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Protein

Inositol 1,4,5-trisphosphate receptor type 1

Gene

Itpr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (PubMed:23542070). 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.4 Publications

GO - Molecular functioni

  • calcium channel inhibitor activity Source: MGI
  • calcium ion binding Source: GO_Central
  • calcium-release channel activity Source: UniProtKB
  • inositol 1,4,5 trisphosphate binding Source: GO_Central
  • inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  • calcium ion transport Source: MGI
  • endoplasmic reticulum calcium ion homeostasis Source: MGI
  • epithelial fluid transport Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  • negative regulation of calcium-mediated signaling Source: MGI
  • post-embryonic development Source: MGI
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • response to hypoxia Source: BHF-UCL
  • voluntary musculoskeletal movement Source: MGI
Complete GO annotation...

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

ReactomeiR-MMU-114508. Effects of PIP2 hydrolysis.
R-MMU-139853. Elevation of cytosolic Ca2+ levels.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-418457. cGMP effects.
R-MMU-5578775. Ion homeostasis.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:96623. Itpr1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 2273CytoplasmicSequence analysisAdd BLAST2273
Transmembranei2274 – 2294HelicalSequence analysisAdd BLAST21
Topological domaini2295 – 2305LumenalSequence analysisAdd BLAST11
Transmembranei2306 – 2326HelicalSequence analysisAdd BLAST21
Topological domaini2327 – 2352CytoplasmicSequence analysisAdd BLAST26
Transmembranei2353 – 2373HelicalSequence analysisAdd BLAST21
Topological domaini2374 – 2396LumenalSequence analysisAdd BLAST23
Transmembranei2397 – 2417HelicalSequence analysisAdd BLAST21
Topological domaini2418 – 2439CytoplasmicSequence analysisAdd BLAST22
Transmembranei2440 – 2460HelicalSequence analysisAdd BLAST21
Topological domaini2461 – 2569LumenalSequence analysisAdd BLAST109
Transmembranei2570 – 2590HelicalSequence analysisAdd BLAST21
Topological domaini2591 – 2749CytoplasmicSequence analysisAdd BLAST159

GO - Cellular componenti

  • calcineurin complex Source: MGI
  • cytoplasm Source: MGI
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • nuclear envelope Source: MGI
  • nuclear inner membrane Source: MGI
  • nucleolus Source: MGI
  • plasma membrane Source: GO_Central
  • platelet dense granule membrane Source: MGI
  • platelet dense tubular network Source: MGI
  • postsynaptic density Source: MGI
  • protein complex Source: MGI
  • sarcoplasmic reticulum Source: MGI
  • secretory granule membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi167Y → A: Nearly abolishes calcium flux. 1 Publication1
Mutagenesisi168K → A: Reduces calcium flux by about 50%. 1 Publication1
Mutagenesisi169L → A: Reduces calcium flux by about 50%. 1
Mutagenesisi267T → A: Abolishes inositol 1,4,5-triphosphate binding. 1 Publication1
Mutagenesisi567Y → A or F: Abolishes inositol 1,4,5-triphosphate binding. 1 Publication1
Mutagenesisi1588S → A: Increases interaction with AHCYL1; when associated with A-1755. 1
Mutagenesisi1588S → E: Decreases interaction with AHCYL1; when associated with A-1755. 1
Mutagenesisi1755S → A: Increases interaction with AHCYL1; when associated with A-1588. 1
Mutagenesisi1755S → E: Decreases interaction with AHCYL1; when associated with A-1588. 1
Mutagenesisi2496C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. 1 Publication1
Mutagenesisi2504C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. 1 Publication1
Mutagenesisi2527C → S: Complete loss of channel activity. Significant decrease of interaction with ERP44. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001539211 – 2749Inositol 1,4,5-trisphosphate receptor type 1Add BLAST2749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei482PhosphotyrosineSequence analysis1
Cross-linki916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1588PhosphoserineCombined sources1
Modified residuei1755Phosphoserine; by PKASequence analysisBy similarity1
Cross-linki1771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1884Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1901Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1924Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki2118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki2257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei2655PhosphotyrosineSequence analysis1

Post-translational modificationi

Phosphorylated by cAMP kinase (PKA). Phosphorylation prevents the ligand-induced opening of the calcium channels. Phosphorylation by PKA increases the interaction with inositol 1,4,5-trisphosphate and decreases the interaction with AHCYL1.1 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.
PeptideAtlasiP11881.
PRIDEiP11881.

PTM databases

iPTMnetiP11881.
PhosphoSitePlusiP11881.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030102.
CleanExiMM_ITPR1.
ExpressionAtlasiP11881. baseline and differential.
GenevisibleiP11881. MM.

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 MRVI1. Interacts with CABP1 (By similarity). Interacts with TESPA1. Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 (PubMed:23542070). Interacts with AHCYL2 (with lower affinity than with AHCYL1) (By similarity). Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (PubMed:23884412).By similarity8 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200847. 17 interactors.
DIPiDIP-32243N.
IntActiP11881. 14 interactors.
MINTiMINT-4099099.
STRINGi10090.ENSMUSP00000032192.

Structurei

Secondary structure

12749
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 23Combined sources10
Beta strandi25 – 30Combined sources6
Beta strandi36 – 39Combined sources4
Helixi41 – 43Combined sources3
Beta strandi46 – 48Combined sources3
Helixi53 – 56Combined sources4
Beta strandi58 – 61Combined sources4
Helixi67 – 74Combined sources8
Helixi86 – 109Combined sources24
Turni110 – 112Combined sources3
Beta strandi120 – 125Combined sources6
Turni126 – 129Combined sources4
Beta strandi130 – 139Combined sources10
Beta strandi141 – 143Combined sources3
Beta strandi146 – 154Combined sources9
Helixi157 – 159Combined sources3
Beta strandi161 – 167Combined sources7
Beta strandi181 – 189Combined sources9
Beta strandi193 – 199Combined sources7
Beta strandi201 – 205Combined sources5
Beta strandi207 – 213Combined sources7
Beta strandi217 – 223Combined sources7
Beta strandi239 – 244Combined sources6
Turni245 – 248Combined sources4
Beta strandi249 – 255Combined sources7
Beta strandi257 – 265Combined sources9
Beta strandi269 – 271Combined sources3
Helixi272 – 274Combined sources3
Helixi278 – 280Combined sources3
Beta strandi282 – 286Combined sources5
Beta strandi303 – 307Combined sources5
Turni308 – 310Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi353 – 359Combined sources7
Helixi364 – 366Combined sources3
Beta strandi368 – 371Combined sources4
Beta strandi388 – 392Combined sources5
Turni393 – 396Combined sources4
Beta strandi397 – 406Combined sources10
Beta strandi409 – 412Combined sources4
Beta strandi415 – 423Combined sources9
Beta strandi430 – 434Combined sources5
Helixi437 – 461Combined sources25
Helixi467 – 484Combined sources18
Turni485 – 487Combined sources3
Helixi495 – 499Combined sources5
Helixi504 – 512Combined sources9
Helixi515 – 524Combined sources10
Helixi525 – 527Combined sources3
Helixi547 – 564Combined sources18
Helixi568 – 585Combined sources18
Helixi589 – 599Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N4KX-ray2.20A224-604[»]
1XZZX-ray1.80A2-223[»]
ProteinModelPortaliP11881.
SMRiP11881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini112 – 166MIR 1PROSITE-ProRule annotationAdd BLAST55
Domaini173 – 223MIR 2PROSITE-ProRule annotationAdd BLAST51
Domaini231 – 287MIR 3PROSITE-ProRule annotationAdd BLAST57
Domaini294 – 373MIR 4PROSITE-ProRule annotationAdd BLAST80
Domaini379 – 435MIR 5PROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni265 – 269Inositol 1,4,5-trisphosphate binding5
Regioni508 – 511Inositol 1,4,5-trisphosphate binding4
Regioni567 – 569Inositol 1,4,5-trisphosphate binding3
Regioni2463 – 2528Interaction with ERP441 PublicationAdd BLAST66

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

eggNOGiKOG3533. Eukaryota.
ENOG410XR97. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP11881.
KOiK04958.
OMAiDPDDHYQ.
OrthoDBiEOG091G00T2.
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. AlignAdd to basket

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

        10         20         30         40         50
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP
60 70 80 90 100
KKFRDCLFKL CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK
110 120 130 140 150
KQNETENRKL LGTVIQYGNV IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT
160 170 180 190 200
LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD KVVLNPVNAG QPLHASSHQL
210 220 230 240 250
VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV RLFHAEQEKF
260 270 280 290 300
LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
310 320 330 340 350
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK
360 370 380 390 400
MVYSLVSVPE GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH
410 420 430 440 450
STNIPIDKEE EKPVMLKIGT SPLKEDKEAF AIVPVSPAEV RDLDFANDAS
460 470 480 490 500
KVLGSIAGKL EKGTITQNER RSVTKLLEDL VYFVTGGTNS GQDVLEVVFS
510 520 530 540 550
KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE LGDQRHAPFR
560 570 580 590 600
HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH
610 620 630 640 650
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE
660 670 680 690 700
LICKAVLNPT NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW
710 720 730 740 750
RDSNKEIRSK SVRELAQDAK EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL
760 770 780 790 800
AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP
810 820 830 840 850
VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV EEYLRDVVCQ
860 870 880 890 900
RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
910 920 930 940 950
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA
960 970 980 990 1000
PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE
1010 1020 1030 1040 1050
FDESNSQSSE TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL
1060 1070 1080 1090 1100
DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV
1110 1120 1130 1140 1150
QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD EPMDGASGEN
1160 1170 1180 1190 1200
EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
1210 1220 1230 1240 1250
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ
1260 1270 1280 1290 1300
NQALLHKHIN LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE
1310 1320 1330 1340 1350
THGRNVQYIK FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS
1360 1370 1380 1390 1400
FQTLIQMMRS ERDRMDENSP LMYHIHLVEL LAVCTEGKNV YTEIKCNSLL
1410 1420 1430 1440 1450
PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI YTSNHMWKLF
1460 1470 1480 1490 1500
ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT
1510 1520 1530 1540 1550
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI
1560 1570 1580 1590 1600
PVDLDSQVNN LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII
1610 1620 1630 1640 1650
ERLQDIVSAL EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG
1660 1670 1680 1690 1700
FICKLIKHTK QLLEENEEKL CIKVLQTLRE MMTKDRGYGE KQISIDESEN
1710 1720 1730 1740 1750
AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV NRYYGNIRPS
1760 1770 1780 1790 1800
GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK
1810 1820 1830 1840 1850
EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK
1860 1870 1880 1890 1900
KSEKFFKVFY DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA
1910 1920 1930 1940 1950
KEPTTQITEE VRDQLLEASA ATRKAFTTFR READPDDHYQ SGEGTQATTD
1960 1970 1980 1990 2000
KAKDDLEMSA VITIMQPILR FLQLLCENHN RDLQNFLRCQ NNKTNYNLVC
2010 2020 2030 2040 2050
ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT EYCQGPCHEN
2060 2070 2080 2090 2100
QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME
2110 2120 2130 2140 2150
SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN
2160 2170 2180 2190 2200
VGHNIYILAH QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL
2210 2220 2230 2240 2250
DRTMEQIVFP VPSICEFLTK ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF
2260 2270 2280 2290 2300
NEMNWQKKLR AQPVLYWCAR NMSFWSSISF NLAVLMNLLV AFFYPFKGVR
2310 2320 2330 2340 2350
GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI LRLIFSVGLQ
2360 2370 2380 2390 2400
PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI
2410 2420 2430 2440 2450
CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL
2460 2470 2480 2490 2500
VYLFSIVGYL FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET
2510 2520 2530 2540 2550
GENCTSPAPK EELLPAEETE QDKEHTCETL LMCIVTVLSH GLRSGGGVGD
2560 2570 2580 2590 2600
VLRKPSKEEP LFAARVIYDL LFFFMVIIIV LNLIFGVIID TFADLRSEKQ
2610 2620 2630 2640 2650
KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY LCFIVLVKVK
2660 2670 2680 2690 2700
DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK
2710 2720 2730 2740
LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH03271 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1264N → K in CAA33433 (PubMed:2554142).Curated1
Sequence conflicti2675P → L in CAA33433 (PubMed:2554142).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002691318 – 332Missing in isoform 2, isoform 4, isoform 6 and isoform 8. CuratedAdd BLAST15
Alternative sequenceiVSP_0026921692 – 1714Missing in isoform 7 and isoform 8. CuratedAdd BLAST23
Alternative sequenceiVSP_0026931715Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8. Curated1
Alternative sequenceiVSP_0026941716 – 1731Missing in isoform 5, isoform 6, isoform 7 and isoform 8. CuratedAdd BLAST16

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_017176897.1. XM_017321408.1. [P11881-3]
XP_017176899.1. XM_017321410.1. [P11881-4]
UniGeneiMm.227912.

Genome annotation databases

EnsembliENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
ENSMUST00000203615; ENSMUSP00000144880; ENSMUSG00000030102. [P11881-3]
GeneIDi16438.
KEGGimmu:16438.
UCSCiuc033itt.1. mouse. [P11881-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_017176897.1. XM_017321408.1. [P11881-3]
XP_017176899.1. XM_017321410.1. [P11881-4]
UniGeneiMm.227912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N4KX-ray2.20A224-604[»]
1XZZX-ray1.80A2-223[»]
ProteinModelPortaliP11881.
SMRiP11881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200847. 17 interactors.
DIPiDIP-32243N.
IntActiP11881. 14 interactors.
MINTiMINT-4099099.
STRINGi10090.ENSMUSP00000032192.

PTM databases

iPTMnetiP11881.
PhosphoSitePlusiP11881.

Proteomic databases

MaxQBiP11881.
PaxDbiP11881.
PeptideAtlasiP11881.
PRIDEiP11881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
ENSMUST00000203615; ENSMUSP00000144880; ENSMUSG00000030102. [P11881-3]
GeneIDi16438.
KEGGimmu:16438.
UCSCiuc033itt.1. mouse. [P11881-1]

Organism-specific databases

CTDi3708.
MGIiMGI:96623. Itpr1.

Phylogenomic databases

eggNOGiKOG3533. Eukaryota.
ENOG410XR97. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP11881.
KOiK04958.
OMAiDPDDHYQ.
OrthoDBiEOG091G00T2.
PhylomeDBiP11881.
TreeFamiTF312815.

Enzyme and pathway databases

ReactomeiR-MMU-114508. Effects of PIP2 hydrolysis.
R-MMU-139853. Elevation of cytosolic Ca2+ levels.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-418457. cGMP effects.
R-MMU-5578775. Ion homeostasis.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

ChiTaRSiItpr1. mouse.
EvolutionaryTraceiP11881.
PROiP11881.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030102.
CleanExiMM_ITPR1.
ExpressionAtlasiP11881. baseline and differential.
GenevisibleiP11881. MM.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.