Q6NS82 · RETR2_MOUSE
- ProteinReticulophagy regulator 2
- GeneRetreg2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids541 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress (PubMed:34338405).
When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins (PubMed:34338405).
Required for collagen quality control in a LIR motif-independent manner (PubMed:34338405).
When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins (PubMed:34338405).
Required for collagen quality control in a LIR motif-independent manner (PubMed:34338405).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | endoplasmic reticulum-autophagosome adaptor activity | |
Biological Process | collagen catabolic process | |
Biological Process | endoplasmic reticulum organization | |
Biological Process | reticulophagy |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameReticulophagy regulator 2
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6NS82
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 10-30 | Helical | ||||
Sequence: GAGGTSGLGLGLGLSLGMGEA | ||||||
Transmembrane | 87-107 | Helical | ||||
Sequence: LFWLLSSSSLRPFFLLSISLL | ||||||
Transmembrane | 199-219 | Helical | ||||
Sequence: VPGVMISYIVLLSILLWPLVV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 487-490 | Abolishes interaction with ATG8 family proteins. Does not affect collagen degradation. | ||||
Sequence: FELL → AELA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000089347 | 1-541 | Reticulophagy regulator 2 | |||
Sequence: MASSGGGNTGAGGTSGLGLGLGLSLGMGEATGDAEEEAAAAEAVGRLATSLWLRLRGWEAVLAAAQRLLVWEKPLHSLVTAATLNGLFWLLSSSSLRPFFLLSISLLTYFLLDLWHPRFLPDVSAPPPEEPHSDSEGAGSGAQPHLLSVPELCRYLAESWLTFQIHLQELLQYKRQNPAQFCARGCAACAVLAVLGHYVPGVMISYIVLLSILLWPLVVYHELIQRMYTRLEPLLMQLDYSMKAEADALHHKHDKRKRQGKSAPPAGDEPLAETESESEAELAGFSPVVDVKKTALALAITDSELSDEEASILESGGFSVSRATTPQLTDVSEDLDQQSLPSEPEEALNRELGEGEETELASPEDLLSAPPALSKQALDTEEEGAADKEALLQLSSPLHFVNTHFNGAGSPQDGVKCPPGAPVKTLSPEAVSGDLMAPSSTLSPQLCLAESGPVTPLSPSVLPSLPQDSPQPLAAPEEEEALTTEDFELLDQGELEQLNAELGLGPEMPPKPPDVLPPPPLGADSHSLVQSDQEAHAEVEP | ||||||
Modified residue | 274 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 276 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 278 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 286 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 306 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 329 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 332 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 339 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 342 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with highest levels in brain, lung, heart, liver and kidney (at protein level) (PubMed:34338405).
Mainly expressed in the central nervous system and in parenchymatous organs including liver, lung and kidney
Mainly expressed in the central nervous system and in parenchymatous organs including liver, lung and kidney
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 249-282 | Disordered | ||||
Sequence: LHHKHDKRKRQGKSAPPAGDEPLAETESESEAEL | ||||||
Region | 331-369 | Disordered | ||||
Sequence: VSEDLDQQSLPSEPEEALNRELGEGEETELASPEDLLSA | ||||||
Region | 403-541 | Disordered | ||||
Sequence: THFNGAGSPQDGVKCPPGAPVKTLSPEAVSGDLMAPSSTLSPQLCLAESGPVTPLSPSVLPSLPQDSPQPLAAPEEEEALTTEDFELLDQGELEQLNAELGLGPEMPPKPPDVLPPPPLGADSHSLVQSDQEAHAEVEP | ||||||
Compositional bias | 434-448 | Polar residues | ||||
Sequence: DLMAPSSTLSPQLCL | ||||||
Motif | 485-490 | LIR motif | ||||
Sequence: EDFELL | ||||||
Compositional bias | 506-520 | Pro residues | ||||
Sequence: PEMPPKPPDVLPPPP |
Domain
The LIR motif interacts with ATG8 family proteins.
Sequence similarities
Belongs to the RETREG family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6NS82-1
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
- Length541
- Mass (Da)57,542
- Last updated2005-07-05 v2
- Checksum88C99862C92BAF10
Q6NS82-2
- Name2
Q6NS82-3
- Name3
- Differences from canonical
- 431-467: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087WNV4 | A0A087WNV4_MOUSE | Retreg2 | 173 | ||
A0A087WNS5 | A0A087WNS5_MOUSE | Retreg2 | 149 | ||
A0A087WPR9 | A0A087WPR9_MOUSE | Retreg2 | 490 | ||
A0A087WS58 | A0A087WS58_MOUSE | Retreg2 | 43 | ||
A0A087WRH7 | A0A087WRH7_MOUSE | Retreg2 | 84 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014550 | 1-226 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 139 | in Ref. 1; BAC28789 | ||||
Sequence: G → R | ||||||
Alternative sequence | VSP_014551 | 431-467 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 434-448 | Polar residues | ||||
Sequence: DLMAPSSTLSPQLCL | ||||||
Compositional bias | 506-520 | Pro residues | ||||
Sequence: PEMPPKPPDVLPPPP | ||||||
Sequence conflict | 515 | in Ref. 1; BAC28789 | ||||
Sequence: V → L | ||||||
Sequence conflict | 525 | in Ref. 1; BAE38485 | ||||
Sequence: S → C |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK034667 EMBL· GenBank· DDBJ | BAC28789.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK160400 EMBL· GenBank· DDBJ | BAE35769.1 EMBL· GenBank· DDBJ | mRNA | ||
AK165957 EMBL· GenBank· DDBJ | BAE38485.1 EMBL· GenBank· DDBJ | mRNA | ||
AK172093 EMBL· GenBank· DDBJ | BAE42822.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026519 EMBL· GenBank· DDBJ | AAH26519.1 EMBL· GenBank· DDBJ | mRNA | ||
BC038286 EMBL· GenBank· DDBJ | AAH38286.1 EMBL· GenBank· DDBJ | mRNA | ||
BC070406 EMBL· GenBank· DDBJ | AAH70406.1 EMBL· GenBank· DDBJ | mRNA |