P11881 · ITPR1_MOUSE
- ProteinInositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- GeneItpr1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2749 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Undergoes conformational changes upon ligand binding, suggesting structural flexibility that allows the channel to switch from a closed state, capable of interacting with its ligands such as inositol 1,4,5-trisphosphate and Ca2+, to an open state, capable of transferring calcium ions across the ER membrane (By similarity).
Cytoplasmic calcium, released from the ER, triggers apoptosis by the activation of CAMK2 complex (PubMed:19752026).
Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (PubMed:29907098).
Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (PubMed:23542070).
Regulates fertilization and egg activation by tuning the frequency and amplitude of calcium oscillations (PubMed:38099643).
Catalytic activity
- Ca2+(in) = Ca2+(out)
Activity regulation
Inositol 1,4,5-trisphosphate-gated calcium channel activity is activated by zinc ions (PubMed:38099643).
Inositol 1,4,5-trisphosphate-gated calcium channel activity is inhibited by CALM1 in a calcium-dependent manner (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 265 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 267 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 268 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 269 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 508 | 1D-myo-inositol 1,4,5-trisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 511 | 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 | 747 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: R | ||||||
Binding site | 1127 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: E | ||||||
Binding site | 1130 | Ca2+ 1 (UniProtKB | ChEBI); low affinity | ||||
Sequence: E | ||||||
Binding site | 1977 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 2041 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 2220 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2223 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2610 | ATP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2610 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2611 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 2613 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2630 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2635 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2635 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2637 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 2653 | 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 ITPR1
- 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 accessionP11881
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-2273 | Cytoplasmic | ||||
Sequence: MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDILSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTALNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDESENAELPQAPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSSSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMS | ||||||
Transmembrane | 2274-2294 | Helical | ||||
Sequence: FWSSISFNLAVLMNLLVAFFY | ||||||
Topological domain | 2295-2305 | Lumenal | ||||
Sequence: PFKGVRGGTLE | ||||||
Transmembrane | 2306-2326 | Helical | ||||
Sequence: PHWSGLLWTAMLISLAIVIAL | ||||||
Topological domain | 2327-2352 | Cytoplasmic | ||||
Sequence: PKPHGIRALIASTILRLIFSVGLQPT | ||||||
Transmembrane | 2353-2373 | Helical | ||||
Sequence: LFLLGAFNVCNKIIFLMSFVG | ||||||
Topological domain | 2374-2396 | Lumenal | ||||
Sequence: NCGTFTRGYRAMVLDVEFLYHLL | ||||||
Transmembrane | 2397-2417 | Helical | ||||
Sequence: YLLICAMGLFVHEFFYSLLLF | ||||||
Topological domain | 2418-2439 | Cytoplasmic | ||||
Sequence: DLVYREETLLNVIKSVTRNGRS | ||||||
Transmembrane | 2440-2460 | Helical | ||||
Sequence: IILTAVLALILVYLFSIVGYL | ||||||
Topological domain | 2461-2569 | Lumenal | ||||
Sequence: FFKDDFILEVDRLPNETAVPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYD | ||||||
Transmembrane | 2570-2590 | Helical | ||||
Sequence: LLFFFMVIIIVLNLIFGVIID | ||||||
Topological domain | 2591-2749 | Cytoplasmic | ||||
Sequence: TFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 56 | Strongly reduced palmitoylation; when associated with A-849 and A-2215. | ||||
Sequence: C → A | ||||||
Mutagenesis | 167 | Nearly abolishes calcium flux. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 168 | Reduces calcium flux by about 50%. | ||||
Sequence: K → A | ||||||
Mutagenesis | 169 | Reduces calcium flux by about 50%. | ||||
Sequence: L → A | ||||||
Mutagenesis | 267 | Abolishes inositol 1,4,5-triphosphate binding. | ||||
Sequence: T → A | ||||||
Mutagenesis | 567 | Abolishes inositol 1,4,5-triphosphate binding. | ||||
Sequence: Y → A or F | ||||||
Mutagenesis | 849 | Strongly reduced palmitoylation; when associated with A-56 and A-2215. | ||||
Sequence: C → A | ||||||
Mutagenesis | 1588 | Increases interaction with AHCYL1; when associated with A-1755. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1588 | Decreases interaction with AHCYL1; when associated with A-1755. | ||||
Sequence: S → E | ||||||
Mutagenesis | 1755 | Increases interaction with AHCYL1; when associated with A-1588. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1755 | Decreases interaction with AHCYL1; when associated with A-1588. | ||||
Sequence: S → E | ||||||
Mutagenesis | 2215 | Strongly reduced palmitoylation; when associated with A-56 and A-849. | ||||
Sequence: C → A | ||||||
Mutagenesis | 2463-2464 | Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Does not affect ERLIN2 binding. | ||||
Sequence: KD → AA | ||||||
Mutagenesis | 2463-2464 | Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 2464-2465 | Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding. | ||||
Sequence: DD → NN | ||||||
Mutagenesis | 2465 | Loss of the vast majority of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding. | ||||
Sequence: D → N | ||||||
Mutagenesis | 2465-2467 | Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of ERLIN2 binding. | ||||
Sequence: DFI → AAA | ||||||
Mutagenesis | 2465-2467 | Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 2468-2470 | Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 2471 | Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 2471-2472 | Loss of binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Does not affect homotetramerization. | ||||
Sequence: DR → AA | ||||||
Mutagenesis | 2471-2472 | Loss of binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. Loss of polyubiquitination. | ||||
Sequence: DR → GG | ||||||
Mutagenesis | 2471-2472 | Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: DR → NQ | ||||||
Mutagenesis | 2471-2472 | Loss of interaction with the complex ERLIN1:ERLIN2:RNF170 after stimulation with GNRH1. Does not affect homotetramerization. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 2472 | Does not affect binding to the ERLIN1:ERLIN2:RNF170 complex. Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: R → Q | ||||||
Mutagenesis | 2496 | No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. | ||||
Sequence: C → S | ||||||
Mutagenesis | 2504 | No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. | ||||
Sequence: C → S | ||||||
Mutagenesis | 2527 | Complete loss of channel activity. Significant decrease of interaction with ERP44. | ||||
Sequence: C → S | ||||||
Mutagenesis | 2550 | Does not affect inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 2596 | Loss of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 116 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, lipidation, cross-link, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153921 | 1-2749 | Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 | |||
Sequence: MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDILSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTALNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDESENAELPQAPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSSSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA | ||||||
Lipidation | 56 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 849 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Cross-link | 916 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 962 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1571 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 1588 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1755 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Cross-link | 1771 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1884 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1885 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1886 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1901 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1924 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 2118 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 2257 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Disulfide bond | 2527↔2533 | |||||
Sequence: CETLLMC |
Post-translational modification
Polyubiquitination targets ITPR1 for proteasomal degradation (PubMed:35568199).
Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (By similarity).
Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1 (Probable)
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homotetramer (PubMed:35568199).
Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity (PubMed:15652484).
The strength of this interaction inversely correlates with calcium concentration (PubMed:15652484).
Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By similarity).
Interacts with IRAG1 (PubMed:16990611).
Interacts with CABP1 (via N-terminus) (By similarity).
Interacts with TESPA1 (PubMed:23650607).
Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 and is increased in the presence of BCL2L10 (PubMed:12525476, PubMed:16527252, PubMed:23542070).
Interacts with AHCYL2 (with lower affinity than with AHCYL1). Interacts with BCL2L10; the interaction is increased in the presence of AHCLY1 (By similarity).
Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (PubMed:23884412).
Interacts with TRPC4 (By similarity).
Interacts with CHGA and CHGB (By similarity).
Interacts with CALM1; this interaction inhibits inositol 1,4,5 trisphosphate binding in both the presence and absence of calcium and Inositol 1,4,5-trisphosphate-induced calcium release in the presence of calcium (PubMed:10620513, PubMed:11955285).
Interacts with the complex composed by ERLIN1, ERLIN2 and RNF170 through ERLIN2; this interaction triggers its ubiquitin-proteasomal degradation (PubMed:35568199).
Interacts with HSPA9; this interaction couples ITPR1 to VDAC1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P11881 | Atp1a1 Q8VDN2 | 3 | EBI-541478, EBI-444536 | |
BINARY | P11881 | Atp1a2 Q6PIE5 | 3 | EBI-541478, EBI-6665421 | |
XENO | P11881 | BCL2 P10415 | 3 | EBI-541478, EBI-77694 | |
BINARY | P11881 | Erp44 Q9D1Q6 | 5 | EBI-541478, EBI-541567 | |
BINARY | P11881 | Slc8a1 O35157 | 4 | EBI-541478, EBI-8351080 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 112-166 | MIR 1 | ||||
Sequence: GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPF | ||||||
Domain | 173-223 | MIR 2 | ||||
Sequence: GDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLF | ||||||
Domain | 231-287 | MIR 3 | ||||
Sequence: DDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVV | ||||||
Domain | 294-373 | MIR 4 | ||||
Sequence: GGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPT | ||||||
Domain | 379-435 | MIR 5 | ||||
Sequence: DSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPV | ||||||
Region | 1005-1026 | Disordered | ||||
Sequence: NSQSSETSSGNSSQEGPSNVPG | ||||||
Compositional bias | 1006-1023 | Polar residues | ||||
Sequence: SQSSETSSGNSSQEGPSN | ||||||
Region | 1136-1167 | Disordered | ||||
Sequence: GQGPDEPMDGASGENEHKKTEEGTSKPLKHES | ||||||
Compositional bias | 1145-1163 | Basic and acidic residues | ||||
Sequence: GASGENEHKKTEEGTSKPL | ||||||
Region | 1695-1730 | Disordered | ||||
Sequence: IDESENAELPQAPEAENSTEQELEPSPPLRQLEDHK | ||||||
Compositional bias | 1705-1719 | Polar residues | ||||
Sequence: QAPEAENSTEQELEP | ||||||
Region | 1751-1788 | Disordered | ||||
Sequence: GRRESLTSFGNGPLSPGGPSKPGGGGGGPGSSSTSRGE | ||||||
Region | 1881-1906 | Disordered | ||||
Sequence: LGNKKKDDEVDRDAPSRKKAKEPTTQ | ||||||
Region | 1932-1952 | Disordered | ||||
Sequence: EADPDDHYQSGEGTQATTDKA | ||||||
Region | 2463-2528 | Interaction with ERP44 | ||||
Sequence: KDDFILEVDRLPNETAVPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCE | ||||||
Region | 2721-2749 | Disordered | ||||
Sequence: QMTEQRKQKQRIGLLGHPPHMNVNPQQPA |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing. There is a combination of two alternatively spliced domains at site SI and site SII (A, B and C). Experimental confirmation may be lacking for some isoforms.
P11881-1
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
- SynonymsSISIIABC
- Length2,749
- Mass (Da)313,167
- Last updated2010-11-30 v2
- ChecksumFC4CF3ABB85EB82B
P11881-2
- Name2
- SynonymsSI-SIIABC
- Differences from canonical
- 318-332: Missing
P11881-3
- Name3
- SynonymsSISIIAC
- Differences from canonical
- 1715-1715: Missing
P11881-4
- Name4
- SynonymsSI-SIIAC
- Differences from canonical
- 318-332: Missing
- 1715-1715: Missing
P11881-5
- Name5
- SynonymsSISIIA
- Differences from canonical
- 1715-1715: Missing
- 1716-1731: Missing
P11881-6
- Name6
- SynonymsSI-SIIA
- Differences from canonical
- 318-332: Missing
- 1715-1715: Missing
- 1716-1731: Missing
P11881-7
- Name7
- SynonymsSISII
- Differences from canonical
- 1692-1714: Missing
- 1715-1715: Missing
- 1716-1731: Missing
P11881-8
- Name8
- SynonymsSI-SII
- Differences from canonical
- 318-332: Missing
- 1692-1714: Missing
- 1715-1715: Missing
- 1716-1731: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0N4SVN2 | A0A0N4SVN2_MOUSE | Itpr1 | 225 | ||
A0A0N4SWI0 | A0A0N4SWI0_MOUSE | Itpr1 | 215 | ||
A0A0N4SWH7 | A0A0N4SWH7_MOUSE | Itpr1 | 313 | ||
A0A0N4SW22 | A0A0N4SW22_MOUSE | Itpr1 | 152 | ||
A0A1D5RLA1 | A0A1D5RLA1_MOUSE | Itpr1 | 213 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002691 | 318-332 | in isoform 2, isoform 4, isoform 6 and isoform 8 | |||
Sequence: Missing | ||||||
Compositional bias | 1006-1023 | Polar residues | ||||
Sequence: SQSSETSSGNSSQEGPSN | ||||||
Compositional bias | 1145-1163 | Basic and acidic residues | ||||
Sequence: GASGENEHKKTEEGTSKPL | ||||||
Sequence conflict | 1264 | in Ref. 1; CAA33433 | ||||
Sequence: N → K | ||||||
Alternative sequence | VSP_002692 | 1692-1714 | in isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Compositional bias | 1705-1719 | Polar residues | ||||
Sequence: QAPEAENSTEQELEP | ||||||
Alternative sequence | VSP_002693 | 1715 | in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002694 | 1716-1731 | in isoform 5, isoform 6, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 2675 | in Ref. 1; CAA33433 | ||||
Sequence: P → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15373 EMBL· GenBank· DDBJ | CAA33433.1 EMBL· GenBank· DDBJ | mRNA | ||
AC120411 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC153986 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC156506 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M75986 EMBL· GenBank· DDBJ | AAA39316.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M75987 EMBL· GenBank· DDBJ | AAA39317.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003271 EMBL· GenBank· DDBJ | AAH03271.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
M21530 EMBL· GenBank· DDBJ | AAA88319.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |