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P29994

- ITPR1_RAT

UniProt

P29994 - ITPR1_RAT

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Protein

Inositol 1,4,5-trisphosphate receptor type 1

Gene

Itpr1

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

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 complex binding Source: RGD
  5. protein C-terminus binding Source: RGD
  6. protein phosphatase binding Source: RGD

GO - Biological processi

  1. cellular response to cAMP Source: RGD
  2. cellular response to hypoxia Source: RGD
  3. inositol phosphate-mediated signaling Source: GOC
  4. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  5. negative regulation of neuron death Source: RGD
  6. positive regulation of calcium ion transport Source: RGD
  7. positive regulation of cytosolic calcium ion concentration Source: RGD
  8. release of sequestered calcium ion into cytosol Source: BHF-UCL
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_194374. Role of phospholipids in phagocytosis.
REACT_194690. Ca2+ pathway.
REACT_203734. FCERI mediated Ca+2 mobilization.
REACT_211910. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_220575. DAG and IP3 signaling.
REACT_221588. PLC beta mediated events.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol 1,4,5-trisphosphate receptor type 1
Alternative name(s):
IP3 receptor isoform 1
Short name:
IP-3-R
Short name:
IP3R 1
Short name:
InsP3R1
Type 1 inositol 1,4,5-trisphosphate receptor
Short name:
Type 1 InsP3 receptor
Gene namesi
Name:Itpr1
Synonyms:Insp3r
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2933. Itpr1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. dendrite Source: RGD
  3. endoplasmic reticulum membrane Source: RGD
  4. integral component of membrane Source: UniProtKB-KW
  5. intracellular membrane-bounded organelle Source: RGD
  6. membrane raft Source: RGD
  7. neuronal cell body Source: RGD
  8. nuclear envelope Source: RGD
  9. perinuclear region of cytoplasm Source: RGD
  10. plasma membrane Source: RGD
  11. postsynaptic density Source: RGD
  12. protein complex Source: RGD
  13. sarcoplasmic reticulum Source: RGD
  14. secretory granule membrane Source: RGD
  15. synaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27502750Inositol 1,4,5-trisphosphate receptor type 1PRO_0000153922Add
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)1 Publication
Cross-linki962 – 962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1572 – 1572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1589 – 15891PhosphoserineBy similarity
Modified residuei1756 – 17561Phosphoserine; by PKASequence Analysis
Cross-linki1772 – 1772Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1885 – 1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1886 – 1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1887 – 1887Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1902 – 1902Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1925 – 1925Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki2119 – 2119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki2258 – 2258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei2656 – 26561PhosphotyrosineSequence Analysis

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29994.
PRIDEiP29994.

PTM databases

PhosphoSiteiP29994.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP29994.

Interactioni

Subunit structurei

Homotetramer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity. The strength of this interaction inversely correlates with calcium concentration. Interacts with CABP1. Interacts with AHCYL1 and MRVI1 (By similarity). Interacts with TESPA1 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi247302. 11 interactions.
DIPiDIP-29715N.
IntActiP29994. 4 interactions.
MINTiMINT-5026585.

Structurei

Secondary structure

1
2750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 2310
Beta strandi25 – 306
Beta strandi36 – 394
Turni41 – 433
Helixi53 – 564
Beta strandi57 – 615
Helixi67 – 748
Helixi87 – 10822
Turni109 – 1124
Beta strandi120 – 1256
Turni126 – 1294
Beta strandi130 – 13910
Beta strandi141 – 1433
Beta strandi147 – 1548
Helixi157 – 1593
Beta strandi161 – 1677
Beta strandi181 – 1899
Beta strandi193 – 1997
Beta strandi201 – 2033
Beta strandi207 – 2137
Beta strandi217 – 2248
Helixi226 – 2283
Beta strandi239 – 2446
Turni245 – 2484
Beta strandi249 – 2568
Beta strandi259 – 2657
Helixi278 – 2803
Beta strandi281 – 2866
Beta strandi302 – 3076
Turni308 – 3103
Beta strandi313 – 3186
Beta strandi353 – 3597
Helixi364 – 3663
Beta strandi368 – 3747
Beta strandi387 – 3926
Turni393 – 3953
Beta strandi398 – 4069
Beta strandi408 – 4125
Beta strandi415 – 4239
Beta strandi430 – 4345
Helixi437 – 46226
Helixi467 – 48317
Helixi504 – 5129
Helixi515 – 5228
Helixi552 – 56211
Turni563 – 5664
Helixi568 – 5758

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T8SX-ray3.77A/B7-602[»]
3UJ0X-ray3.60A/B1-604[»]
3UJ4X-ray3.00A/B1-604[»]
ProteinModelPortaliP29994.
SMRiP29994. Positions 7-225, 236-602.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22742274CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini2296 – 230611LumenalSequence AnalysisAdd
BLAST
Topological domaini2328 – 235326CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini2375 – 239723LumenalSequence AnalysisAdd
BLAST
Topological domaini2419 – 244022CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini2462 – 2569108LumenalSequence AnalysisAdd
BLAST
Topological domaini2591 – 2750160CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2275 – 229521HelicalSequence AnalysisAdd
BLAST
Transmembranei2307 – 232721HelicalSequence AnalysisAdd
BLAST
Transmembranei2354 – 237421HelicalSequence AnalysisAdd
BLAST
Transmembranei2398 – 241821HelicalSequence AnalysisAdd
BLAST
Transmembranei2441 – 246121HelicalSequence 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 bindingBy similarity
Regioni508 – 5114Inositol 1,4,5-trisphosphate bindingBy similarity
Regioni567 – 5693Inositol 1,4,5-trisphosphate bindingBy similarity
Regioni2464 – 252966Interaction 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.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiP29994.
KOiK04958.
PhylomeDBiP29994.

Family and domain databases

Gene3Di1.25.10.30. 2 hits.
InterProiIPR016024. ARM-type_fold.
IPR014821. Ins145_P3_rcpt.
IPR000493. InsP3_rcpt-bd.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR015925. Ryanodine_recept-rel.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 1 hit.
PfamiPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
[Graphical view]
PRINTSiPR00779. INSP3RECEPTR.
SMARTiSM00472. MIR. 4 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF48371. SSF48371. 4 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50919. MIR. 5 hits.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. 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: P29994-1) [UniParc]FASTAAdd to Basket

Also known as: SISIIABC

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP
60 70 80 90 100
KKFRDCLFKL CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK
110 120 130 140 150
KQNETENRKL LGTVIQYGNV IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT
160 170 180 190 200
LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD KVVLNPVNAG QPLHASSHQL
210 220 230 240 250
VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV RLFHAEQEKF
260 270 280 290 300
LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
310 320 330 340 350
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK
360 370 380 390 400
MVYSLVSVPE GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH
410 420 430 440 450
STNIPIDKEE EKPVMLKIGT SPLKEDKEAF AIVPVSPAEV RDLDFANDAS
460 470 480 490 500
KVLGSIAGKL EKGTITQNER RSVTKLLEDL VYFVTGGTNS GQDVLEVVFS
510 520 530 540 550
KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE LGDQRHAPFR
560 570 580 590 600
HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH
610 620 630 640 650
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE
660 670 680 690 700
LICKAVLNPT NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW
710 720 730 740 750
RDSNKEIRSK SVRELAQDAK EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL
760 770 780 790 800
AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP
810 820 830 840 850
VKYARLWSEI PSEIAIDDYD SSGASKDEIK ERFAQTMEFV EEYLRDVVCQ
860 870 880 890 900
RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
910 920 930 940 950
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA
960 970 980 990 1000
PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE
1010 1020 1030 1040 1050
FDESNSQSSE TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL
1060 1070 1080 1090 1100
DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV
1110 1120 1130 1140 1150
QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD EPMDGASGEN
1160 1170 1180 1190 1200
EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
1210 1220 1230 1240 1250
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ
1260 1270 1280 1290 1300
NQALLHKHIN LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE
1310 1320 1330 1340 1350
THGRNVQYIK FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS
1360 1370 1380 1390 1400
FQTLIQMMRS ERDRMDENSP LFMYHIHLVE LLAVCTEGKN VYTEIKCNSL
1410 1420 1430 1440 1450
LPLDDIVRVV THEDCIPEVK IAYINFLNHC YVDTEVEMKE IYTSNHMWKL
1460 1470 1480 1490 1500
FENFLVDICR ACNNTSDRKH ADSVLEKYVT EIVMSIVTTF FSSPFSDQST
1510 1520 1530 1540 1550
TLQTRQPVFV QLLQGVFRVY HCNWLMPSQK ASVESCIRVL SDVAKSRAIA
1560 1570 1580 1590 1600
IPVDLDSQVN NLFLKSHNIV QKTAMNWRLS ARNAARRDSV LAASRDYRNI
1610 1620 1630 1640 1650
IERLQDIVSA LEDRLRPLVQ AELSVLVDVL HRPELLFPEN TDARRKCESG
1660 1670 1680 1690 1700
GFICKLIKHT KQLLEENEEK LCIKVLQTLR EMMTKDRGYG EKQISIDELE
1710 1720 1730 1740 1750
NAELPQPPEA ENSTEQELEP SPPLRQLEDH KRGEALRQIL VNRYYGNIRP
1760 1770 1780 1790 1800
SGRRESLTSF GNGPLSPGGP SKPGGGGGGP GSGSTSRGEM SLAEVQCHLD
1810 1820 1830 1840 1850
KEGASNLVID LIMNASSDRV FHESILLAIA LLEGGNTTIQ HSFFCRLTED
1860 1870 1880 1890 1900
KKSEKFFKVF YDRMKVAQQE IKATVTVNTS DLGNKKKDDE VDRDAPSRKK
1910 1920 1930 1940 1950
AKEPTTQITE EVRDQLLEAS AATRKAFTTF RREADPDDHY QSGEGTQATT
1960 1970 1980 1990 2000
DKAKDDLEMS AVITIMQPIL RFLQLLCENH NRDLQNFLRC QNNKTNYNLV
2010 2020 2030 2040 2050
CETLQFLDCI CGSTTGGLGL LGLYINEKNV ALINQTLESL TEYCQGPCHE
2060 2070 2080 2090 2100
NQNCIATHES NGIDIITALI LNDINPLGKK RMDLVLELKN NASKLLLAIM
2110 2120 2130 2140 2150
ESRHDSENAE RILYNMRPKE LVEVIKKAYM QGEVEFEDGE NGEDGAASPR
2160 2170 2180 2190 2200
NVGHNIYILA HQLARHNKEL QTMLKPGGQV DGDEALEFYA KHTAQIEIVR
2210 2220 2230 2240 2250
LDRTMEQIVF PVPSICEFLT KESKLRIYYT TERDEQGSKI NDFFLRSEDL
2260 2270 2280 2290 2300
FNEMNWQKKL RAQPVLYWCA RNMSFWSSIS FNLAVLMNLL VAFFYPFKGV
2310 2320 2330 2340 2350
RGGTLEPHWS GLLWTAMLIS LAIVIALPKP HGIRALIAST ILRLIFSVGL
2360 2370 2380 2390 2400
QPTLFLLGAF NVCNKIIFLM SFVGNCGTFT RGYRAMVLDV EFLYHLLYLL
2410 2420 2430 2440 2450
ICAMGLFVHE FFYSLLLFDL VYREETLLNV IKSVTRNGRP IILTAALALI
2460 2470 2480 2490 2500
LVYLFSIVGY LFFKDDFILE VDRLPNETAG PETGESLAND FLYSDVCRVE
2510 2520 2530 2540 2550
TGENCTSPAP KEELLPVEET EQDKEHTCET LLMCIVTVLS HGLRSGGGVG
2560 2570 2580 2590 2600
DVLRKPSKEE PLFAARVIYD LLFFFMVIII VLNLIFGVII DTFADLRSEK
2610 2620 2630 2640 2650
QKKEEILKTT CFICGLERDK FDNKTVTFEE HIKEEHNMWH YLCFIVLVKV
2660 2670 2680 2690 2700
KDSTEYTGPE SYVAEMIRER NLDWFPRMRA MSLVSSDSEG EQNELRNLQE
2710 2720 2730 2740 2750
KLESTMKLVT NLSGQLSELK DQMTEQRKQK QRIGLLGHPP HMNVNPQQPA
Length:2,750
Mass (Da):313,264
Last modified:November 2, 2001 - v2
Checksum:i174BB77CBF6F21AC
GO
Isoform 2 (identifier: P29994-2) [UniParc]FASTAAdd to Basket

Also known as: SI-SIIABC

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

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

Also known as: SISIIAC

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

Show »
Length:2,749
Mass (Da):313,136
Checksum:iE80D784F7201E2C9
GO
Isoform 4 (identifier: P29994-4) [UniParc]FASTAAdd to Basket

Also known as: SI-SIIAC

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

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

Also known as: SISIIA

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

Show »
Length:2,733
Mass (Da):311,210
Checksum:i3BE4A15DD99264F5
GO
Isoform 6 (identifier: P29994-6) [UniParc]FASTAAdd to Basket

Also known as: SI-SIIA

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

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

Also known as: SISII

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

Show »
Length:2,710
Mass (Da):308,674
Checksum:i6A7FF31BC8448BFD
GO
Isoform 8 (identifier: P29994-8) [UniParc]FASTAAdd to Basket

Also known as: SI-SII

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1764 – 17641P → R in AAA41447. (PubMed:1849282)Curated
Sequence conflicti1764 – 17641P → R in AAA41448. (PubMed:1849282)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1372 – 13721Missing in all but PI17 clones. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei322 – 33615Missing in isoform 2, isoform 4, isoform 6 and isoform 8. 1 PublicationVSP_002695Add
BLAST
Alternative sequencei1693 – 171523Missing in isoform 7 and isoform 8. CuratedVSP_002696Add
BLAST
Alternative sequencei1716 – 17161Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_002697
Alternative sequencei1717 – 173216Missing in isoform 5, isoform 6, isoform 7 and isoform 8. CuratedVSP_002698Add
BLAST

Sequence databases

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

Genome annotation databases

GeneIDi25262.
KEGGirno:25262.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05510 mRNA. Translation: AAA41358.1 .
J05510 mRNA. Translation: AAA41357.1 .
M64699 mRNA. Translation: AAA41447.1 .
M64698 mRNA. Translation: AAA41448.1 .
U38653 mRNA. Translation: AAC53099.1 .
U38812 mRNA. Translation: AAC53100.1 .
U38665 mRNA. Translation: AAB51330.1 .
PIRi A36579.
B36579.
RefSeqi NP_001257526.1. NM_001270597.1.
UniGenei Rn.2135.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3T8S X-ray 3.77 A/B 7-602 [» ]
3UJ0 X-ray 3.60 A/B 1-604 [» ]
3UJ4 X-ray 3.00 A/B 1-604 [» ]
ProteinModelPortali P29994.
SMRi P29994. Positions 7-225, 236-602.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247302. 11 interactions.
DIPi DIP-29715N.
IntActi P29994. 4 interactions.
MINTi MINT-5026585.

Chemistry

BindingDBi P29994.
ChEMBLi CHEMBL2804.

PTM databases

PhosphoSitei P29994.

Proteomic databases

PaxDbi P29994.
PRIDEi P29994.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25262.
KEGGi rno:25262.

Organism-specific databases

CTDi 3708.
RGDi 2933. Itpr1.

Phylogenomic databases

eggNOGi NOG280601.
HOGENOMi HOG000007660.
HOVERGENi HBG052158.
InParanoidi P29994.
KOi K04958.
PhylomeDBi P29994.

Enzyme and pathway databases

Reactomei REACT_194374. Role of phospholipids in phagocytosis.
REACT_194690. Ca2+ pathway.
REACT_203734. FCERI mediated Ca+2 mobilization.
REACT_211910. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_220575. DAG and IP3 signaling.
REACT_221588. PLC beta mediated events.

Miscellaneous databases

NextBioi 605915.
PROi P29994.

Gene expression databases

Genevestigatori P29994.

Family and domain databases

Gene3Di 1.25.10.30. 2 hits.
InterProi IPR016024. ARM-type_fold.
IPR014821. Ins145_P3_rcpt.
IPR000493. InsP3_rcpt-bd.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR015925. Ryanodine_recept-rel.
[Graphical view ]
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.
SSF48371. SSF48371. 4 hits.
SSF82109. SSF82109. 2 hits.
PROSITEi PS50919. MIR. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure and expression of the rat inositol 1,4,5-trisphosphate receptor."
    Mignery G.A., Newton C.L., Archer B.T. III, Suedhof T.C.
    J. Biol. Chem. 265:12679-12685(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT PHE-1372 DEL.
  2. "Inositol 1,4,5-trisphosphate receptors: distinct neuronal and nonneuronal forms derived by alternative splicing differ in phosphorylation."
    Danoff S.K., Ferris C.D., Donath C., Fischer G.A., Munemitsu S., Ullrich A., Snyder S.H., Ross C.A.
    Proc. Natl. Acad. Sci. U.S.A. 88:2951-2955(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 7).
    Tissue: Brain.
  3. "Inositol 1,4,5-trisphosphate receptor expression in mammalian olfactory tissue."
    Smutzer G., Zimmerman J.E., Hahn C.-G., Ruscheinsky D.D., Rodriguez A., Han L.-Y., Arnold S.E.
    Brain Res. Mol. Brain Res. 44:347-354(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 7 AND 8).
    Strain: Sprague-Dawley.
  4. "Subunit oligomerization, and topology of the inositol 1,4, 5-trisphosphate receptor."
    Galvan D.L., Borrego-Diaz E., Perez P.J., Mignery G.A.
    J. Biol. Chem. 274:29483-29492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels."
    Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F., Foskett J.K.
    Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CABP1.
  6. "Mass spectrometric analysis of type 1 inositol 1,4,5-trisphosphate receptor ubiquitination."
    Sliter D.A., Kubota K., Kirkpatrick D.S., Alzayady K.J., Gygi S.P., Wojcikiewicz R.J.
    J. Biol. Chem. 283:35319-35328(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-916; LYS-962; LYS-1572; LYS-1772; LYS-1885; LYS-1886; LYS-1887; LYS-1902; LYS-1925; LYS-2119 AND LYS-2258.

Entry informationi

Entry nameiITPR1_RAT
AccessioniPrimary (citable) accession number: P29994
Secondary accession number(s): Q62869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 2, 2001
Last modified: October 29, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Calcium appears to inhibit ligand binding to the receptor, most probably by interacting with a distinct calcium-binding protein which then inhibits the receptor.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3