O57382
Gene name |
tll2 (xld) |
Protein name |
Tolloid-like protein 2 |
Names |
Metalloprotease xolloid, Xenopus tolloid |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:399469 |
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 O57382
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O57382-F1 | Predicted | AlphaFoldDB |
No variants for O57382
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O57382 | |||||
No associated diseases with O57382
16 regional properties for O57382
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| ptm | EGF-type aspartate/asparagine hydroxylation site | 595 - 606 | IPR000152-1 |
| ptm | EGF-type aspartate/asparagine hydroxylation site | 750 - 761 | IPR000152-2 |
| domain | EGF-like domain | 579 - 620 | IPR000742-1 |
| domain | EGF-like domain | 738 - 775 | IPR000742-2 |
| domain | CUB domain | 354 - 466 | IPR000859-1 |
| domain | CUB domain | 467 - 579 | IPR000859-2 |
| domain | CUB domain | 623 - 735 | IPR000859-3 |
| domain | CUB domain | 779 - 891 | IPR000859-4 |
| domain | CUB domain | 892 - 1008 | IPR000859-5 |
| domain | Peptidase M12A | 153 - 352 | IPR001506 |
| domain | EGF-like calcium-binding domain | 579 - 620 | IPR001881-1 |
| domain | EGF-like calcium-binding domain | 735 - 775 | IPR001881-2 |
| domain | Peptidase, metallopeptidase | 158 - 300 | IPR006026 |
| conserved_site | EGF-like calcium-binding, conserved site | 579 - 604 | IPR018097-1 |
| conserved_site | EGF-like calcium-binding, conserved site | 735 - 759 | IPR018097-2 |
| domain | Tolloid/BMP1 peptidase domain | 153 - 352 | IPR034036 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| 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 |
|---|---|
| cell differentiation | The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state. |
| 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 |
| MSCGSPQVMM | TLWTLTCVGL | ILLGAIRLSL | GLDYDLESFD | YLMEDNPEEF | DYKDPCKAAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YWGDIALDED | DLKWIFKNKS | NDLRNTRHNQ | THPTTDNFSE | KLGTGSQNET | SSNLNSKKVK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KGSRLKLLIA | EKAATETNST | FQVQTSNDRV | RRAATSRTER | IWPGGIIPYA | IAGNFTGTQR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AIFKQAMRHW | KKHTCVTFVE | RTDEESFIVF | TYRPCGCCSY | VGRRGGGPQA | ISIGKNCDKF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIVVHELGHV | VGFWHEHTRP | DRDEHVSIIR | ENIQPGQEYN | FLKMEPGEVS | SLGETYDFDS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IMHYARNTFS | RGVFLDTILP | RRIDTSVRPT | IGQRIRLSQG | DIAQAKKLYK | CPACGETLQD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SSGNFSAPGY | PSGYPSYTHC | IWRISVTPGE | KIILNFTTMD | LFKSRLCWYD | YIEIRDGYWR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KAALLGRLCG | DKLPDPIISS | DSKLWIEFRS | SSNILGKGFF | AAYEAICGGD | IKKDSGQIQS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PNYPDDYRPA | KECIWKITVS | EGFLVGLSFQ | AFEIERHDNC | AYDYLEVRDG | FSEDHALIGR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FCGYEKPEDI | KSTSNKLWIK | FASDGSINKA | GFSANFFKEM | DECSRPDNGG | CSQRCVNTLG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SYKCVCEPGF | ELTADKKSCE | AACGGFITQL | NGTITSPGWP | KEYPTNKNCV | WQVVAPAQYR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ISLQFEVFEL | EGNDVCKYDY | LEIRSGLSSE | SKLHGKFCGP | EKPEVITSQG | NTVRIEFKSD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NTVSKKGFKA | NFFSDKDECS | KDNGGCQHDC | VNTFGSYICQ | CKNGFILHEN | GHDCKEAGCE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| QKLLNAEGTI | SSPNWPEKYP | SRKECTWDIS | VTAGHRVKLV | FTDFEIEQHQ | ECAYDHLELY |
| 850 | 860 | 870 | 880 | 890 | 900 |
| DGPNGKAAIL | GRFCGSKEPS | PVVASTNNMF | LRFYSDASVQ | RKGFQAKYSP | ECGGRLKAEI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| QTNDIYSHAQ | FGDNNYPVQS | NCEWVIVAED | GYGVELIFQT | FEIEEESDCG | YDYMEVYDGY |
| 970 | 980 | 990 | 1000 | 1010 | |
| DSTAPRLGRY | CGSGPPEEMY | SAGDSIMIRF | HTDDTINKKG | FHGQYTSTKF | QDALHMRRK |