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P11881 (ITPR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Itpr1
Synonyms:Insp3r, Pcd6, Pcp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2749 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.12 Ref.13

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.16

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.

Domain

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.

Post-translational modification

Phosphorylated by cAMP kinase. Phosphorylation prevents the ligand-induced opening of the calcium channels.

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.

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.

Sequence similarities

Belongs to the InsP3 receptor family.

Contains 5 MIR domains.

Sequence caution

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.

Ontologies

Keywords
   Biological processApoptosis
Calcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from direct assay PubMed 16014380. Source: MGI

endoplasmic reticulum calcium ion homeostasis

Inferred from genetic interaction PubMed 15613488. Source: MGI

inositol phosphate-mediated signaling

Inferred from direct assay PubMed 17327232Ref.13. Source: GOC

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.12. Source: UniProtKB

post-embryonic development

Inferred from mutant phenotype PubMed 17590087. Source: MGI

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype Ref.12. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 19120137. Source: BHF-UCL

voluntary musculoskeletal movement

Inferred from mutant phenotype PubMed 17590087. Source: MGI

   Cellular_componentcalcineurin complex

Inferred from direct assay PubMed 12617961. Source: MGI

cytoplasm

Inferred from direct assay PubMed 9858485. Source: MGI

endoplasmic reticulum

Traceable author statement Ref.4. Source: MGI

endoplasmic reticulum membrane

Inferred from direct assay PubMed 15613488. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from direct assay PubMed 16014380. Source: MGI

nuclear inner membrane

Inferred from direct assay PubMed 16014380. Source: MGI

nucleolus

Inferred from direct assay PubMed 16014380. Source: MGI

platelet dense granule membrane

Inferred from electronic annotation. Source: Ensembl

platelet dense tubular network

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from direct assay PubMed 15579147. Source: MGI

protein complex

Inferred from physical interaction PubMed 17416589. Source: MGI

sarcoplasmic reticulum

Inferred from direct assay PubMed 16014380. Source: MGI

   Molecular_functioninositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from direct assay Ref.13. Source: UniProtKB

intracellular ligand-gated calcium channel activity

Inferred from direct assay Ref.13. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Erp44Q9D1Q65EBI-541478,EBI-541567

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform 2 (identifier: P11881-2)

Also known as: SI-SIIABC;

The sequence of this isoform differs from the canonical sequence as follows:
     318-332: Missing.
Isoform 3 (identifier: P11881-3)

Also known as: SISIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     1715-1715: Missing.
Isoform 4 (identifier: P11881-4)

Also known as: SI-SIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     318-332: Missing.
     1715-1715: Missing.
Isoform 5 (identifier: P11881-5)

Also known as: SISIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     1715-1715: Missing.
     1716-1731: Missing.
Isoform 6 (identifier: P11881-6)

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.
Isoform 7 (identifier: P11881-7)

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.
Isoform 8 (identifier: P11881-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27492749Inositol 1,4,5-trisphosphate receptor type 1
PRO_0000153921

Regions

Topological domain1 – 22732273Cytoplasmic Potential
Transmembrane2274 – 229421Helical; Potential
Topological domain2295 – 230511Lumenal Potential
Transmembrane2306 – 232621Helical; Potential
Topological domain2327 – 235226Cytoplasmic Potential
Transmembrane2353 – 237321Helical; Potential
Topological domain2374 – 239623Lumenal Potential
Transmembrane2397 – 241721Helical; Potential
Topological domain2418 – 243922Cytoplasmic Potential
Transmembrane2440 – 246021Helical; Potential
Topological domain2461 – 2569109Lumenal Potential
Transmembrane2570 – 259021Helical; Potential
Topological domain2591 – 2749159Cytoplasmic Potential
Domain112 – 16655MIR 1
Domain173 – 22351MIR 2
Domain231 – 28757MIR 3
Domain294 – 37380MIR 4
Domain379 – 43557MIR 5
Region265 – 2695Inositol 1,4,5-trisphosphate binding
Region508 – 5114Inositol 1,4,5-trisphosphate binding
Region567 – 5693Inositol 1,4,5-trisphosphate binding
Region2463 – 252866Interaction with ERP44

Amino acid modifications

Modified residue4821Phosphotyrosine Potential
Modified residue15881Phosphoserine Ref.11
Modified residue17551Phosphoserine; by PKA Potential
Modified residue26551Phosphotyrosine Potential
Cross-link916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1884Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1901Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1924Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link2118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link2257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence318 – 33215Missing in isoform 2, isoform 4, isoform 6 and isoform 8.
VSP_002691
Alternative sequence1692 – 171423Missing in isoform 7 and isoform 8.
VSP_002692
Alternative sequence17151Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002693
Alternative sequence1716 – 173116Missing in isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002694

Experimental info

Mutagenesis1671Y → A: Nearly abolishes calcium flux. Ref.13
Mutagenesis1681K → A: Reduces calcium flux by about 50%. Ref.13
Mutagenesis1691L → A: Reduces calcium flux by about 50%.
Mutagenesis2671T → A: Abolishes inositol 1,4,5-triphosphate binding. Ref.14
Mutagenesis5671Y → A or F: Abolishes inositol 1,4,5-triphosphate binding. Ref.14
Mutagenesis24961C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. Ref.9
Mutagenesis25041C → S: No effect on channel activity. Significant decrease of interaction with ERP44. Complete loss of channel inhibition by ERP44. Ref.9
Mutagenesis25271C → S: Complete loss of channel activity. Significant decrease of interaction with ERP44. Ref.9
Sequence conflict12641N → K in CAA33433. Ref.1
Sequence conflict26751P → L in CAA33433. Ref.1

Secondary structure

.............................................................................................. 2749
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SISIIABC) [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: FC4CF3ABB85EB82B

FASTA2,749313,167
        10         20         30         40         50         60 
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL 

        70         80         90        100        110        120 
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV 

       130        140        150        160        170        180 
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD 

       190        200        210        220        230        240 
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV 

       250        260        270        280        290        300 
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 

       310        320        330        340        350        360 
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE 

       370        380        390        400        410        420 
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT 

       430        440        450        460        470        480 
SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL 

       490        500        510        520        530        540 
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE 

       550        560        570        580        590        600 
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 

       610        620        630        640        650        660 
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT 

       670        680        690        700        710        720 
NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK 

       730        740        750        760        770        780 
EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS 

       790        800        810        820        830        840 
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV 

       850        860        870        880        890        900 
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV 

       910        920        930        940        950        960 
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP 

       970        980        990       1000       1010       1020 
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG 

      1030       1040       1050       1060       1070       1080 
PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL 

      1090       1100       1110       1120       1130       1140 
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD 

      1150       1160       1170       1180       1190       1200 
EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ 

      1210       1220       1230       1240       1250       1260 
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN 

      1270       1280       1290       1300       1310       1320 
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG 

      1330       1340       1350       1360       1370       1380 
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LMYHIHLVEL 

      1390       1400       1410       1420       1430       1440 
LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI 

      1450       1460       1470       1480       1490       1500 
YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT 

      1510       1520       1530       1540       1550       1560 
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN 

      1570       1580       1590       1600       1610       1620 
LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL EDRLRPLVQA 

      1630       1640       1650       1660       1670       1680 
ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE 

      1690       1700       1710       1720       1730       1740 
MMTKDRGYGE KQISIDESEN AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV 

      1750       1760       1770       1780       1790       1800 
NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK 

      1810       1820       1830       1840       1850       1860 
EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK KSEKFFKVFY 

      1870       1880       1890       1900       1910       1920 
DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA KEPTTQITEE VRDQLLEASA 

      1930       1940       1950       1960       1970       1980 
ATRKAFTTFR READPDDHYQ SGEGTQATTD KAKDDLEMSA VITIMQPILR FLQLLCENHN 

      1990       2000       2010       2020       2030       2040 
RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT 

      2050       2060       2070       2080       2090       2100 
EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME 

      2110       2120       2130       2140       2150       2160 
SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN VGHNIYILAH 

      2170       2180       2190       2200       2210       2220 
QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL DRTMEQIVFP VPSICEFLTK 

      2230       2240       2250       2260       2270       2280 
ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR AQPVLYWCAR NMSFWSSISF 

      2290       2300       2310       2320       2330       2340 
NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI 

      2350       2360       2370       2380       2390       2400 
LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI 

      2410       2420       2430       2440       2450       2460 
CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL VYLFSIVGYL 

      2470       2480       2490       2500       2510       2520 
FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET GENCTSPAPK EELLPAEETE 

      2530       2540       2550       2560       2570       2580 
QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP LFAARVIYDL LFFFMVIIIV 

      2590       2600       2610       2620       2630       2640 
LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY 

      2650       2660       2670       2680       2690       2700 
LCFIVLVKVK DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK 

      2710       2720       2730       2740 
LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA 

« Hide

Isoform 2 (SI-SIIABC) [UniParc].

Checksum: FB3AE790B42F4CE7
Show »

FASTA2,734311,401
Isoform 3 (SISIIAC) [UniParc].

Checksum: 1230FF411AD4E5D2
Show »

FASTA2,748313,039
Isoform 4 (SI-SIIAC) [UniParc].

Checksum: 1424C44D6B2029D7
Show »

FASTA2,733311,273
Isoform 5 (SISIIA) [UniParc].

Checksum: E080B729B56533DE
Show »

FASTA2,732311,113
Isoform 6 (SI-SIIA) [UniParc].

Checksum: 8770BE568800564C
Show »

FASTA2,717309,347
Isoform 7 (SISII) [UniParc].

Checksum: 586D7A1358C19E69
Show »

FASTA2,709308,629
Isoform 8 (SI-SII) [UniParc].

Checksum: 3F2A34C1ACCB2CCF
Show »

FASTA2,694306,863

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Binding of IRBIT to the IP3 receptor: determinants and functional effects."
Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G., Missiaen L., Parys J.B., De Smedt H.
Biochem. Biophys. Res. Commun. 343:49-56(2006) [PubMed] [Europe PMC] [Abstract]
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]"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.
[15]"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.
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRACMSIT. S04844.
RefSeqNP_034715.3. NM_010585.5.
XP_006505693.1. XM_006505630.1.
XP_006505699.1. XM_006505636.1.
XP_006505700.1. XM_006505637.1.
UniGeneMm.227912.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4KX-ray2.20A224-604[»]
1XZZX-ray1.80A2-223[»]
ProteinModelPortalP11881.
SMRP11881. Positions 7-580.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200847. 17 interactions.
DIPDIP-32243N.
IntActP11881. 9 interactions.
MINTMINT-4099099.

Chemistry

BindingDBP11881.

PTM databases

PhosphoSiteP11881.

Proteomic databases

PaxDbP11881.
PRIDEP11881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
GeneID16438.
KEGGmmu:16438.
UCSCuc009ddh.3. mouse. [P11881-1]

Organism-specific databases

CTD3708.
MGIMGI:96623. Itpr1.

Phylogenomic databases

eggNOGNOG280601.
GeneTreeENSGT00690000102000.
HOGENOMHOG000007660.
HOVERGENHBG052158.
InParanoidP11881.
KOK04958.
OMAGENEHKK.
OrthoDBEOG76HQ0M.
PhylomeDBP11881.
TreeFamTF312815.

Gene expression databases

ArrayExpressP11881.
BgeeP11881.
CleanExMM_ITPR1.
GenevestigatorP11881.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR014821. 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]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. 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]
PRINTSPR00779. INSP3RECEPTR.
SMARTSM00472. MIR. 4 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITPR1. mouse.
EvolutionaryTraceP11881.
NextBio289681.
PROP11881.
SOURCESearch...

Entry information

Entry nameITPR1_MOUSE
AccessionPrimary (citable) accession number: P11881
Secondary accession number(s): P20943, Q99LG5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot