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P11881

- ITPR1_MOUSE

UniProt

P11881 - ITPR1_MOUSE

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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

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

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
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

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
Complete GO annotation...

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

BgeeiP11881.
CleanExiMM_ITPR1.
ExpressionAtlasiP11881. baseline and differential.
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. 11 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.
GeneTreeiENSGT00760000119152.
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

        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 AAA88319.1 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. 11 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 ENSGT00760000119152.
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

Bgeei P11881.
CleanExi MM_ITPR1.
ExpressionAtlasi P11881. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 172 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