETPE | PDIHQGFRYL | LDLLSQPGNQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VQISTGSALF | IEKHLQILAE | FKEKARALYQ | AEAFTADFQQ | PLKATKLIND | YVSNHTQGKI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KELISGLKES | TLMVLVNYIY | FKGKWKNPFD | PNDTFKSEFY | LDEKRSVIVS | MMKTGYLTTP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YFRDEELSCT | VVELKYTGNA | SAMFILPDQG | RMQQVEASLQ | PETLRKWKNS | LKPRMIHELR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPKFSISTDY | SLEHILPELG | IREVFSTQAD | LSAITGTKDL | RVSQVVHKAV | LDVAETGTEA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AAATGMAGVG | CCAVFDFLEI | FFNRPFLMII | SDTKAHIALF | MAKVTNPERS | MNFPNGEGAS |
| 430 | |||||
| SQRLESKRLC | FGDPLCLIGQ |