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Protein

Inositol 1,4,5-trisphosphate receptor type 3

Gene

Itpr3

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

Functioni

Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.2 Publications

GO - Molecular functioni

GO - Biological processi

  • calcium ion transport Source: MGI
  • calcium ion transport into cytosol Source: UniProtKB
  • cellular response to cAMP Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: Ensembl
  • long-term synaptic potentiation Source: MGI
  • memory Source: MGI
  • protein heterooligomerization Source: Ensembl
  • protein homooligomerization Source: Ensembl
  • response to calcium ion Source: MGI
  • sensory perception of bitter taste Source: MGI
  • sensory perception of sweet taste Source: MGI
  • sensory perception of umami taste Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

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-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 3
Alternative name(s):
IP3 receptor isoform 3
Short name:
IP3R 3
Short name:
InsP3R3
Type 3 inositol 1,4,5-trisphosphate receptor
Short name:
Type 3 InsP3 receptor
Gene namesi
Name:Itpr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:96624. Itpr3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22332233CytoplasmicSequence analysisAdd
BLAST
Transmembranei2234 – 225421HelicalSequence analysisAdd
BLAST
Topological domaini2255 – 22628ExtracellularSequence analysis
Transmembranei2263 – 228321HelicalSequence analysisAdd
BLAST
Topological domaini2284 – 22929CytoplasmicSequence analysis
Transmembranei2293 – 231018HelicalSequence analysisAdd
BLAST
Topological domaini2311 – 232414ExtracellularSequence analysisAdd
BLAST
Transmembranei2325 – 234521HelicalSequence analysisAdd
BLAST
Topological domaini2346 – 236722CytoplasmicSequence analysisAdd
BLAST
Transmembranei2368 – 238821HelicalSequence analysisAdd
BLAST
Topological domaini2389 – 2495107ExtracellularSequence analysisAdd
BLAST
Transmembranei2496 – 251621HelicalSequence analysisAdd
BLAST
Topological domaini2517 – 2670154CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • dendrite Source: Ensembl
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of plasma membrane Source: MGI
  • membrane Source: MGI
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: Ensembl
  • nuclear outer membrane Source: Ensembl
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681W → A: Loss of calcium flux. 1 Publication
Mutagenesisi507 – 5071K → A: Loss of binding activity. 1 Publication
Mutagenesisi510 – 5101R → A: Loss of binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26702670Inositol 1,4,5-trisphosphate receptor type 3PRO_0000153929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei916 – 9161PhosphoserineCombined sources
Modified residuei934 – 9341PhosphoserineCombined sources
Modified residuei1152 – 11521Phosphoserine1 Publication
Modified residuei1813 – 18131PhosphoserineBy similarity
Modified residuei1832 – 18321PhosphoserineCombined sources
Modified residuei1834 – 18341PhosphoserineBy similarity
Modified residuei2608 – 26081PhosphoserineBy similarity
Modified residuei2669 – 26691PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine residues (By similarity). Phosphorylated by AKT1 on serine and/or threonine residues.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP70227.
MaxQBiP70227.
PaxDbiP70227.
PeptideAtlasiP70227.
PRIDEiP70227.

PTM databases

iPTMnetiP70227.
PhosphoSiteiP70227.

Expressioni

Gene expression databases

BgeeiP70227.
CleanExiMM_ITPR3.
GenevisibleiP70227. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. Interacts with TRPV4 (By similarity). Interacts with SIGMAR1 (PubMed:11149946). Interacts with AKT1 and PML (PubMed:21030605). Interacts with LRMP (via coiled-coil domain) (PubMed:20071408). Interacts with CABP1 (By similarity). Interacts with TMBIM4/LFG4 (By similarity). Interacts with CEMIP (By similarity). Interacts with TESPA1 (PubMed:23650607). Interacts with TMEM203 (By similarity).By similarity4 Publications

Protein-protein interaction databases

BioGridi200849. 4 interactions.
IntActiP70227. 2 interactions.
STRINGi10090.ENSMUSP00000038150.

Structurei

Secondary structure

1
2670
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 2917Combined sources
Beta strandi35 – 384Combined sources
Helixi40 – 423Combined sources
Beta strandi45 – 473Combined sources
Helixi52 – 554Combined sources
Beta strandi57 – 604Combined sources
Helixi66 – 749Combined sources
Helixi84 – 11027Combined sources
Turni111 – 1133Combined sources
Beta strandi121 – 1266Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 14010Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi147 – 1559Combined sources
Helixi158 – 1603Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi182 – 1876Combined sources
Turni188 – 1903Combined sources
Beta strandi194 – 2018Combined sources
Beta strandi204 – 21411Combined sources
Beta strandi218 – 2236Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRRX-ray1.90A/B1-224[»]
ProteinModelPortaliP70227.
SMRiP70227. Positions 4-579.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70227.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 17361MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini174 – 22451MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 28857MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini295 – 37278MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini378 – 43457MIR 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 2705Inositol 1,4,5-trisphosphate binding
Regioni507 – 5104Inositol 1,4,5-trisphosphate binding
Regioni567 – 5693Inositol 1,4,5-trisphosphate binding

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.
InParanoidiP70227.
KOiK04960.
OMAiFVHELFY.
OrthoDBiEOG76HQ0M.
PhylomeDBiP70227.
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. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

P70227-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK
60 70 80 90 100
KFRDCLFKVC PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME
110 120 130 140 150
QKQNDTENKK VHGDVVKYGS VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV
160 170 180 190 200
TLDATGNEGS WLFIQPFWKL RSNGDNVVVG DKVILNPVNA GQPLHASNYE
210 220 230 240 250
LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV VRLFHAEQEK
260 270 280 290 300
FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
310 320 330 340 350
NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGLGAQGR TGRRNAGEKI
360 370 380 390 400
KYRLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS
410 420 430 440 450
TNAPIDVEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS
460 470 480 490 500
MLASAVEKLN EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK
510 520 530 540 550
PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE LSDQKNAPYQ
560 570 580 590 600
YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
610 620 630 640 650
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE
660 670 680 690 700
LICKCVLDPK NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN
710 720 730 740 750
NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE
760 770 780 790 800
ISKQLGVELL FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA
810 820 830 840 850
RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY LNNVVSEAVP
860 870 880 890 900
FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA
910 920 930 940 950
MLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPAGVGVPEQ
960 970 980 990 1000
LDRSKFEDNE HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE
1010 1020 1030 1040 1050
VFPMQDSGAD GTAPAFDSST ATMNLDRIGE QAEAMFGVGK TSSMLEVDDE
1060 1070 1080 1090 1100
GGRMFLRVLL HLTMHDYPSL VSGALQLLFK HFSQRQEAMH TFKQVQLLIS
1110 1120 1130 1140 1150
AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEVE AGATKDKKER
1160 1170 1180 1190 1200
PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
1210 1220 1230 1240 1250
DAHKVMLDLL QIPYDKSDNK MLEILRYTHQ FLQKFCAGNP GNQALLHKHL
1260 1270 1280 1290 1300
QLFLTPGLLE AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL
1310 1320 1330 1340 1350
DFLHTVIKAE GKYVKKCQDM IMTELTNAGD DVVVFYNDKA SLAHLLDMMK
1360 1370 1380 1390 1400
AARDGVEDHS PLMYHISLVD LLAACAEGKN VYTEIKCTSL LPLEDVVTVV
1410 1420 1430 1440 1450
THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL FENFTLDMAL
1460 1470 1480 1490 1500
VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ
1510 1520 1530 1540 1550
LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA
1560 1570 1580 1590 1600
LLSSGGSCSA AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIM
1610 1620 1630 1640 1650
ALEERLKPLV QAELSVLVDM LHWPELLFPE GSEAYQRCES GGFLSKLIRH
1660 1670 1680 1690 1700
TKGLMESEEK LCVKVLRTLQ QMLLKKSKFG DRGNQLRKML LQNYLQNRKS
1710 1720 1730 1740 1750
GARGELTDPT GSGLDQDWSA IAATQCRLDK EGATKLVCDL ITSTKNEKIF
1760 1770 1780 1790 1800
QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET
1810 1820 1830 1840 1850
KSTVAVNMSD LGSQPREDRE PADPATKGRV SSFSMPSSSR YLLGLGLHRG
1860 1870 1880 1890 1900
HDMSERAQNN EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY
1910 1920 1930 1940 1950
NLVCETLQFL DIMCGSTTGG LGLLGLYINE DNVGLVIQTL ETLTEYCQGP
1960 1970 1980 1990 2000
CHENQTCIVT HESNGIDIIT ALILNDISPL CKYRMDLVLQ LKDNASKLLL
2010 2020 2030 2040 2050
ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN SEVSPREVGH
2060 2070 2080 2090 2100
NIYILALQLS RHNKQLQHLL KPVRRIQEEE AEGISSMLSL NNKQLSQMLK
2110 2120 2130 2140 2150
SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET
2160 2170 2180 2190 2200
KHRLFTTTEQ DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM
2210 2220 2230 2240 2250
TLWGSISFNL AVFINIIIAF FYPYVEGAST GVLGSPLISL LFWILICFSI
2260 2270 2280 2290 2300
AALFTKRYSV RPLIVALILR SIYYLGIGPT LNILGALNLT NKIVFVVSFV
2310 2320 2330 2340 2350
GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY SILLFDLIYR
2360 2370 2380 2390 2400
EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR
2410 2420 2430 2440 2450
LPGNHSRASP LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEEPDST
2460 2470 2480 2490 2500
ERACDTLLMC IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF
2510 2520 2530 2540 2550
FIVIIIVLNL IFGVIIDTFA DLRSEKQKKE EILKTTCFIC GLERDKFDNK
2560 2570 2580 2590 2600
TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT DYTGPESYVA QMIKNKNLDW
2610 2620 2630 2640 2650
FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTS QLNELKEQMT
2660 2670
EQRKRRQRLG FVDVQNCMSR
Length:2,670
Mass (Da):304,275
Last modified:October 25, 2005 - v3
Checksum:i9B5BA808B195C58F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2406 – 24138SRASPLGM → FPPSRARR (PubMed:1374893).Curated
Sequence conflicti2430 – 24301D → E in M90088 (PubMed:1374893).Curated
Sequence conflicti2447 – 24471P → L in M90088 (PubMed:1374893).Curated
Sequence conflicti2605 – 26095RAMSL → LGSTS in M90088 (PubMed:1374893).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182289 mRNA. Translation: BAD90683.1.
AK028491 mRNA. Translation: BAC25977.1.
BC010323 mRNA. Translation: AAH10323.1.
M90088 mRNA. No translation available.
Z71174 mRNA. Translation: CAA94862.1.
CCDSiCCDS28560.1.
RefSeqiNP_542120.2. NM_080553.3.
UniGeneiMm.458106.

Genome annotation databases

EnsembliENSMUST00000049308; ENSMUSP00000038150; ENSMUSG00000042644.
GeneIDi16440.
KEGGimmu:16440.
UCSCiuc008bfi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182289 mRNA. Translation: BAD90683.1.
AK028491 mRNA. Translation: BAC25977.1.
BC010323 mRNA. Translation: AAH10323.1.
M90088 mRNA. No translation available.
Z71174 mRNA. Translation: CAA94862.1.
CCDSiCCDS28560.1.
RefSeqiNP_542120.2. NM_080553.3.
UniGeneiMm.458106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JRRX-ray1.90A/B1-224[»]
ProteinModelPortaliP70227.
SMRiP70227. Positions 4-579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200849. 4 interactions.
IntActiP70227. 2 interactions.
STRINGi10090.ENSMUSP00000038150.

PTM databases

iPTMnetiP70227.
PhosphoSiteiP70227.

Proteomic databases

EPDiP70227.
MaxQBiP70227.
PaxDbiP70227.
PeptideAtlasiP70227.
PRIDEiP70227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049308; ENSMUSP00000038150; ENSMUSG00000042644.
GeneIDi16440.
KEGGimmu:16440.
UCSCiuc008bfi.2. mouse.

Organism-specific databases

CTDi3710.
MGIiMGI:96624. Itpr3.

Phylogenomic databases

eggNOGiKOG3533. Eukaryota.
ENOG410XR97. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP70227.
KOiK04960.
OMAiFVHELFY.
OrthoDBiEOG76HQ0M.
PhylomeDBiP70227.
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-5578775. Ion homeostasis.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

ChiTaRSiItpr3. mouse.
EvolutionaryTraceiP70227.
PROiP70227.
SOURCEiSearch...

Gene expression databases

BgeeiP70227.
CleanExiMM_ITPR3.
GenevisibleiP70227. 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. 2 hits.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-trisphosphate receptors and identification of a novel type 2 receptor splice variant."
    Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T., Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.
    J. Biol. Chem. 280:10305-10317(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-507 AND ARG-510.
    Strain: C57BL/6J.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1857-2670.
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "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 2181-2670.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Three additional inositol 1,4,5-trisphosphate receptors: molecular cloning and differential localization in brain and peripheral tissues."
    Ross C.A., Danoff S.K., Schell M.J., Snyder S.H., Ullrich A.
    Proc. Natl. Acad. Sci. U.S.A. 89:4265-4269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2406-2609.
    Tissue: Placenta.
  5. "Isoform diversity of the inositol trisphosphate receptor in cell types of mouse origin."
    De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I., Vanlingen S., Gijsens A., Himpens B., Casteels R.
    Biochem. J. 322:575-583(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2433-2629.
    Strain: C3H/HeJ.
    Tissue: Embryo.
  6. "Regulating ankyrin dynamics: roles of sigma-1 receptors."
    Hayashi T., Su T.-P.
    Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIGMAR1.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934; SER-1832 AND SER-2669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-expressing cells."
    Shindo Y., Kim M.R., Miura H., Yuuki T., Kanda T., Hino A., Kusakabe Y.
    Chem. Senses 35:171-177(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRMP.
  10. "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 TRP-168.
  11. Cited for: FUNCTION, INTERACTION WITH PML AND AKT1, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  12. "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.
  13. "Structural studies of inositol 1,4,5-trisphosphate receptor: coupling ligand binding to channel gating."
    Chan J., Yamazaki H., Ishiyama N., Seo M.D., Mal T.K., Michikawa T., Mikoshiba K., Ikura M.
    J. Biol. Chem. 285:36092-36099(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-224.

Entry informationi

Entry nameiITPR3_MOUSE
AccessioniPrimary (citable) accession number: P70227
Secondary accession number(s): Q5DWM4, Q8CED5, Q91Z08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 25, 2005
Last modified: July 6, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.