P0C1T0
Gene name |
Mmel1 (Mell1, Nep2) |
Protein name |
Membrane metallo-endopeptidase-like 1 |
Names |
NEP2(m), Neprilysin II, NEPII, Neprilysin-2, NEP2, NL2 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
|
EC number |
3.4.24.11: 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 P0C1T0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0C1T0-F1 | Predicted | AlphaFoldDB |
No variants for P0C1T0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0C1T0 | |||||
No associated diseases with P0C1T0
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.24.11 | Metalloendopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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). |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
| 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P42892 | ECE1 | Endothelin-converting enzyme 1 | Homo sapiens (Human) | PR |
| P78562 | PHEX | Phosphate-regulating neutral endopeptidase PHEX | Homo sapiens (Human) | PR |
| P70669 | Phex | Phosphate-regulating neutral endopeptidase PHEX | Mus musculus (Mouse) | PR |
| Q22523 | nep-21 | Neprilysin-21 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGKSESSVGM | MERADNCGRR | RLGFVECGLL | VLLTLLLMGA | IVTLGVFYSI | GKQLPLLNSL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LHVSRHERTV | VKRVLRDSSQ | KSDICTTPSC | VIAAARILQN | MDQSKKPCDN | FYQYACGGWL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RHHVIPETNS | RYSVFDILRD | ELEVILKGVL | EDSSVQHRPA | VEKAKTLYRS | CMNQSVIEKR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSEPLLNVLD | MIGGWPVAMD | KWNETMGPKW | ELERQLAVLN | SQFNRRVLID | LFIWNDDQNS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SRHVIYIDQP | TLGMPSREYY | FKEDSHRVRE | AYLQFMTSVA | TMLRRDLNLP | GETDLVQEEM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AQVLHLETHL | ANATVPQEKR | HDVTALYHRM | GLEELQERFG | LKGFNWTLFI | QNVLSSVQVE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LLPNEEVVVY | GIPYLENLEE | IIDVFPAQTL | QNYLVWRLVL | DRIGSLSQRF | KEARVDYRKA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LYGTTMEEVR | WRECVSYVNS | NMESAVGSLY | IKRAFSKDSK | SIVSELIEKI | RSVFVDNLDE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LNWMDEESKK | KAQEKALNIR | EQIGYPDYIL | EDNNRHLDEE | YSSLTFSEDL | YFENGLQNLK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NNAQRSLKKL | REKVDQNLWI | IGAAVVNAFY | SPNRNLIVFP | AGILQPPFFS | KDQPQALNFG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GIGMVIGHEI | THGFDDNGRN | FDKNGNMLDW | WSNFSARHFR | QQSQCMIYQY | SNFSWELADN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QNVNGFSTLG | ENIADNGGVR | QAYKAYLQWL | AEGGRDQRLP | GLNLTYAQLF | FINYAQVWCG |
| 730 | 740 | 750 | 760 | 770 | |
| SYRPEFAIQS | IKTDVHSPLN | AQVLGSLQNL | PGFSEAFHCP | RGSPMHPMNR | CRIW |