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P11881

- ITPR1_MOUSE

UniProt

P11881 - ITPR1_MOUSE

Protein

Inositol 1,4,5-trisphosphate receptor type 1

Gene

Itpr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways.3 Publications

    GO - Molecular functioni

    1. inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
    2. intracellular ligand-gated calcium channel activity Source: UniProtKB
    3. phosphatidylinositol binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. calcium ion transport Source: MGI
    2. endoplasmic reticulum calcium ion homeostasis Source: MGI
    3. inositol phosphate-mediated signaling Source: GOC
    4. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    5. post-embryonic development Source: MGI
    6. release of sequestered calcium ion into cytosol Source: UniProtKB
    7. response to hypoxia Source: BHF-UCL
    8. voluntary musculoskeletal movement Source: MGI

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Apoptosis, Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188269. DAG and IP3 signaling.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_219232. Effects of PIP2 hydrolysis.
    REACT_221970. Ca2+ pathway.
    REACT_227667. Elevation of cytosolic Ca2+ levels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol 1,4,5-trisphosphate receptor type 1
    Alternative name(s):
    IP3 receptor isoform 1
    Short name:
    IP3R 1
    Short name:
    InsP3R1
    Inositol 1,4,5-trisphosphate-binding protein P400
    Protein PCD-6
    Purkinje cell protein 1
    Type 1 inositol 1,4,5-trisphosphate receptor
    Short name:
    Type 1 InsP3 receptor
    Gene namesi
    Name:Itpr1
    Synonyms:Insp3r, Pcd6, Pcp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:96623. Itpr1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. calcineurin complex Source: MGI
    2. cytoplasm Source: MGI
    3. endoplasmic reticulum Source: MGI
    4. endoplasmic reticulum membrane Source: MGI
    5. integral component of membrane Source: UniProtKB-KW
    6. nuclear envelope Source: MGI
    7. nuclear inner membrane Source: MGI
    8. nucleolus Source: MGI
    9. platelet dense granule membrane Source: Ensembl
    10. platelet dense tubular network Source: Ensembl
    11. postsynaptic density Source: MGI
    12. protein complex Source: MGI
    13. sarcoplasmic reticulum Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi167 – 1671Y → A: Nearly abolishes calcium flux. 1 Publication
    Mutagenesisi168 – 1681K → A: Reduces calcium flux by about 50%. 1 Publication
    Mutagenesisi169 – 1691L → A: Reduces calcium flux by about 50%.
    Mutagenesisi267 – 2671T → A: Abolishes inositol 1,4,5-triphosphate binding. 1 Publication
    Mutagenesisi567 – 5671Y → A or F: Abolishes inositol 1,4,5-triphosphate binding. 1 Publication
    Mutagenesisi2496 – 24961C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. 1 Publication
    Mutagenesisi2504 – 25041C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. 1 Publication
    Mutagenesisi2527 – 25271C → S: Complete loss of channel activity. Significant decrease of interaction with ERP44. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27492749Inositol 1,4,5-trisphosphate receptor type 1PRO_0000153921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei482 – 4821PhosphotyrosineSequence Analysis
    Cross-linki916 – 916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki962 – 962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1571 – 1571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei1588 – 15881Phosphoserine1 Publication
    Modified residuei1755 – 17551Phosphoserine; by PKASequence Analysis
    Cross-linki1771 – 1771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1884 – 1884Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1885 – 1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1886 – 1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1901 – 1901Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1924 – 1924Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki2118 – 2118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki2257 – 2257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei2655 – 26551PhosphotyrosineSequence Analysis

    Post-translational modificationi

    Phosphorylated by cAMP kinase. Phosphorylation prevents the ligand-induced opening of the calcium channels.1 Publication
    Phosphorylated on tyrosine residues.By similarity
    Ubiquitination at multiple lysines targets ITPR1 for proteasomal degradation. Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP11881.
    PaxDbiP11881.
    PRIDEiP11881.

    PTM databases

    PhosphoSiteiP11881.

    Expressioni

    Gene expression databases

    ArrayExpressiP11881.
    BgeeiP11881.
    CleanExiMM_ITPR1.
    GenevestigatoriP11881.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. 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 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. Interacts with AHCYL1 and MRVI1. Interacts with CABP1 By similarity. Interacts with TESPA1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Erp44Q9D1Q65EBI-541478,EBI-541567

    Protein-protein interaction databases

    BioGridi200847. 17 interactions.
    DIPiDIP-32243N.
    IntActiP11881. 9 interactions.
    MINTiMINT-4099099.

    Structurei

    Secondary structure

    1
    2749
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 2310
    Beta strandi25 – 306
    Beta strandi36 – 394
    Helixi41 – 433
    Beta strandi46 – 483
    Helixi53 – 564
    Beta strandi58 – 614
    Helixi67 – 748
    Helixi86 – 10924
    Turni110 – 1123
    Beta strandi120 – 1256
    Turni126 – 1294
    Beta strandi130 – 13910
    Beta strandi141 – 1433
    Beta strandi146 – 1549
    Helixi157 – 1593
    Beta strandi161 – 1677
    Beta strandi181 – 1899
    Beta strandi193 – 1997
    Beta strandi201 – 2055
    Beta strandi207 – 2137
    Beta strandi217 – 2237
    Beta strandi239 – 2446
    Turni245 – 2484
    Beta strandi249 – 2557
    Beta strandi257 – 2659
    Beta strandi269 – 2713
    Helixi272 – 2743
    Helixi278 – 2803
    Beta strandi282 – 2865
    Beta strandi303 – 3075
    Turni308 – 3103
    Beta strandi313 – 3186
    Beta strandi353 – 3597
    Helixi364 – 3663
    Beta strandi368 – 3714
    Beta strandi388 – 3925
    Turni393 – 3964
    Beta strandi397 – 40610
    Beta strandi409 – 4124
    Beta strandi415 – 4239
    Beta strandi430 – 4345
    Helixi437 – 46125
    Helixi467 – 48418
    Turni485 – 4873
    Helixi495 – 4995
    Helixi504 – 5129
    Helixi515 – 52410
    Helixi525 – 5273
    Helixi547 – 56418
    Helixi568 – 58518
    Helixi589 – 59911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N4KX-ray2.20A224-604[»]
    1XZZX-ray1.80A2-223[»]
    ProteinModelPortaliP11881.
    SMRiP11881. Positions 7-580.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11881.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22732273CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2295 – 230511LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2327 – 235226CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2374 – 239623LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2418 – 243922CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2461 – 2569109LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2591 – 2749159CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2274 – 229421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2306 – 232621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2353 – 237321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2397 – 241721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2440 – 246021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2570 – 259021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 16655MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 22351MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini231 – 28757MIR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 37380MIR 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini379 – 43557MIR 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 2695Inositol 1,4,5-trisphosphate binding
    Regioni508 – 5114Inositol 1,4,5-trisphosphate binding
    Regioni567 – 5693Inositol 1,4,5-trisphosphate binding
    Regioni2463 – 252866Interaction with ERP44Add
    BLAST

    Domaini

    The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.

    Sequence similaritiesi

    Belongs to the InsP3 receptor family.Curated
    Contains 5 MIR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG280601.
    GeneTreeiENSGT00690000102000.
    HOGENOMiHOG000007660.
    HOVERGENiHBG052158.
    InParanoidiP11881.
    KOiK04958.
    OMAiKAFTTFR.
    OrthoDBiEOG76HQ0M.
    PhylomeDBiP11881.
    TreeFamiTF312815.

    Family and domain databases

    Gene3Di1.25.10.30. 2 hits.
    InterProiIPR014821. Ins145_P3_rcpt.
    IPR000493. InsP3_rcpt-bd.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR015925. Ryanodine_recept-rel.
    [Graphical view]
    PANTHERiPTHR13715. PTHR13715. 1 hit.
    PfamiPF08709. Ins145_P3_rec. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02815. MIR. 1 hit.
    PF08454. RIH_assoc. 1 hit.
    PF01365. RYDR_ITPR. 2 hits.
    [Graphical view]
    PRINTSiPR00779. INSP3RECEPTR.
    SMARTiSM00472. MIR. 4 hits.
    [Graphical view]
    SUPFAMiSSF100909. SSF100909. 2 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEiPS50919. MIR. 5 hits.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Note: 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.

    Isoform 1 (identifier: P11881-1) [UniParc]FASTAAdd to Basket

    Also known as: SISIIABC

    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.

    « Hide

    MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP     50
    KKFRDCLFKL CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK 100
    KQNETENRKL LGTVIQYGNV IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT 150
    LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD KVVLNPVNAG QPLHASSHQL 200
    VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV RLFHAEQEKF 250
    LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 300
    SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK 350
    MVYSLVSVPE GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH 400
    STNIPIDKEE EKPVMLKIGT SPLKEDKEAF AIVPVSPAEV RDLDFANDAS 450
    KVLGSIAGKL EKGTITQNER RSVTKLLEDL VYFVTGGTNS GQDVLEVVFS 500
    KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE LGDQRHAPFR 550
    HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 600
    NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE 650
    LICKAVLNPT NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW 700
    RDSNKEIRSK SVRELAQDAK EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL 750
    AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP 800
    VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV EEYLRDVVCQ 850
    RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV 900
    TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA 950
    PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE 1000
    FDESNSQSSE TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL 1050
    DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV 1100
    QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD EPMDGASGEN 1150
    EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ 1200
    QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ 1250
    NQALLHKHIN LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE 1300
    THGRNVQYIK FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS 1350
    FQTLIQMMRS ERDRMDENSP LMYHIHLVEL LAVCTEGKNV YTEIKCNSLL 1400
    PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI YTSNHMWKLF 1450
    ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT 1500
    LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI 1550
    PVDLDSQVNN LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII 1600
    ERLQDIVSAL EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG 1650
    FICKLIKHTK QLLEENEEKL CIKVLQTLRE MMTKDRGYGE KQISIDESEN 1700
    AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV NRYYGNIRPS 1750
    GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK 1800
    EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK 1850
    KSEKFFKVFY DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA 1900
    KEPTTQITEE VRDQLLEASA ATRKAFTTFR READPDDHYQ SGEGTQATTD 1950
    KAKDDLEMSA VITIMQPILR FLQLLCENHN RDLQNFLRCQ NNKTNYNLVC 2000
    ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT EYCQGPCHEN 2050
    QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME 2100
    SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN 2150
    VGHNIYILAH QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL 2200
    DRTMEQIVFP VPSICEFLTK ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF 2250
    NEMNWQKKLR AQPVLYWCAR NMSFWSSISF NLAVLMNLLV AFFYPFKGVR 2300
    GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI LRLIFSVGLQ 2350
    PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI 2400
    CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL 2450
    VYLFSIVGYL FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET 2500
    GENCTSPAPK EELLPAEETE QDKEHTCETL LMCIVTVLSH GLRSGGGVGD 2550
    VLRKPSKEEP LFAARVIYDL LFFFMVIIIV LNLIFGVIID TFADLRSEKQ 2600
    KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY LCFIVLVKVK 2650
    DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK 2700
    LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA 2749
    Length:2,749
    Mass (Da):313,167
    Last modified:November 30, 2010 - v2
    Checksum:iFC4CF3ABB85EB82B
    GO
    Isoform 2 (identifier: P11881-2) [UniParc]FASTAAdd to Basket

    Also known as: SI-SIIABC

    The sequence of this isoform differs from the canonical sequence as follows:
         318-332: Missing.

    Show »
    Length:2,734
    Mass (Da):311,401
    Checksum:iFB3AE790B42F4CE7
    GO
    Isoform 3 (identifier: P11881-3) [UniParc]FASTAAdd to Basket

    Also known as: SISIIAC

    The sequence of this isoform differs from the canonical sequence as follows:
         1715-1715: Missing.

    Show »
    Length:2,748
    Mass (Da):313,039
    Checksum:i1230FF411AD4E5D2
    GO
    Isoform 4 (identifier: P11881-4) [UniParc]FASTAAdd to Basket

    Also known as: SI-SIIAC

    The sequence of this isoform differs from the canonical sequence as follows:
         318-332: Missing.
         1715-1715: Missing.

    Show »
    Length:2,733
    Mass (Da):311,273
    Checksum:i1424C44D6B2029D7
    GO
    Isoform 5 (identifier: P11881-5) [UniParc]FASTAAdd to Basket

    Also known as: SISIIA

    The sequence of this isoform differs from the canonical sequence as follows:
         1715-1715: Missing.
         1716-1731: Missing.

    Show »
    Length:2,732
    Mass (Da):311,113
    Checksum:iE080B729B56533DE
    GO
    Isoform 6 (identifier: P11881-6) [UniParc]FASTAAdd to Basket

    Also known as: SI-SIIA

    The sequence of this isoform differs from the canonical sequence as follows:
         318-332: Missing.
         1715-1715: Missing.
         1716-1731: Missing.

    Show »
    Length:2,717
    Mass (Da):309,347
    Checksum:i8770BE568800564C
    GO
    Isoform 7 (identifier: P11881-7) [UniParc]FASTAAdd to Basket

    Also known as: SISII

    The sequence of this isoform differs from the canonical sequence as follows:
         1692-1714: Missing.
         1715-1715: Missing.
         1716-1731: Missing.

    Show »
    Length:2,709
    Mass (Da):308,629
    Checksum:i586D7A1358C19E69
    GO
    Isoform 8 (identifier: P11881-8) [UniParc]FASTAAdd to Basket

    Also known as: SI-SII

    The sequence of this isoform differs from the canonical sequence as follows:
         318-332: Missing.
         1692-1714: Missing.
         1715-1715: Missing.
         1716-1731: Missing.

    Show »
    Length:2,694
    Mass (Da):306,863
    Checksum:i3F2A34C1ACCB2CCF
    GO

    Sequence cautioni

    The sequence AAA88319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH03271.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1264 – 12641N → K in CAA33433. (PubMed:2554142)Curated
    Sequence conflicti2675 – 26751P → L in CAA33433. (PubMed:2554142)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei318 – 33215Missing in isoform 2, isoform 4, isoform 6 and isoform 8. CuratedVSP_002691Add
    BLAST
    Alternative sequencei1692 – 171423Missing in isoform 7 and isoform 8. CuratedVSP_002692Add
    BLAST
    Alternative sequencei1715 – 17151Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8. CuratedVSP_002693
    Alternative sequencei1716 – 173116Missing in isoform 5, isoform 6, isoform 7 and isoform 8. CuratedVSP_002694Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15373 mRNA. Translation: CAA33433.1.
    AC120411 Genomic DNA. No translation available.
    AC153986 Genomic DNA. No translation available.
    AC156506 Genomic DNA. No translation available.
    M75986 Genomic DNA. Translation: AAA39316.1.
    M75987 Genomic DNA. Translation: AAA39317.1.
    BC003271 mRNA. Translation: AAH03271.1. Different initiation.
    M21530 mRNA. Translation: AAA88319.1. Different initiation.
    CCDSiCCDS51869.1. [P11881-1]
    PIRiS04844. ACMSIT.
    RefSeqiNP_034715.3. NM_010585.5. [P11881-1]
    XP_006505693.1. XM_006505630.1. [P11881-2]
    XP_006505699.1. XM_006505636.1. [P11881-7]
    XP_006505700.1. XM_006505637.1. [P11881-8]
    UniGeneiMm.227912.

    Genome annotation databases

    EnsembliENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
    GeneIDi16438.
    KEGGimmu:16438.
    UCSCiuc009ddh.3. mouse. [P11881-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15373 mRNA. Translation: CAA33433.1 .
    AC120411 Genomic DNA. No translation available.
    AC153986 Genomic DNA. No translation available.
    AC156506 Genomic DNA. No translation available.
    M75986 Genomic DNA. Translation: AAA39316.1 .
    M75987 Genomic DNA. Translation: AAA39317.1 .
    BC003271 mRNA. Translation: AAH03271.1 . Different initiation.
    M21530 mRNA. Translation: AAA88319.1 . Different initiation.
    CCDSi CCDS51869.1. [P11881-1 ]
    PIRi S04844. ACMSIT.
    RefSeqi NP_034715.3. NM_010585.5. [P11881-1 ]
    XP_006505693.1. XM_006505630.1. [P11881-2 ]
    XP_006505699.1. XM_006505636.1. [P11881-7 ]
    XP_006505700.1. XM_006505637.1. [P11881-8 ]
    UniGenei Mm.227912.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N4K X-ray 2.20 A 224-604 [» ]
    1XZZ X-ray 1.80 A 2-223 [» ]
    ProteinModelPortali P11881.
    SMRi P11881. Positions 7-580.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200847. 17 interactions.
    DIPi DIP-32243N.
    IntActi P11881. 9 interactions.
    MINTi MINT-4099099.

    Chemistry

    BindingDBi P11881.

    PTM databases

    PhosphoSitei P11881.

    Proteomic databases

    MaxQBi P11881.
    PaxDbi P11881.
    PRIDEi P11881.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032192 ; ENSMUSP00000032192 ; ENSMUSG00000030102 . [P11881-1 ]
    GeneIDi 16438.
    KEGGi mmu:16438.
    UCSCi uc009ddh.3. mouse. [P11881-1 ]

    Organism-specific databases

    CTDi 3708.
    MGIi MGI:96623. Itpr1.

    Phylogenomic databases

    eggNOGi NOG280601.
    GeneTreei ENSGT00690000102000.
    HOGENOMi HOG000007660.
    HOVERGENi HBG052158.
    InParanoidi P11881.
    KOi K04958.
    OMAi KAFTTFR.
    OrthoDBi EOG76HQ0M.
    PhylomeDBi P11881.
    TreeFami TF312815.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188269. DAG and IP3 signaling.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_219232. Effects of PIP2 hydrolysis.
    REACT_221970. Ca2+ pathway.
    REACT_227667. Elevation of cytosolic Ca2+ levels.

    Miscellaneous databases

    ChiTaRSi ITPR1. mouse.
    EvolutionaryTracei P11881.
    NextBioi 289681.
    PROi P11881.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11881.
    Bgeei P11881.
    CleanExi MM_ITPR1.
    Genevestigatori P11881.

    Family and domain databases

    Gene3Di 1.25.10.30. 2 hits.
    InterProi IPR014821. Ins145_P3_rcpt.
    IPR000493. InsP3_rcpt-bd.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR015925. Ryanodine_recept-rel.
    [Graphical view ]
    PANTHERi PTHR13715. PTHR13715. 1 hit.
    Pfami PF08709. Ins145_P3_rec. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02815. MIR. 1 hit.
    PF08454. RIH_assoc. 1 hit.
    PF01365. RYDR_ITPR. 2 hits.
    [Graphical view ]
    PRINTSi PR00779. INSP3RECEPTR.
    SMARTi SM00472. MIR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF100909. SSF100909. 2 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEi PS50919. MIR. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400."
      Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N., Mikoshiba K.
      Nature 342:32-38(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Purkinje cell.
    2. "Nucleotide sequence of cDNA encoding P400 protein in the mouse cerebellum."
      Furuichi T., Yoshikawa S., Mikoshiba K.
      Nucleic Acids Res. 17:5385-5386(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: ICR.
      Tissue: Cerebellum.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner."
      Nakagawa T., Okano H., Furuichi T., Aruga J., Mikoshiba K.
      Proc. Natl. Acad. Sci. U.S.A. 88:6244-6248(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, ALTERNATIVE SPLICING.
      Strain: ICR.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 862-871, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749.
    7. "cDNA cloning and characterization of three genes uniquely expressed in cerebellum by Purkinje neurons."
      Nordquist D.T., Kozak C.A., Orr H.T.
      J. Neurosci. 8:4780-4789(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2250-2749.
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    8. "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor."
      Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.
      J. Biol. Chem. 278:10602-10612(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AHCYL1.
    9. "Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44."
      Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.
      Cell 120:85-98(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERP44, MUTAGENESIS OF CYS-2496; CYS-2504 AND CYS-2527.
    10. Cited for: INTERACTION WITH AHCYL1.
    11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis."
      Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I.
      J. Cell Biol. 186:783-792(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening."
      Yamazaki H., Chan J., Ikura M., Michikawa T., Mikoshiba K.
      J. Biol. Chem. 285:36081-36091(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-167 AND LYS-168.
    14. "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding protein in T and B lymphocytes."
      Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K., Hamabashiri M., Tanaka M., Shirasawa S.
      FEBS Open Bio 2:255-259(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TESPA1.
    15. "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand."
      Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K., Tong K.I., Yoshikawa F., Furuichi T., Iwai M., Michikawa T., Mikoshiba K., Ikura M.
      Nature 420:696-700(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 224-604 IN COMPLEX WITH INOSITOL 1,4,5-TRISPHOSPHATE, MUTAGENESIS OF THR-267 AND TYR-567.
    16. "Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor."
      Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K., Ikura M.
      Mol. Cell 17:193-203(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-223.
    17. "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation."
      Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.
      Blood 109:552-559(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRVI1.

    Entry informationi

    Entry nameiITPR1_MOUSE
    AccessioniPrimary (citable) accession number: P11881
    Secondary accession number(s): P20943, Q99LG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 171 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Calcium appears to inhibit ligand binding to the receptor, most probably by interacting with a distinct calcium-binding protein which then inhibits the receptor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3