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Database: UniProt
Entry: ITPR3_RAT
LinkDB: ITPR3_RAT
Original site: ITPR3_RAT 
ID   ITPR3_RAT               Reviewed;        2670 AA.
AC   Q63269;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 163.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 3;
DE   AltName: Full=IP3 receptor isoform 3;
DE            Short=IP3R 3;
DE            Short=InsP3R3;
DE   AltName: Full=Type 3 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 3 InsP3 receptor;
GN   Name=Itpr3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8388391;
RA   Blondel O., Takeda J., Janssen H., Seino S., Bell G.I.;
RT   "Sequence and functional characterization of a third inositol
RT   trisphosphate receptor subtype, IP3R-3, expressed in pancreatic
RT   islets, kidney, gastrointestinal tract, and other tissues.";
RL   J. Biol. Chem. 268:11356-11363(1993).
RN   [2]
RP   INTERACTION WITH SIGMAR1.
RX   PubMed=11149946; DOI=10.1073/pnas.98.2.491;
RA   Hayashi T., Su T.-P.;
RT   "Regulating ankyrin dynamics: roles of sigma-1 receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001).
RN   [3]
RP   INTERACTION WITH CABP1.
RX   PubMed=12032348; DOI=10.1073/pnas.102006299;
RA   Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K.,
RA   Haeseleer F., Foskett J.K.;
RT   "Identification of a family of calcium sensors as protein ligands of
RT   inositol trisphosphate receptor Ca(2+) release channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934 AND SER-2669, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [5]
RP   INTERACTION WITH BOK.
RX   PubMed=23884412; DOI=10.1074/jbc.M113.496570;
RA   Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.;
RT   "The Bcl-2 protein family member Bok binds to the coupling domain of
RT   inositol 1,4,5-trisphosphate receptors and protects them from
RT   proteolytic cleavage.";
RL   J. Biol. Chem. 288:25340-25349(2013).
CC   -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second
CC       messenger that mediates the release of intracellular calcium.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4.
CC       Interacts with TRPV4 (By similarity). Interacts with SIGMAR1
CC       (PubMed:11149946). Interacts with AKT1 and PML. Interacts with
CC       LRMP (via coiled-coil domain) (By similarity). Interacts with
CC       CABP1 (PubMed:12032348). Interacts with TMBIM4/LFG4 (By
CC       similarity). Interacts with CEMIP (By similarity). Interacts with
CC       TESPA1 (By similarity). Interacts with TMEM203 (By similarity).
CC       Interacts with BOK; regulates ITPR3 expression (PubMed:23884412).
CC       {ECO:0000250|UniProtKB:P70227, ECO:0000250|UniProtKB:Q14573,
CC       ECO:0000269|PubMed:11149946, ECO:0000269|PubMed:12032348,
CC       ECO:0000269|PubMed:23884412}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC       extremity. Its large N-terminal cytoplasmic region has the ligand-
CC       binding site in the N-terminus and modulatory sites in the middle
CC       portion immediately upstream of the channel region.
CC   -!- PTM: Phosphorylated on tyrosine residues. Phosphorylated by AKT1
CC       on serine and/or threonine residues (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
DR   EMBL; L06096; AAA41446.1; -; mRNA.
DR   PIR; A46719; A46719.
DR   RefSeq; NP_037270.1; NM_013138.1.
DR   UniGene; Rn.11242; -.
DR   ProteinModelPortal; Q63269; -.
DR   SMR; Q63269; -.
DR   BioGrid; 247708; 3.
DR   IntAct; Q63269; 1.
DR   STRING; 10116.ENSRNOP00000011516; -.
DR   ChEMBL; CHEMBL2846; -.
DR   TCDB; 1.A.3.2.5; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
DR   CarbonylDB; Q63269; -.
DR   iPTMnet; Q63269; -.
DR   PhosphoSitePlus; Q63269; -.
DR   jPOST; Q63269; -.
DR   PaxDb; Q63269; -.
DR   PRIDE; Q63269; -.
DR   GeneID; 25679; -.
DR   KEGG; rno:25679; -.
DR   UCSC; RGD:2934; rat.
DR   CTD; 3710; -.
DR   RGD; 2934; Itpr3.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q63269; -.
DR   KO; K04960; -.
DR   OrthoDB; 94996at2759; -.
DR   PhylomeDB; Q63269; -.
DR   PRO; PR:Q63269; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR   GO; GO:0005903; C:brush border; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SynGO.
DR   GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; TAS:RGD.
DR   GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; IDA:RGD.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:RGD.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:RGD.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:RGD.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; IDA:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR000699; RIH_dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR   PANTHER; PTHR13715; PTHR13715; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 4.
DR   SUPFAM; SSF100909; SSF100909; 2.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Complete proteome;
KW   Endoplasmic reticulum; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   2670       Inositol 1,4,5-trisphosphate receptor
FT                                type 3.
FT                                /FTId=PRO_0000153930.
FT   TOPO_DOM      1   2201       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2202   2222       Helical. {ECO:0000255}.
FT   TOPO_DOM   2223   2233       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2234   2254       Helical. {ECO:0000255}.
FT   TOPO_DOM   2255   2263       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2264   2284       Helical. {ECO:0000255}.
FT   TOPO_DOM   2285   2324       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2325   2345       Helical. {ECO:0000255}.
FT   TOPO_DOM   2346   2367       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2368   2388       Helical. {ECO:0000255}.
FT   TOPO_DOM   2389   2495       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2496   2516       Helical. {ECO:0000255}.
FT   TOPO_DOM   2517   2670       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      113    173       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      174    224       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      232    288       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      295    372       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      266    270       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      507    510       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   MOD_RES     916    916       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES     934    934       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1813   1813       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1832   1832       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1834   1834       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2608   2608       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2669   2669       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
SQ   SEQUENCE   2670 AA;  304286 MW;  13C787E4C2886E45 CRC64;
     MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC
     PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS
     VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG
     DKVILNPVNA GQPLHASNYE LSDNVGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV
     VRLFHAEQEK FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
     NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGPGAQSR TGRRNAGEKI KYRLVAVPHG
     NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNAPIDVEEE RPIRLMLGTC
     PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV
     FFVSDVPNNG QNVLDIMVTK PNRERQKLMR DENILKQIFG ILKAPFRDKG GEGPLVRLEE
     LSDQKNAPYQ YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE LICKCVLDPK
     NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN NEHHEKSVRQ LAQEARAGNA
     HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISKQLGVELL FLCMADEMLP FDLRASFCHL
     MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY
     LNNVVGEAVP FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA
     VLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPTGVGVPEQ LDRSKFEDNE
     HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSST
     ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLL HLTMHDYPPL VSGALQLLFK
     HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEGE
     AGASKDKKER PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
     DAHKVMLDLL QIPYDKNDNK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL QLFLTPGLLE
     AETMQHIFLN NYQLCSEISE PVLQHFVHCW PTHGRHVQYL DFLHTVIKAE GKYVKKCQDM
     IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN
     VYTEIKCTSL LPLEDVVSVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL
     FENFTLDMAL VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ
     LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA LLSSGGSCSA
     AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIT ALEERLKPLV QAELSVLVDM
     LHWPELLFLE GSEAYQRCES GGFLSKLIRH TKGLMESEEK LCVKVLRTLQ QMLQKKSKYG
     DRGNQLRKML LQNYLQNRKS GPRGELTDPT GSGVDQDWSA IAATQCRLDK EGATKLVCDL
     ITSTKNEKIF QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET
     KSTVAVNMSD LGSQPREDRE PADPTTKGRV SSFSMPSSSR YSLGPGLHRG HDVSERAQNN
     EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY NLVCETLQFL DIMCGSTTGG
     LGLLGLYINE DNVGLVIQTL ETLTEYCQGP CHENQTCIVT HESNGIDIIT ALILNDISPL
     CKYRMDLVLQ LKDNASKLLL ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN
     SEVSPREVGH NIYILALQLS RHNKQLQHLL KPVKRIQEEE AEGISSMLSL NNKQLSQMLK
     SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET KHRLFTTTEQ
     DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM TLWGSISFNL AVFINIIIAF
     FYPYVEGAST GVLGSPLISL LFWILICFSI AALFTKHYSV RPLIVALVLR SIYYLGIGPT
     LNILGALNLT NKIVFVVSFV GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY
     SILLFDLIYR EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR
     LPGNHSRAST LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEELDST ERACDTLLMC
     IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF FIVIIIVLNL IFGVIIDTFA
     DLRSEKQKKE EILKTTCFIC GLERDKFDNK TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT
     DYTGPESYVA QMIKNKNLDW FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTA
     QLNELKEQMT EQRKRRQRLG FVDVQNCMSR
//
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