ID ITPR1_MOUSE STANDARD; PRT; 2749 AA. AC P11881; P20943; Q99LG5; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-MAY-2005 (Rel. 47, 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) (Protein PCD-6). GN Name=Itpr1; Synonyms=Insp3r, Pcd6, Pcp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Purkinje cells; RX MEDLINE=90044039; PubMed=2554142; DOI=10.1038/342032a0; 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 NUCLEOTIDE SEQUENCE (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 NUCLEOTIDE SEQUENCE OF 318-332 AND 1692-1731, AND ALTERNATIVE RP 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749. RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; 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 human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE OF 2250-2749. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX MEDLINE=89068131; PubMed=3199205; RA Nordquist D.T., Kozak C.A., Orr H.T.; RT "cDNA cloning and characterization of three genes uniquely expressed RT in cerebellum by Purkinje neurons."; RL J. Neurosci. 8:4780-4789(1988). 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 TRPC4. The PPXXF motif binds CC HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and CC SHANK3 (By similarity). 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 cAMP kinase. Phosphorylation prevents the CC 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 -!- SIMILARITY: Contains 5 MIR domains. 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 EMBL; M21530; AAA88319.1; ALT_INIT. DR PIR; S04844; ACMSIT. DR PDB; 1XZZ; X-ray; A=2-223. DR SMR; P11881; 7-225. DR MGI; MGI:96623; Itpr1. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS. DR GO; GO:0008095; F:inositol-1,4,5-triphosphate receptor activity; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0006816; P:calcium ion transport; ISS. DR InterPro; IPR008938; ARM. DR InterPro; IPR000699; Ca-rel_channel. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR000493; InsP3_receptor. 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 PRINTS; PR00779; INSP3RECEPTR. DR SMART; SM00472; MIR; 4. DR PROSITE; PS50919; MIR; 5. KW 3D-structure; Alternative splicing; Calcium; Calcium channel; KW Calcium transport; Endoplasmic reticulum; Ion transport; KW Ionic channel; Phosphorylation; Receptor; Repeat; Transmembrane; KW Transport. 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 DOMAIN 112 166 MIR 1. FT DOMAIN 173 223 MIR 2. FT DOMAIN 231 287 MIR 3. FT DOMAIN 294 373 MIR 4. FT DOMAIN 379 435 MIR 5. FT MOD_RES 482 482 Phosphotyrosine (Potential). FT MOD_RES 1588 1588 Phosphoserine (by PKA) (Potential). FT MOD_RES 1755 1755 Phosphoserine (by PKA) (Potential). FT MOD_RES 2655 2655 Phosphotyrosine (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 and 5). FT STRAND 239 244 FT TURN 245 248 FT STRAND 249 255 FT STRAND 260 265 FT HELIX 272 274 FT HELIX 278 280 FT STRAND 282 286 FT STRAND 303 307 FT TURN 308 310 FT STRAND 313 318 FT STRAND 353 358 FT HELIX 364 366 FT STRAND 368 371 FT STRAND 388 392 FT HELIX 393 395 FT TURN 396 396 FT STRAND 397 405 FT STRAND 415 421 FT STRAND 430 434 FT HELIX 437 461 FT TURN 462 462 FT HELIX 467 484 FT TURN 485 487 FT HELIX 495 499 FT HELIX 504 512 FT TURN 513 514 FT HELIX 515 524 FT HELIX 525 527 FT HELIX 547 564 FT TURN 565 566 FT HELIX 568 585 FT TURN 587 588 FT HELIX 589 599 FT TURN 600 601 SQ SEQUENCE 2749 AA; 313197 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 //