GenomeNet

Database: UniProt
Entry: ITPR2_RAT
LinkDB: ITPR2_RAT
Original site: ITPR2_RAT 
ID   ITPR2_RAT               Reviewed;        2701 AA.
AC   P29995; Q99P56;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   30-AUG-2017, entry version 144.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 2;
DE   AltName: Full=IP3 receptor isoform 2;
DE            Short=IP3R 2;
DE            Short=InsP3R2;
DE   AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 2 InsP3 receptor;
GN   Name=Itpr2;
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], AND VARIANTS.
RC   TISSUE=Brain;
RX   PubMed=1655411;
RA   Suedhof T.C., Newton C.A., Archer B.T. III, Ushkaryov Y.A.,
RA   Mignery G.A.;
RT   "Structure of a novel InsP3 receptor.";
RL   EMBO J. 10:3199-3206(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Magnino F., Dufour J.-F.;
RT   "New rat IP3R isoform 2 sequence.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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   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. This
CC       release is regulated by cAMP both dependently and independently of
CC       PKA (By similarity). {ECO:0000250|UniProtKB:P29995}.
CC   -!- SUBUNIT: Homotetramer. Interacts with CABP1. Interacts with BOK;
CC       regulates ITPR2 expression (PubMed:23884412).
CC       {ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:23884412}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
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: Phosphorylation by cAMP-dependent PKA on Ser-937 increases
CC       calcium release. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
DR   EMBL; X61677; CAA43852.1; -; mRNA.
DR   EMBL; AF329470; AAK11622.1; -; mRNA.
DR   PIR; S17796; S17796.
DR   RefSeq; NP_112308.1; NM_031046.3.
DR   UniGene; Rn.89152; -.
DR   ProteinModelPortal; P29995; -.
DR   BioGrid; 249575; 2.
DR   STRING; 10116.ENSRNOP00000047905; -.
DR   TCDB; 1.A.3.2.1; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
DR   iPTMnet; P29995; -.
DR   PhosphoSitePlus; P29995; -.
DR   PaxDb; P29995; -.
DR   PRIDE; P29995; -.
DR   GeneID; 81678; -.
DR   KEGG; rno:81678; -.
DR   UCSC; RGD:69649; rat.
DR   CTD; 3709; -.
DR   RGD; 69649; Itpr2.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; P29995; -.
DR   KO; K04959; -.
DR   PhylomeDB; P29995; -.
DR   Reactome; R-RNO-112043; PLC beta mediated events.
DR   Reactome; R-RNO-1489509; DAG and IP3 signaling.
DR   Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-RNO-4086398; Ca2+ pathway.
DR   Reactome; R-RNO-422356; Regulation of insulin secretion.
DR   Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-RNO-5578775; Ion homeostasis.
DR   Reactome; R-RNO-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   PRO; PR:P29995; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion 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:0007202; P:activation of phospholipase C activity; TAS:Reactome.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:Reactome.
DR   GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt-bd.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR000699; RIH_dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
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; SSF48371; SSF48371; 3.
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; Polymorphism;
KW   Receptor; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   2701       Inositol 1,4,5-trisphosphate receptor
FT                                type 2.
FT                                /FTId=PRO_0000153926.
FT   TOPO_DOM      1   2227       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2228   2248       Helical. {ECO:0000255}.
FT   TOPO_DOM   2249   2260       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2261   2281       Helical. {ECO:0000255}.
FT   TOPO_DOM   2282   2284       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2285   2305       Helical. {ECO:0000255}.
FT   TOPO_DOM   2306   2307       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2308   2328       Helical. {ECO:0000255}.
FT   TOPO_DOM   2329   2351       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2352   2372       Helical. {ECO:0000255}.
FT   TOPO_DOM   2373   2394       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2395   2415       Helical. {ECO:0000255}.
FT   TOPO_DOM   2416   2521       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2522   2542       Helical. {ECO:0000255}.
FT   TOPO_DOM   2543   2701       Extracellular. {ECO:0000255}.
FT   DOMAIN      112    166       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      173    223       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      231    287       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      294    357       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      265    269       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     937    937       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    1160   1160       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14571}.
FT   MOD_RES    1709   1709       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2607   2607       Phosphotyrosine. {ECO:0000255}.
FT   MOD_RES    2633   2633       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2636   2636       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   VARIANT     689    689       D -> H.
FT   VARIANT    1013   1013       G -> C.
FT   VARIANT    1256   1256       L -> P.
FT   VARIANT    2384   2384       V -> I.
FT   VARIANT    2694   2694       E -> V.
FT   CONFLICT    119    119       K -> N (in Ref. 2; AAK11622).
FT                                {ECO:0000305}.
FT   CONFLICT    344    344       H -> R (in Ref. 2; AAK11622).
FT                                {ECO:0000305}.
FT   CONFLICT    943    943       W -> V (in Ref. 2; AAK11622).
FT                                {ECO:0000305}.
FT   CONFLICT   1692   1692       S -> G (in Ref. 2; AAK11622).
FT                                {ECO:0000305}.
FT   CONFLICT   2556   2556       K -> E (in Ref. 2; AAK11622).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2701 AA;  307058 MW;  42BF7F1024335984 CRC64;
     MSDKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLTNPP KKFRDCLFKV
     CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENRKL LGEIVKYSKV
     IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
     KVVLMPVNAG QPLHASNVEL LDNPGCKEVN AVNCNTSWKI TLFMKFSSYR EDVLKGGDVV
     RLFHAEQEKF LTCDDYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
     SLFRFKHLAT GNYLAAELNP DYRDAQNEGK TVRDGELPTS KKKHQAGEKI MYTLVSVPHG
     NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTEEE RPVMLKIGTC
     QTKEDKEAFA IVCVPLSEVR DLDFANDANK VLATTVKKLE NGSITQNERR FVTKLLEDLI
     FFVADVTNNG QDVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
     LGDQRYAPYK YVLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NSTAIPVTQE LICKFMLSPG
     NADILIQTKL VSMQVENPME SSILPDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAREGT
     KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR
     LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
     YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
     SSYFERLSKF QDGSNNVMRT IHGVGEMMTQ MVLSRGSIFP VSWPDAQPSV HPSKQASPGE
     QEDVTVMDTK LKVIEILQFI LSVRLDYRIS YMLSIYKKEF GENDGNGDPS ASGTPETLLP
     SALVPDIDEI AAQAETMFAG RKEKTPVQLD DEGGRTFLRV LIHLIMHDYA PLLSGALQLL
     FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSGSYENGD
     MGEGQAKGGE EANEESNLLS PVQDGAKTPQ IDSNKGNNYR IVKEILIRLS KLCVQNKKCR
     NQHQRLLKNM GAHSVVLDLL QIPYEKTDEK MNEVMDLAHT FLQNFCRGNP QNQVLLHKHL
     NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
     GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLNMMC SERARGDESG PLAYHITLVE
     LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
     IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLERCVT ESVMNIVSGF FNSPFSDNST
     SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRAL AEVAKNRGIA IPVDLDSQVN
     TLFMKNHSST VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEQQFSPM
     MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
     MLEKKDSFME ESSTLRKILL NRYFKGDHSV GVNGPLSGAY AKTAQVGGGF TGQDADKTGI
     SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ NSFYQQLHEQ
     KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGSKKREED SDLMALGPRM RVRDSSLHLK
     EGMKGQLTEA SSATSKAYCV YRREMDPDID TMCPGQEAGS AEEKSAEEVT MSPAITIMRP
     ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK
     NVALVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILSDINPLG KYRMDLVLQL
     KNNASKLLLA IMESRHDSEN AERILFNMRP KELVDVMKNA YNQGLECNHG DEEGGDDGVS
     PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPEEGDEALK YYANHTAQIE IVRHDRTMEQ
     IVFPVPNICE FLTRESKYRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF
     WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PLFSALLWVA VAICTSMLFF
     FSKPVGIRPF LVSIMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
     ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
     LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGNDGV PTMTLTSMLG TCPKENCSPT
     IPSSNAAGEG GEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
     DLLFFFIVII IVLNLIFGVI IDTFADLRSE KQKKEKILKT TCFICGLERD KFDNKTVSFE
     EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMITE KNLDWFPRMR AMSLVSNEGD
     SEQNEIRNLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHENHHMPP
     H
//
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