Itpr1
entrez
25262
canonical
uniprot
P29994
canonical
ensembl
ENSRNOG00000007104
resolver
ensp
ENSRNOP00000048661
resolver
ensp
ENSRNOP00000111175
resolver
genesymbol
Itpr1
resolver
genesymbol_syn
Insp3r
resolver
uniprot
C7E1V2
resolver
uniprot
F1LQS8
resolver
uniprot
Q5BJS8
resolver
uniprot
Q62869
resolver
uniprot_entry
C7E1V2_RAT
resolver
uniprot_entry
ITPR1_RAT
resolver
uniprot_entry
Q5BJS8_RAT
resolver
uniprot_sec
F1LQS8
resolver
uniprot_sec
Q62869
resolver
activity_regulation
ACTIVITY REGULATION: Inositol 1,4,5-trisphosphate-gated calcium channel activity is regulated by cytosolic calcium in a biphasic manner, with low concentrations causing activation and higher concentrations inhibiting channel opening, giving rise to calcium oscillations (PubMed:22547632). ATP increases the open probability of ITPR1 by synergizing with the activating effect of these two primarily ligands, inositol 1,4,5-trisphosphate and calcium (PubMed:22547632). Inositol 1,4,5-trisphosphate-gated calcium channel activity is activated by zinc ions (By similarity). Inositol 1,4,5-trisphosphate-gated calcium channel activity is inhibited by CALM1 in a calcium-dependent manner (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000250|UniProtKB:Q14643, ECO:0000269|PubMed:22547632}.
uniprot
proteins
amino_acid_sequence
MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLFMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSVLEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDELENAELPQPPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSGSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFILEVDRLPNETAGPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
uniprot
proteins
function
FUNCTION: Inositol 1,4,5-trisphosphate-gated calcium channel that, upon inositol 1,4,5-trisphosphate binding, mediates calcium release from the endoplasmic reticulum (ER) (PubMed:2165071, PubMed:22547632, PubMed:36376291). 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 1,4,5-trisphosphate and calcium, to an open state, capable of transferring calcium ions across the ER membrane (PubMed:36376291). Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CAMK2 complex (By similarity). 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 (By similarity). Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Regulates fertilization and egg activation by tuning the frequency and amplitude of calcium oscillations (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:2165071, ECO:0000269|PubMed:22547632, ECO:0000269|PubMed:36376291}.
uniprot
proteins
mass_dalton
313264
uniprot
proteins
mutagenesis
MUTAGEN 1589; /note="S->A: Does nota affect calcium release."; /evidence="ECO:0000269|PubMed:12939273"; MUTAGEN 1756; /note="S->A: Abolishes calcium release."; /evidence="ECO:0000269|PubMed:12939273
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated (PubMed:18955483). Polyubiquitination targets ITPR1 for proteasomal degradation (PubMed:18955483). Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (PubMed:18955483). {ECO:0000269|PubMed:18955483}.; PTM: Phosphorylation by cAMP kinase (PKA) enhances calcium release (PubMed:12939273). Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1 (By similarity). {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:12939273}.; PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q14643}.; PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulation of ITPR1 stability and function. {ECO:0000250|UniProtKB:P11881}.
uniprot
proteins
protein_family
InsP3 receptor family
uniprot
proteins
pubmed
10506212
uniprot
proteins
pubmed
11163362
uniprot
proteins
pubmed
12032348
uniprot
proteins
pubmed
12939273
uniprot
proteins
pubmed
17178908
uniprot
proteins
pubmed
1849282
uniprot
proteins
pubmed
18955483
uniprot
proteins
pubmed
2165071
uniprot
proteins
pubmed
21892169
uniprot
proteins
pubmed
22286060
uniprot
proteins
pubmed
22547632
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
36376291
uniprot
proteins
pubmed
9073177
uniprot
proteins
sequence_length
2750
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10506212}; Multi-pass membrane protein {ECO:0000269|PubMed:10506212}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:10506212}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14643}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000269|PubMed:17178908}.
uniprot
proteins
transmembrane_region
TRANSMEM 2275..2295; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212"; TRANSMEM 2307..2327; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212"; TRANSMEM 2354..2374; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212"; TRANSMEM 2398..2418; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212"; TRANSMEM 2441..2461; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212"; TRANSMEM 2570..2590; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:10506212
uniprot
proteins