UniProt ID | PGPLE_DROME | |
---|---|---|
UniProt AC | Q9VXN9 | |
Protein Name | Peptidoglycan-recognition protein LE | |
Gene Name | PGRP-LE | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 345 | |
Subcellular Localization | Secreted . However, no signal sequence are predicted by sequence analysis tools. | |
Protein Description | Peptidoglycan-recognition protein that plays a key role in innate immnunity by binding to murein peptidoglycans (PGN) of Gram-negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is required for infection-dependent activation of melanization. Required for Relish processing and nuclear translocation following proteolytic cleavage. Its localization suggests a role in the recognition and subsequent activation of the signaling at the first point of contact with invading bacteria.. | |
Protein Sequence | MSESGIKKLSQERTREWLASQEDEELESIAESSVVDSLDYDYTEEEEDADQNTSEEISTMTLGTQIATKKHSIISDTIRDLMNSINSIQTLGNVNISNSTNVHIGNVTNINGNIQIIADGLTQNRRDRRHVSPPRDNAPKTPTHFEDDYQDESEERVRSDVFIRRQKFKIPKELSAIIPRSSWLAQKPMDEPLPLQLPVKYVVILHTATESSEKRAINVRLIRDMQCFHIESRGWNDIAYNFLVGCDGNIYEGRGWKTVGAHTLGYNRISLGISFIGCFMKELPTADALNMCRNLLARGVEDGHISTDYRLICHCQCNSTESPGRRLYEEIQTWPHFYNIEEEEQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
52 | N-linked_Glycosylation | EEEDADQNTSEEIST CHHHCCCCCCHHHHH | 46.23 | - | |
72 | Phosphorylation | QIATKKHSIISDTIR HHHHCCCCHHHHHHH | 30.42 | 22817900 | |
95 | N-linked_Glycosylation | IQTLGNVNISNSTNV CCCCCCEEECCCCCE | 35.65 | - | |
98 | N-linked_Glycosylation | LGNVNISNSTNVHIG CCCEEECCCCCEEEC | 49.40 | - | |
106 | N-linked_Glycosylation | STNVHIGNVTNINGN CCCEEECCEEEECCC | 36.52 | - | |
132 | Phosphorylation | RRDRRHVSPPRDNAP CCHHCCCCCCCCCCC | 24.06 | 21082442 | |
141 | Phosphorylation | PRDNAPKTPTHFEDD CCCCCCCCCCCCCCC | 32.15 | 22817900 | |
159 | Phosphorylation | ESEERVRSDVFIRRQ HHHHHHHHHHHHHCC | 34.96 | 22817900 | |
318 | N-linked_Glycosylation | LICHCQCNSTESPGR EEEEEECCCCCCCCH | 26.53 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PGPLE_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PGPLE_DROME !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PGPLE_DROME !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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