SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11881

- ITPR1_MOUSE

UniProt

P11881 - ITPR1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Inositol 1,4,5-trisphosphate receptor type 1
Gene
Itpr1, Insp3r, Pcd6, Pcp1
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
  4. protein binding Source: IntAct
Complete GO annotation...

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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22732273Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2274 – 229421Helical; Reviewed prediction
Add
BLAST
Topological domaini2295 – 230511Lumenal Reviewed prediction
Add
BLAST
Transmembranei2306 – 232621Helical; Reviewed prediction
Add
BLAST
Topological domaini2327 – 235226Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2353 – 237321Helical; Reviewed prediction
Add
BLAST
Topological domaini2374 – 239623Lumenal Reviewed prediction
Add
BLAST
Transmembranei2397 – 241721Helical; Reviewed prediction
Add
BLAST
Topological domaini2418 – 243922Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2440 – 246021Helical; Reviewed prediction
Add
BLAST
Topological domaini2461 – 2569109Lumenal Reviewed prediction
Add
BLAST
Transmembranei2570 – 259021Helical; Reviewed prediction
Add
BLAST
Topological domaini2591 – 2749159Cytoplasmic Reviewed prediction
Add
BLAST

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 1
PRO_0000153921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei482 – 4821Phosphotyrosine Reviewed prediction
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 PKA Reviewed prediction
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 – 26551Phosphotyrosine Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11881.
PaxDbiP11881.
PRIDEiP11881.

PTM databases

PhosphoSiteiP11881.

Expressioni

Gene expression databases

ArrayExpressiP11881.
BgeeiP11881.
CleanExiMM_ITPR1.
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 TESPA1.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200847. 17 interactions.
DIPiDIP-32243N.
IntActiP11881. 9 interactions.
MINTiMINT-4099099.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP11881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 16655MIR 1
Add
BLAST
Domaini173 – 22351MIR 2
Add
BLAST
Domaini231 – 28757MIR 3
Add
BLAST
Domaini294 – 37380MIR 4
Add
BLAST
Domaini379 – 43557MIR 5
Add
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 ERP44
Add
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.
Contains 5 MIR domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG280601.
GeneTreeiENSGT00690000102000.
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

MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP     50
KKFRDCLFKL CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK 100
KQNETENRKL LGTVIQYGNV IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT 150
LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD KVVLNPVNAG QPLHASSHQL 200
VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV RLFHAEQEKF 250
LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 300
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK 350
MVYSLVSVPE GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH 400
STNIPIDKEE EKPVMLKIGT SPLKEDKEAF AIVPVSPAEV RDLDFANDAS 450
KVLGSIAGKL EKGTITQNER RSVTKLLEDL VYFVTGGTNS GQDVLEVVFS 500
KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE LGDQRHAPFR 550
HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 600
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE 650
LICKAVLNPT NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW 700
RDSNKEIRSK SVRELAQDAK EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL 750
AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP 800
VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV EEYLRDVVCQ 850
RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV 900
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA 950
PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE 1000
FDESNSQSSE TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL 1050
DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV 1100
QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD EPMDGASGEN 1150
EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ 1200
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ 1250
NQALLHKHIN LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE 1300
THGRNVQYIK FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS 1350
FQTLIQMMRS ERDRMDENSP LMYHIHLVEL LAVCTEGKNV YTEIKCNSLL 1400
PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI YTSNHMWKLF 1450
ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT 1500
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI 1550
PVDLDSQVNN LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII 1600
ERLQDIVSAL EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG 1650
FICKLIKHTK QLLEENEEKL CIKVLQTLRE MMTKDRGYGE KQISIDESEN 1700
AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV NRYYGNIRPS 1750
GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK 1800
EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK 1850
KSEKFFKVFY DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA 1900
KEPTTQITEE VRDQLLEASA ATRKAFTTFR READPDDHYQ SGEGTQATTD 1950
KAKDDLEMSA VITIMQPILR FLQLLCENHN RDLQNFLRCQ NNKTNYNLVC 2000
ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT EYCQGPCHEN 2050
QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME 2100
SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN 2150
VGHNIYILAH QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL 2200
DRTMEQIVFP VPSICEFLTK ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF 2250
NEMNWQKKLR AQPVLYWCAR NMSFWSSISF NLAVLMNLLV AFFYPFKGVR 2300
GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI LRLIFSVGLQ 2350
PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI 2400
CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL 2450
VYLFSIVGYL FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET 2500
GENCTSPAPK EELLPAEETE QDKEHTCETL LMCIVTVLSH GLRSGGGVGD 2550
VLRKPSKEEP LFAARVIYDL LFFFMVIIIV LNLIFGVIID TFADLRSEKQ 2600
KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY LCFIVLVKVK 2650
DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK 2700
LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA 2749
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei318 – 33215Missing in isoform 2, isoform 4, isoform 6 and isoform 8.
VSP_002691Add
BLAST
Alternative sequencei1692 – 171423Missing in isoform 7 and isoform 8.
VSP_002692Add
BLAST
Alternative sequencei1715 – 17151Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002693
Alternative sequencei1716 – 173116Missing in isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002694Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1264 – 12641N → K in CAA33433. 1 Publication
Sequence conflicti2675 – 26751P → L in CAA33433. 1 Publication

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...

Protein-protein interaction databases

BioGridi 200847. 17 interactions.
DIPi DIP-32243N.
IntActi P11881. 9 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 ENSGT00690000102000.
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

ArrayExpressi P11881.
Bgeei P11881.
CleanExi MM_ITPR1.
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: September 3, 2014
This is version 170 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

Similar proteinsi