Q6UW15 · REG3G_HUMAN
- ProteinRegenerating islet-derived protein 3-gamma
- GeneREG3G
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids175 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota.
Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Is secreted by different cell types to activate its receptor EXTL3 and induce cell specific signaling pathways. Induced by IL17A in keratinocytes, regulates keratinocyte proliferation and differentiation after skin injury. In parallel, inhibits skin inflammation through the inhibition of inflammatory cytokines such as IL6 and TNF. Induced by IL22 in lung epithelial cells, inhibits cytokine production and regulates allergic airway inflammation. Induced in small intestine by inulin-enriched diet and Lactobacillus gasseri enriched microbiome, plays a role in the improvement of gut barrier function, the regulation of energy balance and glucose levels. Modulates microbiota composition in duodenal contents. Produced by nociceptor in response to endotoxins, prevents endotoxic death by targeting kynurenine pathway in microglia.
Regenerating islet-derived protein 3-gamma 16.5 kDa form
Has bacteriostatic activity.
Regenerating islet-derived protein 3-gamma 15 kDa form
Has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus.
Activity regulation
Regenerating islet-derived protein 3-gamma 15 kDa form
Lipopolysaccharide inhibits pore-forming activity, explaining why is bactericidal for Gram-positive but not Gram-negative bacteria.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | metal ion binding | |
Molecular Function | oligosaccharide binding | |
Molecular Function | peptidoglycan binding | |
Molecular Function | signaling receptor activity | |
Biological Process | acute-phase response | |
Biological Process | antimicrobial humoral immune response mediated by antimicrobial peptide | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | MyD88-dependent toll-like receptor signaling pathway | |
Biological Process | negative regulation of keratinocyte differentiation | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of keratinocyte proliferation | |
Biological Process | positive regulation of wound healing | |
Biological Process | response to peptide hormone |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegenerating islet-derived protein 3-gamma
- Short namesREG-3-gamma
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6UW15
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 371 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MLPPMALPSVSWMLLSCLILLCQVQG | ||||||
Propeptide | PRO_0000422751 | 27-37 | ||||
Sequence: EETQKELPSPR | ||||||
Chain | PRO_0000017434 | 27-175 | Regenerating islet-derived protein 3-gamma 16.5 kDa form | |||
Sequence: EETQKELPSPRISCPKGSKAYGSPCYALFLSPKSWMDADLACQKRPSGKLVSVLSGAEGSFVSSLVRSISNSYSYIWIGLHDPTQGSEPDGDGWEWSSTDVMNYFAWEKNPSTILNPGHCGSLSRSTGFLKWKDYNCDAKLPYVCKFKD | ||||||
Chain | PRO_0000422752 | 38-175 | Regenerating islet-derived protein 3-gamma 15 kDa form | |||
Sequence: ISCPKGSKAYGSPCYALFLSPKSWMDADLACQKRPSGKLVSVLSGAEGSFVSSLVRSISNSYSYIWIGLHDPTQGSEPDGDGWEWSSTDVMNYFAWEKNPSTILNPGHCGSLSRSTGFLKWKDYNCDAKLPYVCKFKD | ||||||
Disulfide bond | 40↔51 | |||||
Sequence: CPKGSKAYGSPC | ||||||
Disulfide bond | 68↔171 | |||||
Sequence: CQKRPSGKLVSVLSGAEGSFVSSLVRSISNSYSYIWIGLHDPTQGSEPDGDGWEWSSTDVMNYFAWEKNPSTILNPGHCGSLSRSTGFLKWKDYNCDAKLPYVC | ||||||
Disulfide bond | 146↔163 | |||||
Sequence: CGSLSRSTGFLKWKDYNC |
Post-translational modification
Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Regenerating islet-derived protein 3-gamma 15 kDa form
Forms a hexameric membrane-permeabilizing oligomeric pore on membrane phospholipids. The hexamer is formed by three dimers related by helical symmetry. Forms filaments, filamentation traps pore complexes and limits damage to host cells. Interacts with EXTL3.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-172 | C-type lectin | ||||
Sequence: YGSPCYALFLSPKSWMDADLACQKRPSGKLVSVLSGAEGSFVSSLVRSISNSYSYIWIGLHDPTQGSEPDGDGWEWSSTDVMNYFAWEKNPSTILNPGHCGSLSRSTGFLKWKDYNCDAKLPYVCK | ||||||
Region | 103-118 | Sufficient to activate EXTL3 | ||||
Sequence: WIGLHDPTQGSEPDGD | ||||||
Motif | 114-116 | EPN | ||||
Sequence: EPD |
Domain
The EPN motif is essential for recognition of the peptidoglycan carbohydrate backbone and for efficient bacterial killing with Glu-114 playing a key role in peptidoglycan binding and bactericidal activity.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q6UW15-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length175
- Mass (Da)19,330
- Last updated2004-07-05 v1
- ChecksumAF0F5FC59ACB90F5
Q6UW15-2
- Name2
- Differences from canonical
- 66-111: Missing
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045169 | 66-111 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 174 | in Ref. 4; CAG46736 | ||||
Sequence: K → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB161037 EMBL· GenBank· DDBJ | BAD51394.1 EMBL· GenBank· DDBJ | mRNA | ||
AB161038 EMBL· GenBank· DDBJ | BAD51396.1 EMBL· GenBank· DDBJ | mRNA | ||
AY428734 EMBL· GenBank· DDBJ | AAR88147.1 EMBL· GenBank· DDBJ | mRNA | ||
AY359047 EMBL· GenBank· DDBJ | AAQ89406.1 EMBL· GenBank· DDBJ | mRNA | ||
CR541938 EMBL· GenBank· DDBJ | CAG46736.1 EMBL· GenBank· DDBJ | mRNA | ||
AB161039 EMBL· GenBank· DDBJ | BAD51395.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK292595 EMBL· GenBank· DDBJ | BAF85284.1 EMBL· GenBank· DDBJ | mRNA | ||
AC017004 EMBL· GenBank· DDBJ | AAX88840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAW99580.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAW99581.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC103852 EMBL· GenBank· DDBJ | AAI03853.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103853 EMBL· GenBank· DDBJ | AAI03854.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103854 EMBL· GenBank· DDBJ | AAI03855.1 EMBL· GenBank· DDBJ | mRNA |