Q6RJR6 · RTN3_RAT
- ProteinReticulon-3
- GeneRtn3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids940 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules. Acts also as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition.
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 | glutamatergic synapse | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | neuron projection | |
Cellular Component | postsynaptic density | |
Cellular Component | presynapse | |
Cellular Component | synapse | |
Biological Process | apoptotic process | |
Biological Process | brain development | |
Biological Process | endoplasmic reticulum tubular network formation | |
Biological Process | endoplasmic reticulum tubular network organization | |
Biological Process | negative regulation of amyloid-beta formation | |
Biological Process | neuron differentiation | |
Biological Process | vesicle-mediated transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReticulon-3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ6RJR6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Golgi apparatus membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-771 | Cytoplasmic | ||||
Sequence: AESSAATQSPSVSSSSSGAEPSTLGGGGGSPGACPALGAKSCGSSCAVGLSSLCSDEPPSKIMTSSFLSSSEIYNPDPTTPLGSETLGSHLVAKDGKDPLVLLDKKTLDSPQGTNKDRVDTPVSLAADIPCSHPSIPDSFPEQPTFLSKETDPTEEWVVKNQEPKNPSEVPSGEDRSALDLGQRKAEHICTHSLSPSEPAVASVEKDSPESPFEVIIDKATFDREFKDLYKESTDDLGGWAAHGDRESPADLLEMNDKVFPLRNKEAGRYPSSALLGRQFSHTTAALEEVSRCVNDMHNFTNEILTWDLDPQAKQQADKSPCTTESTGLDRSEHRSEIPVINLKTSPQQKMPVCSFNGSTPITRSTGDWTETFTEGKPVKGYLSSTKEAGGKGVPDSSQPISGSGAATVEVTLPDLRGTWPNSVLGEVTEVDSSGESDDTVIEDTTENPSVKNNKVLPEKSDSLPSAAVKTSERENKETTSHETVRSEMYENSEQQQAHAETPTQRSLEGQMSPQVPNMLNEVIPENLAMTDTTRVCSAAPPSVLSETGFSLTVPASAKSESLLGKNVEDTDGSSPEDLMAALTGTEEKGTVDKEKGDVLEAVLEKIANVKNTLPVELLHENKLSSSETKNTKSKYSEHSRETNGGAPKVSSDLEQEQLTIRAIKELGAKQVQAERMSPGGKLKRTFDPQSGPQNSSDILEHTDITTGSDLGIPKKPTIIKDTRIDSISSLTKTETVNKHVLARLLSDFPVHDLIFWRDVKKTGFVFGTT | ||||||
Intramembrane | 772-795 | Helical | ||||
Sequence: LIMLLSLAAFSVISVVSYLILALL | ||||||
Topological domain | 796-852 | Cytoplasmic | ||||
Sequence: SVTISFRVYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHSYMNAAMVHVNKALKL | ||||||
Intramembrane | 853-875 | Helical | ||||
Sequence: IIRLFLVEDLVDSLKLAVFMWLM | ||||||
Topological domain | 876-879 | Cytoplasmic | ||||
Sequence: TYVG | ||||||
Intramembrane | 880-902 | Helical | ||||
Sequence: AVFNGITLLILAELLVFSVPIVY | ||||||
Topological domain | 903-940 | Cytoplasmic | ||||
Sequence: EKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000280541 | 2-940 | Reticulon-3 | |||
Sequence: AESSAATQSPSVSSSSSGAEPSTLGGGGGSPGACPALGAKSCGSSCAVGLSSLCSDEPPSKIMTSSFLSSSEIYNPDPTTPLGSETLGSHLVAKDGKDPLVLLDKKTLDSPQGTNKDRVDTPVSLAADIPCSHPSIPDSFPEQPTFLSKETDPTEEWVVKNQEPKNPSEVPSGEDRSALDLGQRKAEHICTHSLSPSEPAVASVEKDSPESPFEVIIDKATFDREFKDLYKESTDDLGGWAAHGDRESPADLLEMNDKVFPLRNKEAGRYPSSALLGRQFSHTTAALEEVSRCVNDMHNFTNEILTWDLDPQAKQQADKSPCTTESTGLDRSEHRSEIPVINLKTSPQQKMPVCSFNGSTPITRSTGDWTETFTEGKPVKGYLSSTKEAGGKGVPDSSQPISGSGAATVEVTLPDLRGTWPNSVLGEVTEVDSSGESDDTVIEDTTENPSVKNNKVLPEKSDSLPSAAVKTSERENKETTSHETVRSEMYENSEQQQAHAETPTQRSLEGQMSPQVPNMLNEVIPENLAMTDTTRVCSAAPPSVLSETGFSLTVPASAKSESLLGKNVEDTDGSSPEDLMAALTGTEEKGTVDKEKGDVLEAVLEKIANVKNTLPVELLHENKLSSSETKNTKSKYSEHSRETNGGAPKVSSDLEQEQLTIRAIKELGAKQVQAERMSPGGKLKRTFDPQSGPQNSSDILEHTDITTGSDLGIPKKPTIIKDTRIDSISSLTKTETVNKHVLARLLSDFPVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRVYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHSYMNAAMVHVNKALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLVFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE | ||||||
Modified residue | 31 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 196 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 212 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 249 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 282 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 508 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 572 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 575 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 576 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 652 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Present in olfactory bulb, olfactory epithelium and retina (at protein level).
Developmental stage
In the optic nerve, expressed more abundantly in the embryo than in the adult.
Gene expression databases
Interaction
Subunit
Homodimer. Interacts with RTN4. Isoform 2 interacts with BACE1, BACE2, BCL2 and FADD. Interacts with ATL2. Interacts with TMEM33 (By similarity).
Interacts with ATL1 (PubMed:19665976).
Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (By similarity).
Interacts with RIGI. Interacts with TRIM25 (By similarity).
Interacts with ATL1 (PubMed:19665976).
Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (By similarity).
Interacts with RIGI. Interacts with TRIM25 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-24 | Polar residues | ||||
Sequence: MAESSAATQSPSVSSSSSGAEPST | ||||||
Region | 1-32 | Disordered | ||||
Sequence: MAESSAATQSPSVSSSSSGAEPSTLGGGGGSP | ||||||
Compositional bias | 71-87 | Polar residues | ||||
Sequence: SSEIYNPDPTTPLGSET | ||||||
Region | 71-91 | Disordered | ||||
Sequence: SSEIYNPDPTTPLGSETLGSH | ||||||
Region | 129-182 | Disordered | ||||
Sequence: DIPCSHPSIPDSFPEQPTFLSKETDPTEEWVVKNQEPKNPSEVPSGEDRSALDL | ||||||
Region | 314-335 | Disordered | ||||
Sequence: AKQQADKSPCTTESTGLDRSEH | ||||||
Region | 381-405 | Disordered | ||||
Sequence: KGYLSSTKEAGGKGVPDSSQPISGS | ||||||
Region | 428-512 | Disordered | ||||
Sequence: EVTEVDSSGESDDTVIEDTTENPSVKNNKVLPEKSDSLPSAAVKTSERENKETTSHETVRSEMYENSEQQQAHAETPTQRSLEGQ | ||||||
Compositional bias | 445-471 | Polar residues | ||||
Sequence: DTTENPSVKNNKVLPEKSDSLPSAAVK | ||||||
Compositional bias | 472-490 | Basic and acidic residues | ||||
Sequence: TSERENKETTSHETVRSEM | ||||||
Compositional bias | 491-512 | Polar residues | ||||
Sequence: YENSEQQQAHAETPTQRSLEGQ | ||||||
Region | 623-655 | Disordered | ||||
Sequence: NKLSSSETKNTKSKYSEHSRETNGGAPKVSSDL | ||||||
Compositional bias | 624-643 | Basic and acidic residues | ||||
Sequence: KLSSSETKNTKSKYSEHSRE | ||||||
Region | 672-701 | Disordered | ||||
Sequence: QVQAERMSPGGKLKRTFDPQSGPQNSSDIL | ||||||
Domain | 752-940 | Reticulon | ||||
Sequence: VHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRVYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHSYMNAAMVHVNKALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLVFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE | ||||||
Region | 895-940 | Interaction with FADD | ||||
Sequence: VFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE | ||||||
Region | 908-910 | Interaction with BACE1 | ||||
Sequence: QID |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6RJR6-1
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
- Length940
- Mass (Da)101,517
- Last updated2004-07-05 v1
- Checksum701B0CF84473D36B
Q6RJR6-2
- Name2
- Differences from canonical
- 49-751: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6ASN6 | A0A8I6ASN6_RAT | Rtn3 | 959 | ||
A0A8I6AFX0 | A0A8I6AFX0_RAT | Rtn3 | 256 | ||
A0A0H2UHX1 | A0A0H2UHX1_RAT | Rtn3 | 297 | ||
A0A8I6G4J6 | A0A8I6G4J6_RAT | Rtn3 | 208 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-24 | Polar residues | ||||
Sequence: MAESSAATQSPSVSSSSSGAEPST | ||||||
Sequence conflict | 26 | in Ref. 1; AAP47276 and 2; AAL35353/AAL35354 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_023771 | 49-751 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 71-87 | Polar residues | ||||
Sequence: SSEIYNPDPTTPLGSET | ||||||
Compositional bias | 445-471 | Polar residues | ||||
Sequence: DTTENPSVKNNKVLPEKSDSLPSAAVK | ||||||
Compositional bias | 472-490 | Basic and acidic residues | ||||
Sequence: TSERENKETTSHETVRSEM | ||||||
Compositional bias | 491-512 | Polar residues | ||||
Sequence: YENSEQQQAHAETPTQRSLEGQ | ||||||
Compositional bias | 624-643 | Basic and acidic residues | ||||
Sequence: KLSSSETKNTKSKYSEHSRE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY164698 EMBL· GenBank· DDBJ | AAP47276.1 EMBL· GenBank· DDBJ | mRNA | ||
AY496443 EMBL· GenBank· DDBJ | AAR89918.1 EMBL· GenBank· DDBJ | mRNA | ||
AF442357 EMBL· GenBank· DDBJ | AAL35353.1 EMBL· GenBank· DDBJ | mRNA | ||
AF442358 EMBL· GenBank· DDBJ | AAL35354.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062068 EMBL· GenBank· DDBJ | AAH62068.1 EMBL· GenBank· DDBJ | mRNA | ||
BC107448 EMBL· GenBank· DDBJ | AAI07449.1 EMBL· GenBank· DDBJ | mRNA |