Q8R5J9 · PRAF3_MOUSE
- ProteinPRA1 family protein 3
- GeneArl6ip5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids188 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates intracellular concentrations of taurine and glutamate (By similarity).
Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner (PubMed:12119102, PubMed:18684713).
Plays a role in the retention of SLC1A1/EAAC1 in the endoplasmic reticulum (By similarity).
Negatively modulates SLC1A1/EAAC1 glutamate transport activity by decreasing its affinity for glutamate in a PKC activity-dependent manner (PubMed:12119102, PubMed:18684713).
Plays a role in the retention of SLC1A1/EAAC1 in the endoplasmic reticulum (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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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePRA1 family protein 3
- Alternative names
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 accessionQ8R5J9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Cell membrane ; Multi-pass membrane protein
Note: Also exists as a soluble form in the cytoplasm. Associated with microtubules.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-39 | Cytoplasmic | ||||
Sequence: MDVNLAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSN | ||||||
Transmembrane | 40-60 | Helical | ||||
Sequence: LLYYQTNYLVVAAMMISVVGF | ||||||
Transmembrane | 64-84 | Helical | ||||
Sequence: FNMILGGVIVVLVFMGFVWAA | ||||||
Topological domain | 85-92 | Cytoplasmic | ||||
Sequence: HNKDILRR | ||||||
Transmembrane | 93-113 | Helical | ||||
Sequence: MKKQYPTAFVMVVMLASYFLI | ||||||
Transmembrane | 115-135 | Helical | ||||
Sequence: MFGGVMVFVFGITLPLLLMFI | ||||||
Topological domain | 136-188 | Cytoplasmic | ||||
Sequence: HASLRLRNLKNKLENKMEGIGLKKTPMGIILDALEQQEDNINKFADYISKARE |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 110 | Significant decrease in interaction with ARL6IP1 and no influence on SLC1A1/EAAC1-mediated glutamate transport; when associated with A-112. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 112 | Significant decrease in interaction with ARL6IP1 and no influence on SLC1A1/EAAC1-mediated glutamate transport; when associated with A-110. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000220884 | 1-188 | PRA1 family protein 3 | |||
Sequence: MDVNLAPLRAWDDFFPGSDRFARPDFRDISKWNNRVVSNLLYYQTNYLVVAAMMISVVGFLSPFNMILGGVIVVLVFMGFVWAAHNKDILRRMKKQYPTAFVMVVMLASYFLISMFGGVMVFVFGITLPLLLMFIHASLRLRNLKNKLENKMEGIGLKKTPMGIILDALEQQEDNINKFADYISKARE |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the cerebral cortex, cerebellum, hippocampus, olfactory bulbs, medulla oblongate and limbic system (at protein level) (PubMed:18684713).
Ubiquitous
Ubiquitous
Induction
By methyl-beta-cyclodextrin. Up-regulated upon chronic morphine injection, in amygdala only, other brain regions remain unaffected. Induction by morphine may affect glutamate uptake in the amygdala, causing mice to develop morphine tolerance and dependence (PubMed:12438930).
Was originally reported to be induced by retinoic acid (PubMed:12562531).
Was originally reported to be induced by retinoic acid (PubMed:12562531).
Gene expression databases
Interaction
Subunit
Homodimer. Heterodimer with ARL6IP1 (PubMed:18684713).
Forms multimers. Interacts with ARL6 (PubMed:10508919).
Interacts with prenylated RAB1A and RAB3A. Interacts with SLC1A1/EAAC1 (PubMed:12119102, PubMed:18684713).
Interacts with RTN2 (via first transmembrane domain) (By similarity).
Does not interact with VAMP1, VAMP2 or VAMP3 (By similarity).
Forms multimers. Interacts with ARL6 (PubMed:10508919).
Interacts with prenylated RAB1A and RAB3A. Interacts with SLC1A1/EAAC1 (PubMed:12119102, PubMed:18684713).
Interacts with RTN2 (via first transmembrane domain) (By similarity).
Does not interact with VAMP1, VAMP2 or VAMP3 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 103-117 | Required for homodimer formation and heterodimer formation with ARL6IP1 | ||||
Sequence: MVVMLASYFLISMFG | ||||||
Region | 136-188 | Targeting to endoplasmic reticulum membrane | ||||
Sequence: HASLRLRNLKNKLENKMEGIGLKKTPMGIILDALEQQEDNINKFADYISKARE |
Sequence similarities
Belongs to the PRA1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length188
- Mass (Da)21,558
- Last updated2005-01-04 v2
- Checksum5A679FC5071319F0
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11 | in Ref. 4; BAC40209 | ||||
Sequence: W → R | ||||||
Sequence conflict | 14 | in Ref. 4; BAC40209 | ||||
Sequence: F → S | ||||||
Sequence conflict | 19 | in Ref. 6 | ||||
Sequence: Missing | ||||||
Sequence conflict | 86 | in Ref. 6 | ||||
Sequence: Missing | ||||||
Sequence conflict | 103 | in Ref. 4; BAB25717 | ||||
Sequence: M → T | ||||||
Sequence conflict | 117 | in Ref. 6 | ||||
Sequence: G → R | ||||||
Sequence conflict | 140 | in Ref. 4; BAB25717 | ||||
Sequence: R → K | ||||||
Sequence conflict | 163 | in Ref. 1; AAL77876 | ||||
Sequence: G → V | ||||||
Sequence conflict | 178 | in Ref. 4; BAC40209 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF421860 EMBL· GenBank· DDBJ | AAL77876.1 EMBL· GenBank· DDBJ | mRNA | ||
D87211 EMBL· GenBank· DDBJ | BAC24103.1 EMBL· GenBank· DDBJ | mRNA | ||
AF265214 EMBL· GenBank· DDBJ | AAL74056.1 EMBL· GenBank· DDBJ | mRNA | ||
AK005259 EMBL· GenBank· DDBJ | BAB23912.1 EMBL· GenBank· DDBJ | mRNA | ||
AK008519 EMBL· GenBank· DDBJ | BAB25717.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088205 EMBL· GenBank· DDBJ | BAC40209.1 EMBL· GenBank· DDBJ | mRNA | ||
AK076519 EMBL· GenBank· DDBJ | BAC36376.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003897 EMBL· GenBank· DDBJ | AAH03897.1 EMBL· GenBank· DDBJ | mRNA | ||
AF133912 EMBL· GenBank· DDBJ | AAD33050.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |