P70227 · ITPR3_MOUSE
- ProteinInositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- GeneItpr3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2670 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inositol 1,4,5-trisphosphate-gated calcium channel that, upon 1D-myo-inositol 1,4,5-trisphosphate binding, transports calcium from the endoplasmic reticulum lumen to cytoplasm, thus releasing the intracellular calcium and therefore participates in cellular calcium ion homeostasis (PubMed:15632133, PubMed:20813840, PubMed:9065779).
1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (By similarity).
Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (By similarity).
1D-myo-inositol 1,4,5-trisphosphate binds to the ligand-free channel without altering its global conformation, yielding the low-energy resting state, then progresses through resting-to preactivated transitions to the higher energy preactivated state, which increases affinity for calcium, promoting binding of the low basal cytosolic calcium at the juxtamembrane domain (JD) site, favoring the transition through the ensemble of high-energy intermediate states along the trajectory to the fully-open activated state (By similarity).
Upon opening, releases calcium in the cytosol where it can bind to the low-affinity cytoplasmic domain (CD) site and stabilizes the inhibited state to terminate calcium release (By similarity).
Catalytic activity
- Ca2+(in) = Ca2+(out)
Activity regulation
Inositol 1,4,5-trisphosphate-gated calcium channel is regulated by cytosolic calcium in a biphasic manner. At low concentrations, cytosolic calcium binds at a high-affinity juxtamembrane domain (JD) calcium binding site, allowing ITPR3 to activate by escaping a low-energy resting state through an ensemble of preactivated states. At high cytosolic calcium concentrations, ITPR3 preferentially enters an inhibited state stabilized by calcium binding at a second, low-affinity cytoplasmic domain (CD) calcium binding site.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 266 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 269 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 270 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 503 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 507 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 510 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 567 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 568 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 569 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 743 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: R | ||||||
Binding site | 1122 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: E | ||||||
Binding site | 1125 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: E | ||||||
Binding site | 1881 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 1945 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 1995 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 2148 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2151 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2537 | ATP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2537 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2538 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 2540 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2557 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2559 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2562 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2562 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2563 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 2564 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 2580 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: T |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- 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 accessionP70227
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Cytoplasmic vesicle, secretory vesicle membrane ; Multi-pass membrane protein
Note: Also localizes at mitochondria-associated membranes (MAMs).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-2233 | Cytoplasmic | ||||
Sequence: MNEMSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEKIADVVLLQKLQHAAQMEQKQNDTENKKVHGDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGNYLAAEENPSYKGDVSDPKAAGLGAQGRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDFANDASSMLASAVEKLNEGFISQNDRRFVIQLLEDLVFFVSDVPNNGQNVLDIMVTKPNRERQKLMREQNILKQIFGILKAPFRDKGGEGPLVRLEELSDQKNAPYQYMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAEDTITALLHNNRKLLEKHITKTEVETFVSLVRKNREPRFLDYLSDLCVSNRIAIPVTQELICKCVLDPKNSDILIQTELRPVKEMAQSHEYLSIEYSEEEVWLTWTDRNNEHHEKSVRQLAQEARAGNAHDENVLSYYRYQLKLFARMCLDRQYLAIDEISKQLGVELLFLCMADEMLPFDLRASFCHLMLHVHVDRDPQELVTPVKFARLWTEIPTAITIKDYDSNLNASRDDKKNKFASTMEFVEDYLNNVVSEAVPFANDEKNILTFEVVSLAHNLIYFGFYSFSELLRLTRTLLGIIDCIQAPAAMLQAYEEPGGKNVRRSIQGVGHMMSTMVLSRKQSVFGASSLPAGVGVPEQLDRSKFEDNEHTVVMETKLKILEILQFILNVRLDYRISYLLSVFKKEFVEVFPMQDSGADGTAPAFDSSTATMNLDRIGEQAEAMFGVGKTSSMLEVDDEGGRMFLRVLLHLTMHDYPSLVSGALQLLFKHFSQRQEAMHTFKQVQLLISAQDVENYKVIKSELDRLRTMVEKSELWVDKKGSVKGEEVEAGATKDKKERPSDEEGFLQPHGEKSSENYQIVKGILERLNKMCGVGEQMRKKQQRLLKNMDAHKVMLDLLQIPYDKSDNKMLEILRYTHQFLQKFCAGNPGNQALLHKHLQLFLTPGLLEAETMQHIFLNNYQLCSEISEPVLQHFVHLLATHGRHVQYLDFLHTVIKAEGKYVKKCQDMIMTELTNAGDDVVVFYNDKASLAHLLDMMKAARDGVEDHSPLMYHISLVDLLAACAEGKNVYTEIKCTSLLPLEDVVTVVTHEDCITEVKMAYVNFVNHCYVDTEVEMKEIYTSNHIWTLFENFTLDMALVCNKREKRLSDPTLEKYVLTVVLDTISAFFSSPFSENSTSLQTHQTIVVQLLQSTTRLLECPWLQQQHKGSVEACVRTLAMVAKSRAILLPMDLDAHMSALLSSGGSCSAAAQRSAANYKTATRTFPRVIPTANQWDYKNIIEKLQDIIMALEERLKPLVQAELSVLVDMLHWPELLFPEGSEAYQRCESGGFLSKLIRHTKGLMESEEKLCVKVLRTLQQMLLKKSKFGDRGNQLRKMLLQNYLQNRKSGARGELTDPTGSGLDQDWSAIAATQCRLDKEGATKLVCDLITSTKNEKIFQESIGLAIRLLDGGNTEIQKSFYNLMTSDKKSERFFKVLHDRMKRAQQETKSTVAVNMSDLGSQPREDREPADPATKGRVSSFSMPSSSRYLLGLGLHRGHDMSERAQNNEMGTSVLIMRPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDIMCGSTTGGLGLLGLYINEDNVGLVIQTLETLTEYCQGPCHENQTCIVTHESNGIDIITALILNDISPLCKYRMDLVLQLKDNASKLLLALMESRHDSENAERILISLRPQELVDVIKKAYLQEEERENSEVSPREVGHNIYILALQLSRHNKQLQHLLKPVRRIQEEEAEGISSMLSLNNKQLSQMLKSSAPAQEEEEDPLAYYENHTSQIEIVRQDRSMEQIVFPVPAICQFLTEETKHRLFTTTEQDEQGSKVSDFFDQSSFLHNEMEWQRRLRSMPLIYWFSRRMTLWGSISFNLAVFINIIIAFFYPYVEGASTGVL | ||||||
Transmembrane | 2234-2254 | Helical | ||||
Sequence: GSPLISLLFWILICFSIAALF | ||||||
Topological domain | 2255-2262 | Extracellular | ||||
Sequence: TKRYSVRP | ||||||
Transmembrane | 2263-2283 | Helical | ||||
Sequence: LIVALILRSIYYLGIGPTLNI | ||||||
Topological domain | 2284-2292 | Cytoplasmic | ||||
Sequence: LGALNLTNK | ||||||
Transmembrane | 2293-2310 | Helical | ||||
Sequence: IVFVVSFVGNRGTFIRGY | ||||||
Topological domain | 2311-2324 | Extracellular | ||||
Sequence: KAMVMDMEFLYHVG | ||||||
Transmembrane | 2325-2345 | Helical | ||||
Sequence: YILTSVLGLFAHELFYSILLF | ||||||
Topological domain | 2346-2367 | Cytoplasmic | ||||
Sequence: DLIYREETLFNVIKSVTRNGRS | ||||||
Transmembrane | 2368-2388 | Helical | ||||
Sequence: ILLTALLALILVYLFSIVGFL | ||||||
Topological domain | 2389-2495 | Extracellular | ||||
Sequence: FLKDDFILEVDRLPGNHSRASPLGMPHGAATFMGTCSGDKMDCVSEVSVPEILEEDEEPDSTERACDTLLMCIVTVMNHGLRNGGGVGDILRKPSKDESLFPARVVY | ||||||
Transmembrane | 2496-2516 | Helical | ||||
Sequence: DLLFFFIVIIIVLNLIFGVII | ||||||
Topological domain | 2517-2670 | Cytoplasmic | ||||
Sequence: DTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKLEHNMWNYLYFIVLVRVKNKTDYTGPESYVAQMIKNKNLDWFPRMRAMSLVSGEGEGEQNEIRILQEKLGSTMKLVSHLTSQLNELKEQMTEQRKRRQRLGFVDVQNCMSR |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 168 | Loss of calcium flux. | ||||
Sequence: W → A | ||||||
Mutagenesis | 507 | Loss of binding activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 510 | Loss of binding activity. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 130 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153929 | 1-2670 | Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3 | |||
Sequence: MNEMSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEKIADVVLLQKLQHAAQMEQKQNDTENKKVHGDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGNYLAAEENPSYKGDVSDPKAAGLGAQGRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDFANDASSMLASAVEKLNEGFISQNDRRFVIQLLEDLVFFVSDVPNNGQNVLDIMVTKPNRERQKLMREQNILKQIFGILKAPFRDKGGEGPLVRLEELSDQKNAPYQYMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAEDTITALLHNNRKLLEKHITKTEVETFVSLVRKNREPRFLDYLSDLCVSNRIAIPVTQELICKCVLDPKNSDILIQTELRPVKEMAQSHEYLSIEYSEEEVWLTWTDRNNEHHEKSVRQLAQEARAGNAHDENVLSYYRYQLKLFARMCLDRQYLAIDEISKQLGVELLFLCMADEMLPFDLRASFCHLMLHVHVDRDPQELVTPVKFARLWTEIPTAITIKDYDSNLNASRDDKKNKFASTMEFVEDYLNNVVSEAVPFANDEKNILTFEVVSLAHNLIYFGFYSFSELLRLTRTLLGIIDCIQAPAAMLQAYEEPGGKNVRRSIQGVGHMMSTMVLSRKQSVFGASSLPAGVGVPEQLDRSKFEDNEHTVVMETKLKILEILQFILNVRLDYRISYLLSVFKKEFVEVFPMQDSGADGTAPAFDSSTATMNLDRIGEQAEAMFGVGKTSSMLEVDDEGGRMFLRVLLHLTMHDYPSLVSGALQLLFKHFSQRQEAMHTFKQVQLLISAQDVENYKVIKSELDRLRTMVEKSELWVDKKGSVKGEEVEAGATKDKKERPSDEEGFLQPHGEKSSENYQIVKGILERLNKMCGVGEQMRKKQQRLLKNMDAHKVMLDLLQIPYDKSDNKMLEILRYTHQFLQKFCAGNPGNQALLHKHLQLFLTPGLLEAETMQHIFLNNYQLCSEISEPVLQHFVHLLATHGRHVQYLDFLHTVIKAEGKYVKKCQDMIMTELTNAGDDVVVFYNDKASLAHLLDMMKAARDGVEDHSPLMYHISLVDLLAACAEGKNVYTEIKCTSLLPLEDVVTVVTHEDCITEVKMAYVNFVNHCYVDTEVEMKEIYTSNHIWTLFENFTLDMALVCNKREKRLSDPTLEKYVLTVVLDTISAFFSSPFSENSTSLQTHQTIVVQLLQSTTRLLECPWLQQQHKGSVEACVRTLAMVAKSRAILLPMDLDAHMSALLSSGGSCSAAAQRSAANYKTATRTFPRVIPTANQWDYKNIIEKLQDIIMALEERLKPLVQAELSVLVDMLHWPELLFPEGSEAYQRCESGGFLSKLIRHTKGLMESEEKLCVKVLRTLQQMLLKKSKFGDRGNQLRKMLLQNYLQNRKSGARGELTDPTGSGLDQDWSAIAATQCRLDKEGATKLVCDLITSTKNEKIFQESIGLAIRLLDGGNTEIQKSFYNLMTSDKKSERFFKVLHDRMKRAQQETKSTVAVNMSDLGSQPREDREPADPATKGRVSSFSMPSSSRYLLGLGLHRGHDMSERAQNNEMGTSVLIMRPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDIMCGSTTGGLGLLGLYINEDNVGLVIQTLETLTEYCQGPCHENQTCIVTHESNGIDIITALILNDISPLCKYRMDLVLQLKDNASKLLLALMESRHDSENAERILISLRPQELVDVIKKAYLQEEERENSEVSPREVGHNIYILALQLSRHNKQLQHLLKPVRRIQEEEAEGISSMLSLNNKQLSQMLKSSAPAQEEEEDPLAYYENHTSQIEIVRQDRSMEQIVFPVPAICQFLTEETKHRLFTTTEQDEQGSKVSDFFDQSSFLHNEMEWQRRLRSMPLIYWFSRRMTLWGSISFNLAVFINIIIAFFYPYVEGASTGVLGSPLISLLFWILICFSIAALFTKRYSVRPLIVALILRSIYYLGIGPTLNILGALNLTNKIVFVVSFVGNRGTFIRGYKAMVMDMEFLYHVGYILTSVLGLFAHELFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGFLFLKDDFILEVDRLPGNHSRASPLGMPHGAATFMGTCSGDKMDCVSEVSVPEILEEDEEPDSTERACDTLLMCIVTVMNHGLRNGGGVGDILRKPSKDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKLEHNMWNYLYFIVLVRVKNKTDYTGPESYVAQMIKNKNLDWFPRMRAMSLVSGEGEGEQNEIRILQEKLGSTMKLVSHLTSQLNELKEQMTEQRKRRQRLGFVDVQNCMSR | ||||||
Modified residue | 916 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 934 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1813 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1832 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1834 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 2454↔2460 | |||||
Sequence: CDTLLMC | ||||||
Modified residue | 2608 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2669 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by AKT1 on serine and/or threonine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:20843799).
Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. Interacts with TRPV4 (By similarity).
Interacts with SIGMAR1 (PubMed:11149946).
Found in a complex with AKT1 and PML; this interaction modulates IP3R3-phosphorylation and in turn ITPR3-dependent calcium release (PubMed:21030605).
Interacts with IRAG2 (via coiled-coil domain) (PubMed:20071408).
Interacts with CABP1 (By similarity).
Interacts with TMBIM4/LFG4 (By similarity).
Interacts with CEMIP (By similarity).
Interacts with TESPA1 (PubMed:23650607).
Interacts with TMEM203 (By similarity).
Interacts with BOK; regulates ITPR3 expression (By similarity).
Interacts with BCL2L10 (By similarity).
Interacts with CHGA and CHGB (By similarity).
Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. Interacts with TRPV4 (By similarity).
Interacts with SIGMAR1 (PubMed:11149946).
Found in a complex with AKT1 and PML; this interaction modulates IP3R3-phosphorylation and in turn ITPR3-dependent calcium release (PubMed:21030605).
Interacts with IRAG2 (via coiled-coil domain) (PubMed:20071408).
Interacts with CABP1 (By similarity).
Interacts with TMBIM4/LFG4 (By similarity).
Interacts with CEMIP (By similarity).
Interacts with TESPA1 (PubMed:23650607).
Interacts with TMEM203 (By similarity).
Interacts with BOK; regulates ITPR3 expression (By similarity).
Interacts with BCL2L10 (By similarity).
Interacts with CHGA and CHGB (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 113-173 | MIR 1 | ||||
Sequence: GDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSN | ||||||
Domain | 174-224 | MIR 2 | ||||
Sequence: GDNVVVGDKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLF | ||||||
Domain | 232-288 | MIR 3 | ||||
Sequence: EEVLKGGDVVRLFHAEQEKFLTCDEYRGKLQVFLRTTLRQSATSATSSNALWEVEVV | ||||||
Domain | 295-372 | MIR 4 | ||||
Sequence: GGAGHWNGLYRFKHLATGNYLAAEENPSYKGDVSDPKAAGLGAQGRTGRRNAGEKIKYRLVAVPHGNDIASLFELDPT | ||||||
Domain | 378-434 | MIR 5 | ||||
Sequence: DSFVPRNSYVRLRHLCTNTWIQSTNAPIDVEEERPIRLMLGTCPTKEDKEAFAIVSV | ||||||
Compositional bias | 1138-1161 | Basic and acidic residues | ||||
Sequence: EVEAGATKDKKERPSDEEGFLQPH | ||||||
Region | 1138-1164 | Disordered | ||||
Sequence: EVEAGATKDKKERPSDEEGFLQPHGEK | ||||||
Region | 1807-1835 | Disordered | ||||
Sequence: NMSDLGSQPREDREPADPATKGRVSSFSM |
Domain
Composed of a large N-terminal cytoplasmic domain (CD) followed by a juxtamembrane domain (JD) and a transmembrane domain (TMD).
Sequence similarities
Belongs to the InsP3 receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,670
- Mass (Da)304,275
- Last updated2005-10-25 v3
- Checksum9B5BA808B195C58F
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1138-1161 | Basic and acidic residues | ||||
Sequence: EVEAGATKDKKERPSDEEGFLQPH | ||||||
Sequence conflict | 2406-2413 | in Ref. 4 | ||||
Sequence: SRASPLGM → FPPSRARR | ||||||
Sequence conflict | 2430 | in Ref. 4; M90088 | ||||
Sequence: D → E | ||||||
Sequence conflict | 2447 | in Ref. 4; M90088 | ||||
Sequence: P → L | ||||||
Sequence conflict | 2605-2609 | in Ref. 4; M90088 | ||||
Sequence: RAMSL → LGSTS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB182289 EMBL· GenBank· DDBJ | BAD90683.1 EMBL· GenBank· DDBJ | mRNA | ||
AK028491 EMBL· GenBank· DDBJ | BAC25977.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010323 EMBL· GenBank· DDBJ | AAH10323.1 EMBL· GenBank· DDBJ | mRNA | ||
M90088 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
Z71174 EMBL· GenBank· DDBJ | CAA94862.1 EMBL· GenBank· DDBJ | mRNA |