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 03-AUG-2022, entry version 169.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS.
RC TISSUE=Brain;
RX PubMed=1655411; DOI=10.1002/j.1460-2075.1991.tb04882.x;
RA Suedhof T.C., Newton C.A., Archer B.T. III, Ushkaryov Y.A., 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 TRPC4.
RX PubMed=11163362; DOI=10.1016/s0014-5793(00)02362-0;
RA Mery L., Magnino F., Schmidt K., Krause K.-H., Dufour J.-F.;
RT "Alternative splice variants of hTrp4 differentially interact with the C-
RT terminal portion of the inositol 1,4,5-trisphosphate receptors.";
RL FEBS Lett. 487:377-383(2001).
RN [4]
RP SUBUNIT, AND INTERACTION WITH CABP1.
RX PubMed=12032348; DOI=10.1073/pnas.102006299;
RA Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F.,
RA 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 [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 proteolytic
RT cleavage.";
RL J. Biol. Chem. 288:25340-25349(2013).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium. This release is
CC regulated by cAMP both dependently and independently of PKA (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z329}.
CC -!- SUBUNIT: Homotetramer (PubMed:12032348). Interacts with CABP1
CC (PubMed:12032348). Interacts with BOK; regulates ITPR2 expression
CC (PubMed:23884412). Interacts with BCL2L10 (By similarity). Interacts
CC with TRPC4 (PubMed:11163362). {ECO:0000250|UniProtKB:Q14571,
CC ECO:0000269|PubMed:11163362, ECO:0000269|PubMed:12032348,
CC 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 calcium
CC release. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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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 SMR; P29995; -.
DR BioGRID; 249575; 2.
DR IntAct; P29995; 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 jPOST; 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 InParanoid; P29995; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; P29995; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-5578775; Ion homeostasis.
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:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
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; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0015278; F:calcium-release channel activity; ISO: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:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR035910; RyR/IP3R_RIH_dom_sf.
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; 1.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Endoplasmic reticulum;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..2701
FT /note="Inositol 1,4,5-trisphosphate receptor type 2"
FT /id="PRO_0000153926"
FT TOPO_DOM 1..2227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2228..2248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2249..2260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2261..2281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2282..2284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2285..2305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2306..2307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2308..2328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2329..2351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2352..2372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2373..2394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2395..2415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2416..2521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2522..2542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2543..2701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 112..166
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 173..223
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 231..287
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 294..357
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 378..434
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1134..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2676..2701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..269
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 507..510
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 567..569
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT MOD_RES 937
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14571"
FT MOD_RES 1709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT VARIANT 689
FT /note="D -> H"
FT VARIANT 1013
FT /note="G -> C"
FT VARIANT 1256
FT /note="L -> P"
FT VARIANT 2384
FT /note="V -> I"
FT VARIANT 2694
FT /note="E -> V"
FT CONFLICT 119
FT /note="K -> N (in Ref. 2; AAK11622)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="H -> R (in Ref. 2; AAK11622)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="W -> V (in Ref. 2; AAK11622)"
FT /evidence="ECO:0000305"
FT CONFLICT 1692
FT /note="S -> G (in Ref. 2; AAK11622)"
FT /evidence="ECO:0000305"
FT CONFLICT 2556
FT /note="K -> E (in Ref. 2; AAK11622)"
FT /evidence="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
