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 Q28478
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q28478-F1 | Predicted | AlphaFoldDB |
No variants for Q28478
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q28478 | |||||
No associated diseases with Q28478
7 regional properties for Q28478
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | EGF-like domain | 612 - 645 | IPR000742 |
| domain | Peptidase M12B, ADAM/reprolysin | 178 - 375 | IPR001590 |
| domain | Disintegrin domain | 384 - 473 | IPR001762 |
| domain | Peptidase M12B, propeptide | 31 - 141 | IPR002870 |
| domain | ADAM, cysteine-rich domain | 472 - 609 | IPR006586 |
| conserved_site | Disintegrin, conserved site | 427 - 446 | IPR018358 |
| domain | Reprolysin domain, adamalysin-type | 178 - 373 | IPR034027 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
|---|---|
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| single fertilization | The union of male and female gametes to form a zygote. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MWRVLFLLSG | LGGLWMDSNF | DSLPVQITVP | EKIRSIIKEE | IESQVSYKIV | IEGKPYTANL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MQKNFLSHNF | RVYSYNGTGI | MKPLDQDFQN | FCHYQGYIEG | YPKSVAMVST | CTGLRGLLQF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ENVSYGIEPL | ESSVGFEHVI | YQVKHKKADV | SLYNEKDIES | RDLSFKLQSI | EPQKDFAKYI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EMHVVVEKQL | YNHMGSGTTV | VTQKIFQLIG | LTNAIFVSLN | ITVILSSLEL | WIDENKIATT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GDAKELLHTF | LRWKRSYLVL | RPHDVAFLLV | YREKSNYVGA | TFQGKMCDAN | YAGGVLLHPR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TISLESLAVI | LAQLLSLSMG | IPYDDINQCQ | CSAAVCIMNP | EAIHFSGVKI | FSNCSIEDFA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HFISKQKSQC | LHNQPRLDPF | FKQQAVCGNA | KLEAGEECDC | GTQQNCFLLG | AKCCDTATCR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FKAGSNCAEG | PCCENCLFMS | QERVCRPSFD | ECDLPEYCNG | TSASCPENHF | IQTGHPCGPN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QWVCIDGVCM | NGDKQCMDTF | GGEAEFGPTE | CYSYLNSKTD | VSGNCGIGDS | GYTQCEADNL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QCGKLICKYA | GEFLLQIPRA | TIIYANISGH | LCVAVEFASD | HEDSHKMWIK | DGTSCGSNKV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| CKNQRCVSSS | YLGYDCTTDK | CNHRGVCNNK | KHCHCSASYL | PPDCSVQSDT | SPGGSIDSGN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| FPLVAVPARL | PERRHMENVY | HSKPMRWPLF | LFIPFFIIFC | VLIAIMVKVH | FQRKKWRTED |
| 730 | |||||
| YSTDEQPESE | SEPKG |