P29994 · ITPR1_RAT
- ProteinInositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- GeneItpr1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2750 (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 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).
Catalytic activity
- Ca2+(in) = Ca2+(out)
Activity regulation
ATP increases the open probability of IP3R1 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).
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 | 1978 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 2042 | Ca2+ 2 (UniProtKB | ChEBI); high affinity | ||||
Sequence: E | ||||||
Binding site | 2221 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2224 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2611 | ATP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2611 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2612 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 2614 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2631 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2636 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2636 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2638 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 2654 | 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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP29994
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-2274 | Cytoplasmic | ||||
Sequence: MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLFMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSVLEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDELENAELPQPPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSGSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMS | ||||||
Transmembrane | 2275-2295 | Helical | ||||
Sequence: FWSSISFNLAVLMNLLVAFFY | ||||||
Topological domain | 2296-2306 | Lumenal | ||||
Sequence: PFKGVRGGTLE | ||||||
Transmembrane | 2307-2327 | Helical | ||||
Sequence: PHWSGLLWTAMLISLAIVIAL | ||||||
Topological domain | 2328-2353 | Cytoplasmic | ||||
Sequence: PKPHGIRALIASTILRLIFSVGLQPT | ||||||
Transmembrane | 2354-2374 | Helical | ||||
Sequence: LFLLGAFNVCNKIIFLMSFVG | ||||||
Topological domain | 2375-2397 | Lumenal | ||||
Sequence: NCGTFTRGYRAMVLDVEFLYHLL | ||||||
Transmembrane | 2398-2418 | Helical | ||||
Sequence: YLLICAMGLFVHEFFYSLLLF | ||||||
Topological domain | 2419-2440 | Cytoplasmic | ||||
Sequence: DLVYREETLLNVIKSVTRNGRP | ||||||
Transmembrane | 2441-2461 | Helical | ||||
Sequence: IILTAALALILVYLFSIVGYL | ||||||
Topological domain | 2462-2569 | Lumenal | ||||
Sequence: FFKDDFILEVDRLPNETAGPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIY | ||||||
Transmembrane | 2570-2590 | Helical | ||||
Sequence: DLLFFFMVIIIVLNLIFGVII | ||||||
Topological domain | 2591-2750 | Cytoplasmic | ||||
Sequence: DTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 1372 | in all but PI17 clones | ||||
Sequence: Missing | ||||||
Mutagenesis | 1589 | Does nota affect calcium release. | ||||
Sequence: S → A | ||||||
Mutagenesis | 1756 | Abolishes calcium release. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, lipidation, cross-link, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153922 | 1-2750 | Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 | |||
Sequence: MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLFMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSVLEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDELENAELPQPPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSGSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFILEVDRLPNETAGPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA | ||||||
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 | 1572 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 1589 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1756 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Cross-link | 1772 | 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 | 1887 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1902 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 1925 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 2119 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 2258 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Disulfide bond | 2528↔2534 | |||||
Sequence: CETLLMC |
Post-translational modification
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).
Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1 (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer (PubMed:21892169, PubMed:22286060).
Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity. The strength of this interaction inversely correlates with calcium concentration (By similarity).
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 (By similarity).
Interacts with CABP1 (via N-terminus) (PubMed:12032348).
Interacts with TESPA1. 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. Interacts with AHCYL2 (with lower affinity than with AHCYL1). Interacts with BCL2L10; the interaction is increased in the presence of AHCLY1. Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (By similarity).
Interacts with TRPC4 (PubMed:11163362).
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. Interacts with the complex composed by ERLIN1, ERLIN2 and RNF170 through ERLIN2; this interaction triggers its ubiquitin-proteasomal degradation (By similarity).
Interacts with HSPA9; this interaction couples ITPR1 to VDAC1 (PubMed:17178908).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P29994 | Hap1 P54256-1 | 2 | EBI-8614640, EBI-994549 | |
BINARY | P29994 | Hap1 P54256-2 | 4 | EBI-8614640, EBI-994554 | |
BINARY | P29994 | Htt P51111 | 4 | EBI-8614640, EBI-9674649 | |
XENO | P29994 | HTT P42858 | 2 | EBI-8614640, EBI-466029 | |
XENO | P29994-1 | Crtc2 Q3U182 | 2 | EBI-15683709, EBI-8018890 | |
BINARY | P29994-1 | Itpr1 P29994-1 | 2 | EBI-15683709, EBI-15683709 |
Protein-protein interaction databases
Chemistry
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 | 1705-1731 | Disordered | ||||
Sequence: PQPPEAENSTEQELEPSPPLRQLEDHK | ||||||
Region | 1752-1790 | Disordered | ||||
Sequence: GRRESLTSFGNGPLSPGGPSKPGGGGGGPGSGSTSRGEM | ||||||
Region | 1882-1907 | Disordered | ||||
Sequence: LGNKKKDDEVDRDAPSRKKAKEPTTQ | ||||||
Region | 1933-1953 | Disordered | ||||
Sequence: EADPDDHYQSGEGTQATTDKA | ||||||
Region | 2464-2529 | Interaction with ERP44 | ||||
Sequence: KDDFILEVDRLPNETAGPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCE | ||||||
Region | 2723-2750 | Disordered | ||||
Sequence: MTEQRKQKQRIGLLGHPPHMNVNPQQPA |
Domain
The solenoid scaffold includes domains responsible for binding of ligands and regulatory proteins and is connected via an allosteric nexus at the cytosolic-membrane interface to the transmembrane channel assembly (PubMed:36376291).
Six transmembrane helices from each subunit form the central ion-conduction pore (PubMed:36376291).
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.
P29994-1
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
- Length2,750
- Mass (Da)313,264
- Last updated2001-11-02 v2
- Checksum174BB77CBF6F21AC
P29994-2
- Name2
- SynonymsSI-SIIABC
- Differences from canonical
- 322-336: Missing
P29994-3
- Name3
- SynonymsSISIIAC
- Differences from canonical
- 1716-1716: Missing
P29994-4
- Name4
- SynonymsSI-SIIAC
- Differences from canonical
- 322-336: Missing
- 1716-1716: Missing
P29994-5
- Name5
- SynonymsSISIIA
- Differences from canonical
- 1716-1716: Missing
- 1717-1732: Missing
P29994-6
- Name6
- SynonymsSI-SIIA
- Differences from canonical
- 322-336: Missing
- 1716-1716: Missing
- 1717-1732: Missing
P29994-7
- Name7
- SynonymsSISII
- Differences from canonical
- 1693-1715: Missing
- 1716-1716: Missing
- 1717-1732: Missing
P29994-8
- Name8
- SynonymsSI-SII
- Differences from canonical
- 322-336: Missing
- 1693-1715: Missing
- 1716-1716: Missing
- 1717-1732: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2KAH9 | A0A0G2KAH9_RAT | Itpr1 | 2574 | ||
A0A0A0MY31 | A0A0A0MY31_RAT | Itpr1 | 2738 | ||
A0A8J8XAG4 | A0A8J8XAG4_RAT | Itpr1 | 2758 | ||
F1LQX8 | F1LQX8_RAT | Itpr1 | 2752 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002695 | 322-336 | 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 | ||||||
Alternative sequence | VSP_002696 | 1693-1715 | in isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002697 | 1716 | in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002698 | 1717-1732 | in isoform 5, isoform 6, isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 1764 | in Ref. 2; AAA41447/AAA41448 | ||||
Sequence: P → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05510 EMBL· GenBank· DDBJ | AAA41358.1 EMBL· GenBank· DDBJ | mRNA | ||
J05510 EMBL· GenBank· DDBJ | AAA41357.1 EMBL· GenBank· DDBJ | mRNA | ||
M64699 EMBL· GenBank· DDBJ | AAA41447.1 EMBL· GenBank· DDBJ | mRNA | ||
M64698 EMBL· GenBank· DDBJ | AAA41448.1 EMBL· GenBank· DDBJ | mRNA | ||
U38653 EMBL· GenBank· DDBJ | AAC53099.1 EMBL· GenBank· DDBJ | mRNA | ||
U38812 EMBL· GenBank· DDBJ | AAC53100.1 EMBL· GenBank· DDBJ | mRNA | ||
U38665 EMBL· GenBank· DDBJ | AAB51330.1 EMBL· GenBank· DDBJ | mRNA |