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Protein

Inositol 1,4,5-trisphosphate receptor type 3

Gene

ITPR3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22272227CytoplasmicSequence analysisAdd
BLAST
Transmembranei2228 – 224821HelicalSequence analysisAdd
BLAST
Topological domaini2249 – 22568ExtracellularSequence analysis
Transmembranei2257 – 227721HelicalSequence analysisAdd
BLAST
Topological domaini2278 – 22869CytoplasmicSequence analysis
Transmembranei2287 – 230418HelicalSequence analysisAdd
BLAST
Topological domaini2305 – 231814ExtracellularSequence analysisAdd
BLAST
Transmembranei2319 – 233921HelicalSequence analysisAdd
BLAST
Topological domaini2340 – 236122CytoplasmicSequence analysisAdd
BLAST
Transmembranei2362 – 238221HelicalSequence analysisAdd
BLAST
Topological domaini2383 – 2489107ExtracellularSequence analysisAdd
BLAST
Transmembranei2490 – 251021HelicalSequence analysisAdd
BLAST
Topological domaini2511 – 2664154CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • rough endoplasmic reticulum Source: CACAO
  • secretory granule Source: CACAO
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2853.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26642664Inositol 1,4,5-trisphosphate receptor type 3PRO_0000153927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei909 – 9091PhosphoserineBy similarity
Modified residuei927 – 9271PhosphoserineBy similarity
Modified residuei1806 – 18061PhosphoserineBy similarity
Modified residuei1825 – 18251PhosphoserineBy similarity
Modified residuei1827 – 18271PhosphoserineBy similarity
Modified residuei2602 – 26021PhosphoserineBy similarity
Modified residuei2663 – 26631PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8WN95.
PeptideAtlasiQ8WN95.
PRIDEiQ8WN95.

Interactioni

Subunit structurei

Homotetramer. Interacts with TRPC1, TRPC3 and TRPC4. Interacts with TRPV4 (By similarity). Interacts with SIGMAR1 (By similarity). Interacts with PML and AKT1 (By similarity). Interacts with LRMP (via coiled-coil domain) (By similarity). Interacts with CABP1. Interacts with TMBIM4/LFG4. Interacts with CEMIP (By similarity). Interacts with TESPA1 (By similarity). Interacts with TMEM203 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000047648.

Chemistry

BindingDBiQ8WN95.

Structurei

3D structure databases

ProteinModelPortaliQ8WN95.
SMRiQ8WN95. Positions 6-226, 237-602.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni507 – 5104Inositol 1,4,5-trisphosphate bindingBy similarity
Regioni567 – 5693Inositol 1,4,5-trisphosphate bindingBy similarity

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.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiQ8WN95.
KOiK04960.

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.

Q8WN95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMSSFLHI 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 PSYKGDASDP KAAGTGAQGR TGRRNAGEKI
360 370 380 390 400
KYRLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS
410 420 430 440 450
TNVPIDVEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS
460 470 480 490 500
MLASAVEKLH EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK
510 520 530 540 550
PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE LSDQKNAPYQ
560 570 580 590 600
HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
610 620 630 640 650
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE
660 670 680 690 700
LICKCVLDPK NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN
710 720 730 740 750
NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE
760 770 780 790 800
ISQQLGVDLI FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA
810 820 830 840 850
RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY LNNVVSEAVP
860 870 880 890 900
FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQAYED
910 920 930 940 950
PGGKNVRRST QGVGHMMSTM VLNRKQSVFG GPSLPAGAGA PEPLDGSKFE
960 970 980 990 1000
ENEDIVVMET KLKILEILQF ILNVRLDYRI SYLLSVFKKE FVEVFPMQDS
1010 1020 1030 1040 1050
GADGTAPAFD STTANMNLDR IGEQAEAMFG VGKTSSMLEV DDEGGRMLLR
1060 1070 1080 1090 1100
VLIHLTMHDY APLVSGALQL LFKHFSQRQE VMHTFKQVQL LISAQDVENY
1110 1120 1130 1140 1150
KVIKSELDRL RTMVEKSELW VDKKGASKGE EGEAGPAKDK KERPTDEEGF
1160 1170 1180 1190 1200
LHPPGEKSSE NYQIVKGILE RLNKMCGVGE QMRKKQQRLL KNMDAHKVML
1210 1220 1230 1240 1250
DLLQIPYDKG DAKMMEILRY THQFLQKFCA GNPGNQALLH KHLHLFLTPG
1260 1270 1280 1290 1300
LLEAETMQHI FLNNYQLCSE IGEPVLQHFV HLLATHGHHV QYLDFLHTVI
1310 1320 1330 1340 1350
KAEGKYVKKC QDMIMTEPAN AGDDVVVFYN DKASLAHLLD MMKAARDGVE
1360 1370 1380 1390 1400
DHSPLMYHIS LVDLLAACAE GKNVYTEIKC TSLLPLEDVV SVVTHEDCIT
1410 1420 1430 1440 1450
EVKMAYVNFV NHCYVDTEVE MKEIYTSNHI WTLFENFTLD MARVCSKREK
1460 1470 1480 1490 1500
RLADPALEKY VLTVVLDTIS AFFSSPFSEN STSLQTHQTI VVQLLQSTMR
1510 1520 1530 1540 1550
LLECPWLQQQ HKGSVEACIR TLAMVAKGRA ISLPMDLDAH ISSLLSSGAS
1560 1570 1580 1590 1600
CVAAAQRNAS NYKTATRAFP RVMPTANQWD YKNIIEKLQD IITALEERLR
1610 1620 1630 1640 1650
PLVQAELSVL VDVLHWPELL FLEGSDAYQR CESGGFLSKL IQHTKDLMES
1660 1670 1680 1690 1700
EEKLCVKVLR TLQQMLLKKT KYGDRGNQLR KMLLQNYLQN RKSSSRGDLP
1710 1720 1730 1740 1750
DPMGTGLDQD WSAIAATQCR LDKEGATKLV CDLITSTKNE KIFQESIGLA
1760 1770 1780 1790 1800
IRLLDGGNTE IQKSFYNLMT SDKKSERFFK VLHDRMKRAQ QETKSTVAVN
1810 1820 1830 1840 1850
MSDLGSQPRE DREQADPTSK GRVASFSMPS SSSRYALGPS LRRGHEVGER
1860 1870 1880 1890 1900
VQSNEMGTSV LIMQPILRFL QLLCENHNRD LQNFLRCQNN KTNYNLVCET
1910 1920 1930 1940 1950
LQFLDIMCGS TTGGLGLLGL YINEDNVGLV IQTLETLTEY CQGPCHENQT
1960 1970 1980 1990 2000
CIVTHESNGI DIITALILND ISPLCKYRMD LVLQLKDNAS KLLLALMESR
2010 2020 2030 2040 2050
HDSENAERIL ISLRPQELVD VIKKAYLQEE ERENSDVSPR EVGHNIYILA
2060 2070 2080 2090 2100
LQLSRHNKQL QHLLKPVKRI QEEEAEGISS MLSLNNKQLT QMLKSSAPVQ
2110 2120 2130 2140 2150
EQEEDPLAYY ENHTSQIEIV RQDRSMEQIV FPVPGICQFL TEETKHRLFT
2160 2170 2180 2190 2200
TTEQDEQGSK VSDLFDQPSF LHNEMEWQRK LRSMPLIYWF SRRMTLWGSI
2210 2220 2230 2240 2250
SFNLAVFINI IIAFFYPYVE GASTGVLGSP LISLLFWILI CFSIAALFTK
2260 2270 2280 2290 2300
RYSVRPLIVA LILRSIYYLG IGPTLNILGA LNLTNKIVFV VSFVGNRGTF
2310 2320 2330 2340 2350
IRGYKAMVMD MEFLYHVGYI LTSVLGLFAH ELFYSILLFD LIYREETLFN
2360 2370 2380 2390 2400
VIKSVTRNGR SILLTALLAL ILVYLFSIVG FLFLKDDFIL EVDRLPGNHS
2410 2420 2430 2440 2450
RANPLGMPHG AATFVNTCSG DNVDCVSGVS VPEVLAEDEE PDSTERACDT
2460 2470 2480 2490 2500
LLMCIVTVMN HGLRNGGGVG DILRKPSKDE SLFPARVVYD LLFFFIVIII
2510 2520 2530 2540 2550
VLNLIFGVII DTFADLRSEK QKKEEILKTT CFICGLERDK FDNKTVSFEE
2560 2570 2580 2590 2600
HIKFEHNMWN YLYFIVLVRV KNKTDYTGPE SYVAQMIKNK NLDWFPRMRA
2610 2620 2630 2640 2650
MSLVSSEGEG EQNEIRILQD KLSATMKLVS HLTAQLSELK EQMTEQRKRR
2660
QRLGFVDVQN CMSR
Length:2,664
Mass (Da):303,040
Last modified:March 1, 2002 - v1
Checksum:i9C2C9979146E19AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF402601 mRNA. Translation: AAL39078.1.
RefSeqiNP_776795.1. NM_174370.3.
UniGeneiBt.9025.

Genome annotation databases

GeneIDi281879.
KEGGibta:281879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF402601 mRNA. Translation: AAL39078.1.
RefSeqiNP_776795.1. NM_174370.3.
UniGeneiBt.9025.

3D structure databases

ProteinModelPortaliQ8WN95.
SMRiQ8WN95. Positions 6-226, 237-602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000047648.

Chemistry

BindingDBiQ8WN95.
ChEMBLiCHEMBL2853.

Proteomic databases

PaxDbiQ8WN95.
PeptideAtlasiQ8WN95.
PRIDEiQ8WN95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281879.
KEGGibta:281879.

Organism-specific databases

CTDi3710.

Phylogenomic databases

eggNOGiKOG3533. Eukaryota.
ENOG410XR97. LUCA.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiQ8WN95.
KOiK04960.

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

  1. "Localization of three types of the inositol 1,4,5-trisphosphate receptor/Ca2+ channel in the secretory granules and coupling with the Ca2+ storage proteins chromogranins A and B."
    Yoo S.H., Oh Y.S., Kang M.K., Huh Y.H., So S.H., Park H.S., Park H.Y.
    J. Biol. Chem. 276:45806-45812(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Adrenal medulla.

Entry informationi

Entry nameiITPR3_BOVIN
AccessioniPrimary (citable) accession number: Q8WN95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.