ID IP3R_MOUSE STANDARD; PRT; 2749 AA. AC P11881; Q99LG5; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Inositol 1,4,5-trisphosphate receptor type 1 (Type 1 inositol 1,4,5- DE trisphosphate receptor) (Type 1 InsP3 receptor) (IP3 receptor isoform DE 1) (InsP3R1) (Inositol 1,4,5-trisphosphate-binding protein P400) DE (Purkinje cell protein 1). GN ITPR1 OR INSP3R. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC TISSUE=Purkinje cells; RX MEDLINE=90044039; PubMed=2554142; RA Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N., RA Mikoshiba K.; RT "Primary structure and functional expression of the inositol 1,4,5- RT trisphosphate-binding protein P400."; RL Nature 342:32-38(1989). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1). RC STRAIN=ICR; TISSUE=Cerebellum; RX MEDLINE=89345101; PubMed=2762133; RA Furuichi T., Yoshikawa S., Mikoshiba K.; RT "Nucleotide sequence of cDNA encoding P400 protein in the mouse RT cerebellum."; RL Nucleic Acids Res. 17:5385-5386(1989). RN [3] RP SEQUENCE OF 318-332 AND 1692-1731 FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=ICR; RX MEDLINE=91296797; PubMed=1648733; RA Nakagawa T., Okano H., Furuichi T., Aruga J., Mikoshiba K.; RT "The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are RT expressed in a tissue-specific and developmentally specific manner."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6244-6248(1991). RN [4] RP SEQUENCE OF 2098-2749 FROM N.A. RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: RECEPTOR FOR INOSITOL 1,4,5-TRISPHOSPHATE, A SECOND CC MESSENGER THAT MEDIATES THE RELEASE OF INTRACELLULAR CALCIUM. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Endoplasmic CC reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=There is a combination of two alternatively spliced CC domains at site SI and site SII (A, B and C). Experimental CC confirmation may be lacking for some isoforms; CC Name=1; Synonyms=SISIIABC; CC IsoId=P11881-1; Sequence=Displayed; CC Name=2; Synonyms=SI-SIIABC; CC IsoId=P11881-2; Sequence=VSP_002691; CC Name=3; Synonyms=SISIIAC; CC IsoId=P11881-3; Sequence=VSP_002693; CC Name=4; Synonyms=SI-SIIAC; CC IsoId=P11881-4; Sequence=VSP_002691, VSP_002693; CC Name=5; Synonyms=SISIIA; CC IsoId=P11881-5; Sequence=VSP_002693, VSP_002694; CC Name=6; Synonyms=SI-SIIA; CC IsoId=P11881-6; Sequence=VSP_002691, VSP_002693, VSP_002694; CC Name=7; Synonyms=SISII; CC IsoId=P11881-7; Sequence=VSP_002692, VSP_002693, VSP_002694; CC Name=8; Synonyms=SI-SII; CC IsoId=P11881-8; Sequence=VSP_002691, VSP_002692, VSP_002693, CC VSP_002694; 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 BY CYCLIC-AMP KINASE. PHOSPHORYLATION PREVENTS CC THE LIGAND-INDUCED OPENING OF THE CALCIUM CHANNELS. CC -!- PTM: Phosphorylated on tyrosine residues (By similarity). CC -!- MISCELLANEOUS: CALCIUM APPEARS TO INHIBIT LIGAND BINDING TO THE CC RECEPTOR, MOST PROBABLY BY INTERACTING WITH A DISTINCT CALCIUM- CC BINDING PROTEIN WHICH THEN INHIBITS THE RECEPTOR. CC -!- SIMILARITY: BELONGS TO THE INSP3 RECEPTOR FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X15373; CAA33433.1; -. DR EMBL; M75986; AAA39316.1; -. DR EMBL; M75987; AAA39317.1; -. DR EMBL; BC003271; AAH03271.1; ALT_INIT. DR PIR; S04844; ACMSIT. DR PDB; 1N4K; 25-DEC-02. DR MGD; MGI:96623; Itpr1. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS. DR GO; GO:0004872; F:receptor activity; ISS. DR GO; GO:0006816; P:calcium ion transport; ISS. DR InterPro; IPR000699; Ca-rel_channel. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR003608; MIR. DR Pfam; PF00520; ion_trans; 1. DR Pfam; PF02815; MIR; 4. DR Pfam; PF01365; RYDR_ITPR; 2. DR SMART; SM00472; MIR; 4. KW Receptor; Transmembrane; Phosphorylation; Endoplasmic reticulum; KW Ionic channel; Ion transport; Calcium channel; Alternative splicing; KW 3D-structure. FT DOMAIN 1 2273 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2274 2294 POTENTIAL. FT DOMAIN 2295 2305 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2306 2326 POTENTIAL. FT DOMAIN 2327 2352 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2353 2373 POTENTIAL. FT DOMAIN 2374 2396 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2397 2417 POTENTIAL. FT DOMAIN 2418 2439 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 2440 2460 POTENTIAL. FT DOMAIN 2461 2569 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 2570 2590 POTENTIAL. FT DOMAIN 2591 2749 CYTOPLASMIC (POTENTIAL). FT MOD_RES 482 482 PHOSPHORYLATION (POTENTIAL). FT MOD_RES 1588 1588 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT MOD_RES 1755 1755 PHOSPHORYLATION (BY PKA) (POTENTIAL). FT MOD_RES 2655 2655 PHOSPHORYLATION (POTENTIAL). FT VARSPLIC 318 332 Missing (in isoform 2, isoform 4, isoform FT 6 and isoform 8). FT /FTId=VSP_002691. FT VARSPLIC 1692 1714 Missing (in isoform 7 and isoform 8). FT /FTId=VSP_002692. FT VARSPLIC 1715 1715 Missing (in isoform 3, isoform 4, isoform FT 5, isoform 6, isoform 7 and isoform 8). FT /FTId=VSP_002693. FT VARSPLIC 1716 1731 Missing (in isoform 5, isoform 6, isoform FT 7 and isoform 8). FT /FTId=VSP_002694. FT CONFLICT 2675 2675 L -> P (IN REF. 4). SQ SEQUENCE 2749 AA; 313193 MW; 47E5F24BCD5F4153 CRC64; MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN LFLKPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LMYHIHLVEL LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE MMTKDRGYGE KQISIDESEN AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK KSEKFFKVFY DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA KEPTTQITEE VRDQLLEASA ATRKAFTTFR READPDDHYQ SGEGTQATTD KAKDDLEMSA VITIMQPILR FLQLLCENHN RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN VGHNIYILAH QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL DRTMEQIVFP VPSICEFLTK ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR AQPVLYWCAR NMSFWSSISF NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL VYLFSIVGYL FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET GENCTSPAPK EELLPAEETE QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP LFAARVIYDL LFFFMVIIIV LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY LCFIVLVKVK DSTEYTGPES YVAEMIRERN LDWFLRMRAM SLVSSDSEGE QNELRNLQEK LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA //