Itpr2
entrez
81678
canonical
uniprot
P29995
canonical
ensembl
ENSRNOG00000001804
resolver
ensp
ENSRNOP00000043615
resolver
ensp
ENSRNOP00000077641
resolver
ensp
ENSRNOP00000101675
resolver
enst
ENSRNOT00000040255
resolver
enst
ENSRNOT00000173337
resolver
genesymbol
Itpr2
resolver
uniprot
A0ABK0L0M5
resolver
uniprot
F1LNT1
resolver
uniprot
Q99P56
resolver
uniprot_entry
A0ABK0L0M5_RAT
resolver
uniprot_entry
F1LNT1_RAT
resolver
uniprot_entry
ITPR2_RAT
resolver
uniprot_sec
Q99P56
resolver
activity_regulation
ACTIVITY REGULATION: Inositol 1,4,5-trisphosphate-gated calcium channel activity is inhibited by CALM1 in a calcium-dependent manner (PubMed:10620513). Inositol 1,4,5-trisphosphate-gated calcium channel activity is increased by cAMP that occurs independently of PKA activation. ATP and cytosolic calcium modulate the open probability (Po) predominantly by facilitating extended 'bursting' activity of the channel (By similarity). {ECO:0000250|UniProtKB:Q9Z329, ECO:0000269|PubMed:10620513}.
uniprot
proteins
amino_acid_sequence
MSDKMSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLTNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHTEAALLKKLQHAAELEQKQNESENRKLLGEIVKYSKVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGNEGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLHASNVELLDNPGCKEVNAVNCNTSWKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKTVRDGELPTSKKKHQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEVRDLDFANDANKVLATTVKKLENGSITQNERRFVTKLLEDLIFFVADVTNNGQDVLDVVITKPNRERQKLMREQNILAQVFGILKAPFKEKAGEGSMLRLEDLGDQRYAPYKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAEDTITALLHNNRKLLEKHITAKEIETFVSLLRRNREPRFLDYLSDLCVSNSTAIPVTQELICKFMLSPGNADILIQTKLVSMQVENPMESSILPDDIDDEEVWLYWIDSNKEPHGKAIRHLAQEAREGTKADLEVLTYYRYQLNLFARMCLDRQYLAINQISTQLSVDLILRCVSDESLPFDLRASFCRLMLHMHVDRDPQESVVPVRYARLWTEIPTKITIHEYDSITDSSRNDMKRKFALTMEFVEEYLKEVVNQPFPFGDKEKNKLTFEVVHLARNLIYFGFYSFSELLRLTRTLLAILDIVQAPMSSYFERLSKFQDGSNNVMRTIHGVGEMMTQMVLSRGSIFPVSWPDAQPSVHPSKQASPGEQEDVTVMDTKLKVIEILQFILSVRLDYRISYMLSIYKKEFGENDGNGDPSASGTPETLLPSALVPDIDEIAAQAETMFAGRKEKTPVQLDDEGGRTFLRVLIHLIMHDYAPLLSGALQLLFKHFSQRAEVLQAFKQVQLLVSNQDVDNYKQIKADLDQLRLTVEKSELWVEKSGSYENGDMGEGQAKGGEEANEESNLLSPVQDGAKTPQIDSNKGNNYRIVKEILIRLSKLCVQNKKCRNQHQRLLKNMGAHSVVLDLLQIPYEKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTPGLLEAETMRHIFMNNYHLCNEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINGGEDVLIFYNDRASFPILLNMMCSERARGDESGPLAYHITLVELLAACTEGKNVYTEIKCNSLLPLDDIVRVVTHDDCIPEVKIAYVNFVNHCYVDTEVEMKEIYTSNHIWKLFENFLVDMARVCNTTTDRKHADTFLERCVTESVMNIVSGFFNSPFSDNSTSLQTHQPVFIQLLQSAFRIYNCTWPNPAQKASVESCIRALAEVAKNRGIAIPVDLDSQVNTLFMKNHSSTVQRAAMGWRLSARSGPRFKEALGGPAWDYRNIIEKLQDVVASLEQQFSPMMQAEFSVLVDVLYSPELLFPEGSDARIRCGAFMSKLINHTKKLMEKEEKLCIKILQTLREMLEKKDSFMEESSTLRKILLNRYFKGDHSVGVNGPLSGAYAKTAQVGGGFTGQDADKTGISMSDIQCLLDKEGASELVIDVIVNTKNDRIFSEGILLGIALLEGGNTQTQNSFYQQLHEQKKSEKFFKVLYDRMKAAQKEIRSTVTVNTIDLGSKKREEDSDLMALGPRMRVRDSSLHLKEGMKGQLTEASSATSKAYCVYRREMDPDIDTMCPGQEAGSAEEKSAEEVTMSPAITIMRPILRFLQLLCENHNRELQNFLRNQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALVNQTLESLTEYCQGPCHENQTCIATHESNGIDIIIALILSDINPLGKYRMDLVLQLKNNASKLLLAIMESRHDSENAERILFNMRPKELVDVMKNAYNQGLECNHGDEEGGDDGVSPKDVGHNIYILAHQLARHNKLLQQMLKPGSDPEEGDEALKYYANHTAQIEIVRHDRTMEQIVFPVPNICEFLTRESKYRVFNTTERDEQGSKVNDFFQQTEDLYNEMKWQKKIRNNPALFWFSRHISLWGSISFNLAVFINLAVALFYPFGDDGDEGTLSPLFSALLWVAVAICTSMLFFFSKPVGIRPFLVSIMLRSIYTIGLGPTLILLGAANLCNKIVFLVSFVGNRGTFTRGYRAVILDMAFLYHVAYVLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFTMEVDRLKNRTPVTGNDGVPTMTLTSMLGTCPKENCSPTIPSSNAAGEGGEDGIERTCDTLLMCIVTVLNQGLRNGGGVGDVLRRPSKDEPLFAARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQKKEKILKTTCFICGLERDKFDNKTVSFEEHIKSEHNMWHYLYFIVLVKVKDPTEYTGPESYVAQMITEKNLDWFPRMRAMSLVSNEGDSEQNEIRNLQEKLESTMSLVKQLSGQLAELKEQMTEQRKNKQRLGFLGSNTPHENHHMPPH
uniprot
proteins
function
FUNCTION: Inositol 1,4,5-trisphosphate-gated calcium channel that upon inositol 1,4,5-trisphosphate binding transports calcium from the endoplasmic reticulum lumen to cytoplasm (PubMed:10620513, PubMed:1655411, PubMed:23019322). Exists in two states; a long-lived closed state where the channel is essentially 'parked' with only very rare visits to an open state and that ligands facilitate the transition from the 'parked' state into a 'drive' mode represented by periods of bursting activity (By similarity). {ECO:0000250|UniProtKB:Q9Z329, ECO:0000269|PubMed:10620513, ECO:0000269|PubMed:1655411, ECO:0000269|PubMed:23019322}.
uniprot
proteins
mass_dalton
307058
uniprot
proteins
mutagenesis
MUTAGEN 150; /note="S->A: Loss of phosphorylation by CaMK2. Does not affect Inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity."; /evidence="ECO:0000269|PubMed:23019322"; MUTAGEN 150; /note="S->E: Decreases Inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity."; /evidence="ECO:0000269|PubMed:23019322
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by CaMK2 on Ser-150 significantly decreases the channel open probability. {ECO:0000269|PubMed:23019322}.; PTM: Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium release. {ECO:0000250|UniProtKB:Q9Z329}.
uniprot
proteins
protein_family
InsP3 receptor family
uniprot
proteins
pubmed
10620513
uniprot
proteins
pubmed
11163362
uniprot
proteins
pubmed
12032348
uniprot
proteins
pubmed
1655411
uniprot
proteins
pubmed
23019322
uniprot
proteins
pubmed
23884412
uniprot
proteins
sequence_length
2701
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z329}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q8WN96}; Multi-pass membrane protein {ECO:0000255}. Note=Forms clusters on endoplasmic reticulum membrane upon inositol 1,4,5-trisphosphate binding. {ECO:0000250|UniProtKB:Q9Z329}.
uniprot
proteins
transmembrane_region
TRANSMEM 2228..2248; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2261..2281; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2285..2305; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2308..2328; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2352..2372; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2395..2415; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2522..2542; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins