Q60664 · IRAG2_MOUSE
- ProteinInositol 1,4,5-triphosphate receptor associated 2
- GeneIrag2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids539 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the delivery of peptides to major histocompatibility complex (MHC) class I molecules; this occurs in a transporter associated with antigen processing (TAP)-independent manner. May play a role in taste signal transduction via ITPR3. May play a role during fertilization in pronucleus congression and fusion (PubMed:9314557).
Plays a role in maintaining nuclear shape, maybe as a component of the LINC complex and through interaction with microtubules (PubMed:29878215).
Plays a role in the regulation of cellular excitability by regulating the hyperpolarization-activated cyclic nucleotide-gated HCN4 channel activity (PubMed:32647060).
Plays a role in maintaining nuclear shape, maybe as a component of the LINC complex and through interaction with microtubules (PubMed:29878215).
Plays a role in the regulation of cellular excitability by regulating the hyperpolarization-activated cyclic nucleotide-gated HCN4 channel activity (PubMed:32647060).
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 | centrosome | |
Cellular Component | chromosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | spindle pole | |
Molecular Function | microtubule binding | |
Biological Process | immune system process | |
Biological Process | nucleus organization | |
Biological Process | single fertilization |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameInositol 1,4,5-triphosphate receptor associated 2
- Alternative names
- Cleaved into 1 chains
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 accessionQ60664
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type IV membrane protein
Note: Colocalized with ITPR3 on the endoplasmic reticulum membrane.
Processed inositol 1,4,5-triphosphate receptor associated 2
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-479 | Cytoplasmic | ||||
Sequence: MLCVKGPPEQEPEDGALDVTRGCQCPLPTEDSILGQELLDCTRMNEDQSTDENGAGHFYSESPSQLREYLTQPSSEQTSSSESTVTSSESGSDILHMASGDLDCKPLCEKEEEARAASAMQGTSLAPAAYGDYTSVGVAKAASQLEAGEELRTTENGGKGSAPGETEISMPPKASVKLVNFQQSENTSANEKEVEAEFLRLSLGLKCDWFTLEKRVKLEERSRDLAEENLKKEITNCLKLLESLTPLCEEDNQAQEIVKKLEKSIVLLSQCTARVASRAEMLGAINQESRVSRAVEVMIQHVENLKRMYAKEHAELEDLKQALLQNDRSFNSLPDEDDCQIKKRSSSLNSKPSSLRRVTIASLPRNLGNVGLVSGMENNDRFSRRSSSWRILGTKQGEHRPSLHRFISTYSWADAEDERSDVKARDAPEPQGEEAVERTRKPSLSERRSSTLAWDRGTICSSVASWVTHLQASFRRANR | ||||||
Transmembrane | 480-500 | Helical; Anchor for type IV membrane protein | ||||
Sequence: ALWLTGLIIILIAALMSFLTG | ||||||
Topological domain | 501-539 | Lumenal | ||||
Sequence: QLFQTAVEAAPTQEGDSWLSLEHILWPFTRLGHDGPPPV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 480-539 | Results in cytosolic distribution. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000296245 | 1-? | Processed inositol 1,4,5-triphosphate receptor associated 2 | |||
Chain | PRO_0000084484 | 1-539 | Inositol 1,4,5-triphosphate receptor associated 2 | |||
Sequence: MLCVKGPPEQEPEDGALDVTRGCQCPLPTEDSILGQELLDCTRMNEDQSTDENGAGHFYSESPSQLREYLTQPSSEQTSSSESTVTSSESGSDILHMASGDLDCKPLCEKEEEARAASAMQGTSLAPAAYGDYTSVGVAKAASQLEAGEELRTTENGGKGSAPGETEISMPPKASVKLVNFQQSENTSANEKEVEAEFLRLSLGLKCDWFTLEKRVKLEERSRDLAEENLKKEITNCLKLLESLTPLCEEDNQAQEIVKKLEKSIVLLSQCTARVASRAEMLGAINQESRVSRAVEVMIQHVENLKRMYAKEHAELEDLKQALLQNDRSFNSLPDEDDCQIKKRSSSLNSKPSSLRRVTIASLPRNLGNVGLVSGMENNDRFSRRSSSWRILGTKQGEHRPSLHRFISTYSWADAEDERSDVKARDAPEPQGEEAVERTRKPSLSERRSSTLAWDRGTICSSVASWVTHLQASFRRANRALWLTGLIIILIAALMSFLTGQLFQTAVEAAPTQEGDSWLSLEHILWPFTRLGHDGPPPV | ||||||
Modified residue | 78 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 347 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 354 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 408 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
The removal of the C-terminal lumenal domain occurs by proteolytic processing.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Spleen and thymus. Expressed at high levels in pre B-cells, mature B-cells and pre T-cells. Expressed at low levels in mature T-cells and plasma B-cells. Expressed in circumvallate (CV), foliate (FL) and fungiform (FF) taste papillae cells of the tongue epithelium.
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MLCVKGPPEQEPEDGALDVTR | ||||||
Compositional bias | 69-94 | Polar residues | ||||
Sequence: YLTQPSSEQTSSSESTVTSSESGSDI | ||||||
Region | 69-98 | Disordered | ||||
Sequence: YLTQPSSEQTSSSESTVTSSESGSDILHMA | ||||||
Region | 147-171 | Disordered | ||||
Sequence: AGEELRTTENGGKGSAPGETEISMP | ||||||
Coiled coil | 298-326 | |||||
Sequence: MIQHVENLKRMYAKEHAELEDLKQALLQN | ||||||
Region | 334-353 | Disordered | ||||
Sequence: PDEDDCQIKKRSSSLNSKPS | ||||||
Compositional bias | 418-445 | Basic and acidic residues | ||||
Sequence: ERSDVKARDAPEPQGEEAVERTRKPSLS | ||||||
Region | 418-449 | Disordered | ||||
Sequence: ERSDVKARDAPEPQGEEAVERTRKPSLSERRS |
Sequence similarities
Belongs to the IRAG2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length539
- Mass (Da)59,588
- Last updated1996-11-01 v1
- Checksum4DA4639632E841F0
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31 | in Ref. 3; AAH52909 | ||||
Sequence: D → G | ||||||
Sequence conflict | 56-58 | in Ref. 3; AAH52909 | ||||
Sequence: GHF → DHL | ||||||
Compositional bias | 69-94 | Polar residues | ||||
Sequence: YLTQPSSEQTSSSESTVTSSESGSDI | ||||||
Sequence conflict | 195 | in Ref. 3; AAH52909 | ||||
Sequence: E → G | ||||||
Compositional bias | 418-445 | Basic and acidic residues | ||||
Sequence: ERSDVKARDAPEPQGEEAVERTRKPSLS | ||||||
Sequence conflict | 438 | in Ref. 3; AAH52909 | ||||
Sequence: R → G | ||||||
Sequence conflict | 532 | in Ref. 3; AAH52909 | ||||
Sequence: G → V | ||||||
Sequence conflict | 537 | in Ref. 3; AAH52909 | ||||
Sequence: P → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10484 EMBL· GenBank· DDBJ | AAA21603.1 EMBL· GenBank· DDBJ | mRNA | ||
AY753324 EMBL· GenBank· DDBJ | AAV31716.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052909 EMBL· GenBank· DDBJ | AAH52909.1 EMBL· GenBank· DDBJ | mRNA |