Q5RAC8
Gene name |
MBTPS2 |
Protein name |
Membrane-bound transcription factor site-2 protease |
Names |
Endopeptidase S2P |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
|
EC number |
3.4.24.85: Metalloendopeptidases |
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 Q5RAC8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RAC8-F1 | Predicted | AlphaFoldDB |
No variants for Q5RAC8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RAC8 | |||||
No associated diseases with Q5RAC8
1 regional properties for Q5RAC8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M50 | 161 - 501 | IPR008915 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.24.85 | Metalloendopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| bone maturation | A developmental process, independent of morphogenetic (shape) change, that is required for bone to attain its fully functional state. |
| cholesterol metabolic process | The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIPVSLVVVV | VGGWTVVYLT | DLVLKSSVYF | KHSYEDWLES | NGLSISPFHI | RWQTAVFNRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FYSWGRRKAR | MLYQWFNFGM | VFGVIAMFSS | FFLLGKTLMQ | TLAQMMADSP | SSYSSSSSSS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSSSSSSSSS | SSSSSSSSLH | NEQVLQVVVP | GINLPVNQLT | YFFAAVLISG | VVHEIGHGIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AIREQVRFNG | FGIFLFIIYP | GAFVDLFTTH | LQLISPVQQL | RIFCAGIWHN | FVLALLGILA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LVLLPVILLP | FYYTGVGVLI | TEVAEDSPAI | GPRGLFVGDL | VTHLQDCPVT | NVQDWNECLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TIAYEPQIGY | CISASTLQQL | SFPVRAYKRL | DGSTECCNNH | SLTDVCFSYR | NNFNKRLHTC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LPARKAVEAT | QVCRTNKDCK | KSSSSSFCII | PSLETHTRLI | KVKHPPQIDM | LYVGHPLHLH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YTVSITSFIP | RFNFLSIDLP | VVVETFVKYL | ISLSGALAIV | NAVPCFALDG | QWILNSFLDA |
| 490 | 500 | 510 | 520 | ||
| TLTSVIGDND | VKDLIGFFIL | LGGSVLLAAN | VTLGLWMVTA | R |