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Protein

Inositol 1,4,5-trisphosphate receptor type 1

Gene

Itpr1

Organism
Rattus norvegicus (Rat)
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 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.By similarity

GO - Molecular functioni

GO - Biological processi

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-RNO-112043. PLC beta mediated events.
R-RNO-1489509. DAG and IP3 signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-2871809. FCERI mediated Ca+2 mobilization.
R-RNO-4086398. Ca2+ pathway.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-5218921. VEGFR2 mediated cell proliferation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-RNO-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:
IP-3-R
Short name:
IP3R 1
Short name:
InsP3R1
Type 1 inositol 1,4,5-trisphosphate receptor
Short name:
Type 1 InsP3 receptor
Gene namesi
Name:Itpr1
Synonyms:Insp3r
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2933. Itpr1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 2274CytoplasmicSequence analysisAdd BLAST2274
Transmembranei2275 – 2295HelicalSequence analysisAdd BLAST21
Topological domaini2296 – 2306LumenalSequence analysisAdd BLAST11
Transmembranei2307 – 2327HelicalSequence analysisAdd BLAST21
Topological domaini2328 – 2353CytoplasmicSequence analysisAdd BLAST26
Transmembranei2354 – 2374HelicalSequence analysisAdd BLAST21
Topological domaini2375 – 2397LumenalSequence analysisAdd BLAST23
Transmembranei2398 – 2418HelicalSequence analysisAdd BLAST21
Topological domaini2419 – 2440CytoplasmicSequence analysisAdd BLAST22
Transmembranei2441 – 2461HelicalSequence analysisAdd BLAST21
Topological domaini2462 – 2569LumenalSequence analysisAdd BLAST108
Transmembranei2570 – 2590HelicalSequence analysisAdd BLAST21
Topological domaini2591 – 2750CytoplasmicSequence analysisAdd BLAST160

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • endoplasmic reticulum membrane Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • membrane raft Source: RGD
  • neuronal cell body Source: RGD
  • nuclear envelope Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • protein complex Source: RGD
  • sarcoplasmic reticulum Source: RGD
  • secretory granule membrane Source: RGD
  • synaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001539221 – 2750Inositol 1,4,5-trisphosphate receptor type 1Add BLAST2750

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei482PhosphotyrosineSequence analysis1
Cross-linki916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1589PhosphoserineCombined sources1
Modified residuei1756PhosphoserineCombined sources1
Cross-linki1772Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1887Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1902Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1925Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki2119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki2258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei2656PhosphotyrosineSequence 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.By similarity
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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29994.
PRIDEiP29994.

PTM databases

iPTMnetiP29994.
PhosphoSitePlusiP29994.
SwissPalmiP29994.

Expressioni

Tissue specificityi

Isoform 3 is found in the brain while isoform 7 is found in the fetal brain and peripheral tissues.

Interactioni

Subunit structurei

omotetramer. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. 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. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. Interacts with MRVI1 and CABP1 (via N-terminus). Interacts with TESPA1. Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1. 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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Hap1P54256-12EBI-8614640,EBI-994549
Hap1P54256-24EBI-8614640,EBI-994554
HTTP428582EBI-8614640,EBI-466029From a different organism.
HttP511114EBI-8614640,EBI-9674649

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein phosphatase binding Source: RGD

Protein-protein interaction databases

BioGridi247302. 11 interactors.
DIPiDIP-29715N.
IntActiP29994. 4 interactors.
MINTiMINT-5026585.
STRINGi10116.ENSRNOP00000063885.

Chemistry databases

BindingDBiP29994.

Structurei

Secondary structure

12750
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
Turni41 – 43Combined sources3
Helixi53 – 56Combined sources4
Beta strandi57 – 61Combined sources5
Helixi67 – 74Combined sources8
Helixi87 – 108Combined sources22
Turni109 – 112Combined sources4
Beta strandi120 – 125Combined sources6
Turni126 – 129Combined sources4
Beta strandi130 – 139Combined sources10
Beta strandi141 – 143Combined sources3
Beta strandi147 – 154Combined sources8
Helixi157 – 159Combined sources3
Beta strandi161 – 167Combined sources7
Beta strandi181 – 189Combined sources9
Beta strandi193 – 199Combined sources7
Beta strandi201 – 203Combined sources3
Beta strandi207 – 213Combined sources7
Beta strandi217 – 224Combined sources8
Helixi226 – 228Combined sources3
Beta strandi239 – 244Combined sources6
Turni245 – 248Combined sources4
Beta strandi249 – 256Combined sources8
Beta strandi259 – 265Combined sources7
Helixi278 – 280Combined sources3
Beta strandi281 – 286Combined sources6
Beta strandi302 – 307Combined sources6
Turni308 – 310Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi353 – 359Combined sources7
Helixi364 – 366Combined sources3
Beta strandi368 – 374Combined sources7
Beta strandi387 – 392Combined sources6
Turni393 – 395Combined sources3
Beta strandi398 – 406Combined sources9
Beta strandi408 – 412Combined sources5
Beta strandi415 – 423Combined sources9
Beta strandi430 – 434Combined sources5
Helixi437 – 462Combined sources26
Helixi467 – 483Combined sources17
Helixi504 – 512Combined sources9
Helixi515 – 522Combined sources8
Helixi552 – 562Combined sources11
Turni563 – 566Combined sources4
Helixi568 – 575Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JAVelectron microscopy4.70A/B/C/D1-2750[»]
3T8SX-ray3.77A/B7-602[»]
3UJ0X-ray3.60A/B1-604[»]
3UJ4X-ray3.00A/B1-604[»]
ProteinModelPortaliP29994.
SMRiP29994.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity5
Regioni508 – 511Inositol 1,4,5-trisphosphate bindingBy similarity4
Regioni567 – 569Inositol 1,4,5-trisphosphate bindingBy similarity3
Regioni2464 – 2529Interaction with ERP44Add 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.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP29994.
KOiK04958.
PhylomeDBiP29994.

Family and domain databases

Gene3Di1.25.10.30. 2 hits.
InterProiIPR016024. ARM-type_fold.
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]
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.
SSF48371. SSF48371. 4 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: P29994-1) [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 EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL
760 770 780 790 800
AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP
810 820 830 840 850
VKYARLWSEI PSEIAIDDYD SSGASKDEIK 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 LFMYHIHLVE LLAVCTEGKN VYTEIKCNSL
1410 1420 1430 1440 1450
LPLDDIVRVV THEDCIPEVK IAYINFLNHC YVDTEVEMKE IYTSNHMWKL
1460 1470 1480 1490 1500
FENFLVDICR ACNNTSDRKH ADSVLEKYVT EIVMSIVTTF FSSPFSDQST
1510 1520 1530 1540 1550
TLQTRQPVFV QLLQGVFRVY HCNWLMPSQK ASVESCIRVL SDVAKSRAIA
1560 1570 1580 1590 1600
IPVDLDSQVN NLFLKSHNIV QKTAMNWRLS ARNAARRDSV LAASRDYRNI
1610 1620 1630 1640 1650
IERLQDIVSA LEDRLRPLVQ AELSVLVDVL HRPELLFPEN TDARRKCESG
1660 1670 1680 1690 1700
GFICKLIKHT KQLLEENEEK LCIKVLQTLR EMMTKDRGYG EKQISIDELE
1710 1720 1730 1740 1750
NAELPQPPEA ENSTEQELEP SPPLRQLEDH KRGEALRQIL VNRYYGNIRP
1760 1770 1780 1790 1800
SGRRESLTSF GNGPLSPGGP SKPGGGGGGP GSGSTSRGEM SLAEVQCHLD
1810 1820 1830 1840 1850
KEGASNLVID LIMNASSDRV FHESILLAIA LLEGGNTTIQ HSFFCRLTED
1860 1870 1880 1890 1900
KKSEKFFKVF YDRMKVAQQE IKATVTVNTS DLGNKKKDDE VDRDAPSRKK
1910 1920 1930 1940 1950
AKEPTTQITE EVRDQLLEAS AATRKAFTTF RREADPDDHY QSGEGTQATT
1960 1970 1980 1990 2000
DKAKDDLEMS AVITIMQPIL RFLQLLCENH NRDLQNFLRC QNNKTNYNLV
2010 2020 2030 2040 2050
CETLQFLDCI CGSTTGGLGL LGLYINEKNV ALINQTLESL TEYCQGPCHE
2060 2070 2080 2090 2100
NQNCIATHES NGIDIITALI LNDINPLGKK RMDLVLELKN NASKLLLAIM
2110 2120 2130 2140 2150
ESRHDSENAE RILYNMRPKE LVEVIKKAYM QGEVEFEDGE NGEDGAASPR
2160 2170 2180 2190 2200
NVGHNIYILA HQLARHNKEL QTMLKPGGQV DGDEALEFYA KHTAQIEIVR
2210 2220 2230 2240 2250
LDRTMEQIVF PVPSICEFLT KESKLRIYYT TERDEQGSKI NDFFLRSEDL
2260 2270 2280 2290 2300
FNEMNWQKKL RAQPVLYWCA RNMSFWSSIS FNLAVLMNLL VAFFYPFKGV
2310 2320 2330 2340 2350
RGGTLEPHWS GLLWTAMLIS LAIVIALPKP HGIRALIAST ILRLIFSVGL
2360 2370 2380 2390 2400
QPTLFLLGAF NVCNKIIFLM SFVGNCGTFT RGYRAMVLDV EFLYHLLYLL
2410 2420 2430 2440 2450
ICAMGLFVHE FFYSLLLFDL VYREETLLNV IKSVTRNGRP IILTAALALI
2460 2470 2480 2490 2500
LVYLFSIVGY LFFKDDFILE VDRLPNETAG PETGESLAND FLYSDVCRVE
2510 2520 2530 2540 2550
TGENCTSPAP KEELLPVEET EQDKEHTCET LLMCIVTVLS HGLRSGGGVG
2560 2570 2580 2590 2600
DVLRKPSKEE PLFAARVIYD LLFFFMVIII VLNLIFGVII DTFADLRSEK
2610 2620 2630 2640 2650
QKKEEILKTT CFICGLERDK FDNKTVTFEE HIKEEHNMWH YLCFIVLVKV
2660 2670 2680 2690 2700
KDSTEYTGPE SYVAEMIRER NLDWFPRMRA MSLVSSDSEG EQNELRNLQE
2710 2720 2730 2740 2750
KLESTMKLVT NLSGQLSELK DQMTEQRKQK QRIGLLGHPP HMNVNPQQPA
Length:2,750
Mass (Da):313,264
Last modified:November 2, 2001 - v2
Checksum:i174BB77CBF6F21AC
GO
Isoform 2 (identifier: P29994-2) [UniParc]FASTAAdd to basket
Also known as: SI-SIIABC

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.

Show »
Length:2,735
Mass (Da):311,498
Checksum:iA80CC16884635058
GO
Isoform 3 (identifier: P29994-3) [UniParc]FASTAAdd to basket
Also known as: SISIIAC

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

Show »
Length:2,749
Mass (Da):313,136
Checksum:iE80D784F7201E2C9
GO
Isoform 4 (identifier: P29994-4) [UniParc]FASTAAdd to basket
Also known as: SI-SIIAC

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1716-1716: Missing.

Show »
Length:2,734
Mass (Da):311,370
Checksum:iEF7B6C747E701605
GO
Isoform 5 (identifier: P29994-5) [UniParc]FASTAAdd to basket
Also known as: SISIIA

The sequence of this isoform differs from the canonical sequence as follows:
     1716-1716: Missing.
     1717-1732: Missing.

Show »
Length:2,733
Mass (Da):311,210
Checksum:i3BE4A15DD99264F5
GO
Isoform 6 (identifier: P29994-6) [UniParc]FASTAAdd to basket
Also known as: SI-SIIA

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1716-1716: Missing.
     1717-1732: Missing.

Show »
Length:2,718
Mass (Da):309,444
Checksum:iFBE35154A6AF0190
GO
Isoform 7 (identifier: P29994-7) [UniParc]FASTAAdd to basket
Also known as: SISII

The sequence of this isoform differs from the canonical sequence as follows:
     1693-1715: Missing.
     1716-1716: Missing.
     1717-1732: Missing.

Show »
Length:2,710
Mass (Da):308,674
Checksum:i6A7FF31BC8448BFD
GO
Isoform 8 (identifier: P29994-8) [UniParc]FASTAAdd to basket
Also known as: SI-SII

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1693-1715: Missing.
     1716-1716: Missing.
     1717-1732: Missing.

Show »
Length:2,695
Mass (Da):306,909
Checksum:i81B8B4551AB0814F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1764P → R in AAA41447 (PubMed:1849282).Curated1
Sequence conflicti1764P → R in AAA41448 (PubMed:1849282).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1372Missing in all but PI17 clones. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002695322 – 336Missing in isoform 2, isoform 4, isoform 6 and isoform 8. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_0026961693 – 1715Missing in isoform 7 and isoform 8. CuratedAdd BLAST23
Alternative sequenceiVSP_0026971716Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8. 1 Publication1
Alternative sequenceiVSP_0026981717 – 1732Missing in isoform 5, isoform 6, isoform 7 and isoform 8. CuratedAdd BLAST16

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05510 mRNA. Translation: AAA41358.1.
J05510 mRNA. Translation: AAA41357.1.
M64699 mRNA. Translation: AAA41447.1.
M64698 mRNA. Translation: AAA41448.1.
U38653 mRNA. Translation: AAC53099.1.
U38812 mRNA. Translation: AAC53100.1.
U38665 mRNA. Translation: AAB51330.1.
PIRiA36579.
B36579.
RefSeqiNP_001257526.1. NM_001270597.1.
UniGeneiRn.2135.

Genome annotation databases

GeneIDi25262.
KEGGirno:25262.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05510 mRNA. Translation: AAA41358.1.
J05510 mRNA. Translation: AAA41357.1.
M64699 mRNA. Translation: AAA41447.1.
M64698 mRNA. Translation: AAA41448.1.
U38653 mRNA. Translation: AAC53099.1.
U38812 mRNA. Translation: AAC53100.1.
U38665 mRNA. Translation: AAB51330.1.
PIRiA36579.
B36579.
RefSeqiNP_001257526.1. NM_001270597.1.
UniGeneiRn.2135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JAVelectron microscopy4.70A/B/C/D1-2750[»]
3T8SX-ray3.77A/B7-602[»]
3UJ0X-ray3.60A/B1-604[»]
3UJ4X-ray3.00A/B1-604[»]
ProteinModelPortaliP29994.
SMRiP29994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247302. 11 interactors.
DIPiDIP-29715N.
IntActiP29994. 4 interactors.
MINTiMINT-5026585.
STRINGi10116.ENSRNOP00000063885.

Chemistry databases

BindingDBiP29994.
ChEMBLiCHEMBL2804.

PTM databases

iPTMnetiP29994.
PhosphoSitePlusiP29994.
SwissPalmiP29994.

Proteomic databases

PaxDbiP29994.
PRIDEiP29994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25262.
KEGGirno:25262.

Organism-specific databases

CTDi3708.
RGDi2933. Itpr1.

Phylogenomic databases

eggNOGiKOG3533. Eukaryota.
ENOG410XR97. LUCA.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP29994.
KOiK04958.
PhylomeDBiP29994.

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-1489509. DAG and IP3 signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-2871809. FCERI mediated Ca+2 mobilization.
R-RNO-4086398. Ca2+ pathway.
R-RNO-422356. Regulation of insulin secretion.
R-RNO-5218921. VEGFR2 mediated cell proliferation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-RNO-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

PROiP29994.

Family and domain databases

Gene3Di1.25.10.30. 2 hits.
InterProiIPR016024. ARM-type_fold.
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]
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.
SSF48371. SSF48371. 4 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITPR1_RAT
AccessioniPrimary (citable) accession number: P29994
Secondary accession number(s): Q62869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 2, 2001
Last modified: November 2, 2016
This is version 164 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.