O75298 · RTN2_HUMAN
- ProteinReticulon-2
- GeneRTN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids545 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity).
Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell (By similarity).
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 | cell surface | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | intermediate filament | |
Cellular Component | sarcoplasmic reticulum membrane | |
Cellular Component | T-tubule | |
Cellular Component | terminal cisterna | |
Cellular Component | Z disc | |
Biological Process | gene expression | |
Biological Process | intracellular protein transmembrane transport | |
Biological Process | negative regulation of amyloid-beta formation | |
Biological Process | regulation of glucose import |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReticulon-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75298
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 368-388 | Helical | ||||
Sequence: LLCLLHFSIVSVAAHLALLLL | ||||||
Transmembrane | 463-483 | Helical | ||||
Sequence: LLFYILTFVGAIFNGLTLLIL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spastic paraplegia 12, autosomal dominant (SPG12)
- Note
- DescriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
- See alsoMIM:604805
Natural variants in SPG12
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067562 | 367 | S>F | in SPG12; dbSNP:rs140494585 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067562 | 367 | in SPG12; dbSNP:rs140494585 | |||
Sequence: S → F | ||||||
Natural variant | VAR_053632 | 425 | in dbSNP:rs35461805 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 651 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000030351 | 1-545 | UniProt | Reticulon-2 | |||
Sequence: MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEEDEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSTARRPRPQGRSVSEPRDQHPQPSLGDSLESIPSLSQSPEPGRRGDPDTAPPSERPLEDLRLRLDHLGWVARGTGSGEDSSTSSSTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLTPQLSPGSGTPQAGTPSPSRSRDSNSGPEEPLLEEEEKQWGPLEREPVRGQCLDSTDQLEFTVEPRLLGTAMEWLKTSLLLAVYKTVPILELSPPLWTAIGWVQRGPTPPTPVLRVLLKWAKSPRSSGVPSLSLGADMGSKVADLLYWKDTRTSGVVFTGLMVSLLCLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVHRGDGANPFQAYLDVDLTLTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGALASAAAAVSGSKAKAE | |||||||
Modified residue | 44 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 227 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform RTN2-C
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with BACE1 (PubMed:15286784).
Interacts (via first transmembrane domain) with ARL6IP5/GTRAP3-18 (By similarity).
Interacts (via N-terminus) with SLC1A1/EAAC1; the interaction promotes cell surface expression of SLC1A1 (By similarity).
Isoform RTN2-B
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75298 | RTN4 Q9NQC3 | 3 | EBI-2797962, EBI-715945 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-183 | Disordered | ||||
Sequence: MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEEDEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSTARRPRPQGRSVSEPRDQHPQPSLGDSLESIPSLSQSPEPGRRGDPDTAPPSERPLEDLRLRLDHLGWVARGTGSGEDSSTSSSTPLEDEEPQEPNRLETGE | ||||||
Compositional bias | 28-45 | Basic and acidic residues | ||||
Sequence: GNDDSDFRELHTAREFSE | ||||||
Compositional bias | 80-94 | Basic and acidic residues | ||||
Sequence: DSTARRPRPQGRSVS | ||||||
Compositional bias | 95-118 | Polar residues | ||||
Sequence: EPRDQHPQPSLGDSLESIPSLSQS | ||||||
Compositional bias | 127-146 | Basic and acidic residues | ||||
Sequence: PDTAPPSERPLEDLRLRLDH | ||||||
Compositional bias | 155-170 | Polar residues | ||||
Sequence: GSGEDSSTSSSTPLED | ||||||
Compositional bias | 199-229 | Polar residues | ||||
Sequence: SPEVLTPQLSPGSGTPQAGTPSPSRSRDSNS | ||||||
Region | 199-250 | Disordered | ||||
Sequence: SPEVLTPQLSPGSGTPQAGTPSPSRSRDSNSGPEEPLLEEEEKQWGPLEREP | ||||||
Compositional bias | 230-247 | Basic and acidic residues | ||||
Sequence: GPEEPLLEEEEKQWGPLE | ||||||
Domain | 345-545 | Reticulon | ||||
Sequence: VADLLYWKDTRTSGVVFTGLMVSLLCLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVHRGDGANPFQAYLDVDLTLTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGALASAAAAVSGSKAKAE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing & Alternative initiation.
O75298-1
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.
- NameRTN2-A
- Length545
- Mass (Da)59,264
- Last updated1998-11-01 v1
- Checksum971FD2F909E1E9E6
O75298-2
- NameRTN2-B
- Differences from canonical
- 272-344: Missing
O75298-3
- NameRTN2-C
- NoteProduced by alternative initiation at Met-341 of isoform RTN2-A.
- Differences from canonical
- 1-340: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018870 | 1-340 | in isoform RTN2-C | |||
Sequence: Missing | ||||||
Compositional bias | 28-45 | Basic and acidic residues | ||||
Sequence: GNDDSDFRELHTAREFSE | ||||||
Compositional bias | 80-94 | Basic and acidic residues | ||||
Sequence: DSTARRPRPQGRSVS | ||||||
Compositional bias | 95-118 | Polar residues | ||||
Sequence: EPRDQHPQPSLGDSLESIPSLSQS | ||||||
Compositional bias | 127-146 | Basic and acidic residues | ||||
Sequence: PDTAPPSERPLEDLRLRLDH | ||||||
Compositional bias | 155-170 | Polar residues | ||||
Sequence: GSGEDSSTSSSTPLED | ||||||
Compositional bias | 199-229 | Polar residues | ||||
Sequence: SPEVLTPQLSPGSGTPQAGTPSPSRSRDSNS | ||||||
Compositional bias | 230-247 | Basic and acidic residues | ||||
Sequence: GPEEPLLEEEEKQWGPLE | ||||||
Alternative sequence | VSP_005649 | 272-344 | in isoform RTN2-B | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF004222 EMBL· GenBank· DDBJ | AAC32542.1 EMBL· GenBank· DDBJ | mRNA | ||
AF004223 EMBL· GenBank· DDBJ | AAC32543.1 EMBL· GenBank· DDBJ | mRNA | ||
AF004224 EMBL· GenBank· DDBJ | AAC32544.1 EMBL· GenBank· DDBJ | mRNA | ||
AF038540 EMBL· GenBank· DDBJ | AAC14910.1 EMBL· GenBank· DDBJ | mRNA | ||
BK001686 EMBL· GenBank· DDBJ | DAA01944.1 EMBL· GenBank· DDBJ | mRNA | ||
BK001687 EMBL· GenBank· DDBJ | DAA01932.1 EMBL· GenBank· DDBJ | mRNA | ||
BK001688 EMBL· GenBank· DDBJ | DAA01933.1 EMBL· GenBank· DDBJ | mRNA |