Q6PGD0 · ARAID_MOUSE
- ProteinAll-trans retinoic acid-induced differentiation factor
- GeneAtraid
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids223 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Promotes osteoblast cell differentiation and terminal mineralization. Plays a role in inducing the cell cycle arrest via inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal pathway (By similarity).
In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol (PubMed:29745899).
In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol (PubMed:29745899).
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 | intracellular membrane-bounded organelle | |
Cellular Component | lysosomal membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | xenobiotic transmembrane transporter activity | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of osteoblast proliferation | |
Biological Process | negative regulation of protein catabolic process | |
Biological Process | positive regulation of bone mineralization | |
Biological Process | positive regulation of osteoblast differentiation | |
Biological Process | regulation of gene expression | |
Biological Process | xenobiotic transmembrane transport |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAll-trans retinoic acid-induced differentiation factor
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6PGD0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Lysosome membrane ; Multi-pass membrane protein
Note: Colocalizes with NELL1 on the nuclear envelope and the perinuclear region.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-193 | Extracellular | ||||
Sequence: LPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFS | ||||||
Transmembrane | 194-214 | Helical | ||||
Sequence: LLMFFGILGSTTLAISILLWG | ||||||
Topological domain | 215-223 | Cytoplasmic | ||||
Sequence: TQRRKAKAS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MASRESGGSRAAALLLVLGVERALA | ||||||
Chain | PRO_0000020753 | 26-223 | All-trans retinoic acid-induced differentiation factor | |||
Sequence: LPEICTLCPGGMHNLSRVAAYCEDTSKLMQARCCLNQKGTILGLDLQNCSLKDPGPNFLQAYTAIIIDLQANPLKDDLANTFRGFTQLQTLILPQDVPCPGGSNAWDNVTSFKDKQICQGQRDLCNSTGSPEMCPENGSCASDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGSTTLAISILLWGTQRRKAKAS | ||||||
Disulfide bond | 150↔165 | |||||
Sequence: CNSTGSPEMCPENGSC | ||||||
Disulfide bond | 159↔175 | |||||
Sequence: CPENGSCASDGPGLLQC | ||||||
Disulfide bond | 177↔186 | |||||
Sequence: CADGFHGYKC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with NELL1; the interaction promotes osteoblastic differentiation and mineralization (By similarity).
Interacts with SLC37A3; the interaction is direct and both proteins are mutually dependent for their stability (PubMed:29745899).
Interacts with SLC37A3; the interaction is direct and both proteins are mutually dependent for their stability (PubMed:29745899).
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q6PGD0-1
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
- Length223
- Mass (Da)23,858
- Last updated2004-10-11 v2
- Checksum1CB921F5F6D3E595
Q6PGD0-2
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
- Differences from canonical
- 37-223: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 23 | in Ref. 1; BAB21981 | ||||
Sequence: A → S | ||||||
Sequence conflict | 28 | in Ref. 1; BAB21981 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_039970 | 37-223 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 65 | in Ref. 1; BAB21981 | ||||
Sequence: T → P | ||||||
Sequence conflict | 70 | in Ref. 1; BAB21981 | ||||
Sequence: D → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK002276 EMBL· GenBank· DDBJ | BAB21981.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151307 EMBL· GenBank· DDBJ | BAE30289.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151366 EMBL· GenBank· DDBJ | BAE30340.1 EMBL· GenBank· DDBJ | mRNA | ||
AK169267 EMBL· GenBank· DDBJ | BAE41028.1 EMBL· GenBank· DDBJ | mRNA | ||
BC049637 EMBL· GenBank· DDBJ | AAH49637.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC057097 EMBL· GenBank· DDBJ | AAH57097.2 EMBL· GenBank· DDBJ | mRNA |