ID   ITPR1_MOUSE             Reviewed;        2749 AA.
AC   P11881; P20943; Q99LG5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   18-MAR-2008, entry version 105.
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   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Purkinje cell;
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 [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=89345101; PubMed=2762133; DOI=10.1093/nar/17.13.5385;
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 [GENOMIC DNA] OF 318-332 AND 1692-1731, AND
RP   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   PROTEIN SEQUENCE OF 862-871, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] 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).
RN   [7]
RP   INTERACTION WITH AHCYL1.
RX   MEDLINE=22526701; PubMed=12525476; DOI=10.1074/jbc.M210119200;
RA   Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
RT   "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
RT   protein, is released from the IP3 receptor upon IP3 binding to the
RT   receptor.";
RL   J. Biol. Chem. 278:10602-10612(2003).
RN   [8]
RP   INTERACTION WITH TXNDC4, AND MUTAGENESIS OF CYS-2496; CYS-2504 AND
RP   CYS-2527.
RX   PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA   Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T.,
RA   Mikoshiba K.;
RT   "Subtype-specific and ER lumenal environment-dependent regulation of
RT   inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL   Cell 120:85-98(2005).
RN   [9]
RP   INTERACTION WITH AHCYL1.
RX   PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
RA   Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
RA   Missiaen L., Parys J.B., De Smedt H.;
RT   "Binding of IRBIT to the IP3 receptor: determinants and functional
RT   effects.";
RL   Biochem. Biophys. Res. Commun. 343:49-56(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-223.
RX   PubMed=15664189; DOI=10.1016/j.molcel.2004.11.047;
RA   Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K.,
RA   Ikura M.;
RT   "Crystal structure of the ligand binding suppressor domain of type 1
RT   inositol 1,4,5-trisphosphate receptor.";
RL   Mol. Cell 17:193-203(2005).
RN   [12]
RP   INTERACTION WITH MRVI1.
RX   PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
RA   Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I.,
RA   Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.;
RT   "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation
RT   and thrombus formation.";
RL   Blood 109:552-559(2007).
CC   -!- FUNCTION: Intracellular channel that mediates calcium release from
CC       the endoplasmic reticulum following stimulation by inositol 1,4,5-
CC       trisphosphate.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC4. The PPXXF motif binds
CC       HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and
CC       SHANK3. Part of cGMP kinase signaling complex at least composed of
CC       ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and
CC       ITPR1 (By similarity). Interacts with TXNDC4 in a pH-, redox
CC       state- and calcium-dependent manner which results in the
CC       inhibition the calcium channel activity. The strength of this
CC       interaction inversely correlates with calcium concentration.
CC       Interacts with AHCYL1 and MRVI1.
CC   -!- INTERACTION:
CC       Q9D1Q6:Txndc4; NbExp=2; IntAct=EBI-541478, EBI-541567;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
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.
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DR   EMBL; X15373; CAA33433.1; -; mRNA.
DR   EMBL; M75986; AAA39316.1; -; Genomic_DNA.
DR   EMBL; M75987; AAA39317.1; -; Genomic_DNA.
DR   EMBL; BC003271; AAH03271.1; ALT_INIT; mRNA.
DR   EMBL; M21530; AAA88319.1; ALT_INIT; mRNA.
DR   PIR; S04844; ACMSIT.
DR   UniGene; Mm.227912; -.
DR   PDB; 1N4K; X-ray; 2.20 A; A=224-604.
DR   PDB; 1XZZ; X-ray; 1.80 A; A=2-223.
DR   PDBsum; 1N4K; -.
DR   PDBsum; 1XZZ; -.
DR   IntAct; P11881; -.
DR   PhosphoSite; P11881; -.
DR   Ensembl; ENSMUSG00000030102; Mus musculus.
DR   KEGG; mmu:16438; -.
DR   MGI; MGI:96623; Itpr1.
DR   LinkHub; P11881; -.
DR   ArrayExpress; P11881; -.
DR   CleanEx; MM_ITPR1; -.
DR   GermOnline; ENSMUSG00000030102; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0043234; C:protein complex; IPI:MGI.
DR   GO; GO:0008095; F:inositol-1,4,5-triphosphate receptor activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
DR   InterPro; IPR000699; Ca-rel_channel.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt_bd.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003608; MIR.
DR   InterPro; IPR013662; RIH_assoc.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   PANTHER; PTHR13715; Ryanodine_recept-rel; 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   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Direct protein sequencing; Endoplasmic reticulum;
KW   Ion transport; Ionic channel; Membrane; Phosphoprotein; Receptor;
KW   Repeat; Transmembrane; Transport.
FT   CHAIN         1   2749       Inositol 1,4,5-trisphosphate receptor
FT                                type 1.
FT                                /FTId=PRO_0000153921.
FT   TOPO_DOM      1   2273       Cytoplasmic (Potential).
FT   TRANSMEM   2274   2294       Potential.
FT   TOPO_DOM   2295   2305       Lumenal (Potential).
FT   TRANSMEM   2306   2326       Potential.
FT   TOPO_DOM   2327   2352       Cytoplasmic (Potential).
FT   TRANSMEM   2353   2373       Potential.
FT   TOPO_DOM   2374   2396       Lumenal (Potential).
FT   TRANSMEM   2397   2417       Potential.
FT   TOPO_DOM   2418   2439       Cytoplasmic (Potential).
FT   TRANSMEM   2440   2460       Potential.
FT   TOPO_DOM   2461   2569       Lumenal (Potential).
FT   TRANSMEM   2570   2590       Potential.
FT   TOPO_DOM   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   REGION     2463   2528       Interaction with TXNDC4.
FT   MOD_RES     482    482       Phosphotyrosine (Potential).
FT   MOD_RES    1588   1588       Phosphoserine.
FT   MOD_RES    1755   1755       Phosphoserine; by PKA (Potential).
FT   MOD_RES    2655   2655       Phosphotyrosine (Potential).
FT   VAR_SEQ     318    332       Missing (in isoform 2, isoform 4, isoform
FT                                6 and isoform 8).
FT                                /FTId=VSP_002691.
FT   VAR_SEQ    1692   1714       Missing (in isoform 7 and isoform 8).
FT                                /FTId=VSP_002692.
FT   VAR_SEQ    1715   1715       Missing (in isoform 3, isoform 4, isoform
FT                                5, isoform 6, isoform 7 and isoform 8).
FT                                /FTId=VSP_002693.
FT   VAR_SEQ    1716   1731       Missing (in isoform 5, isoform 6, isoform
FT                                7 and isoform 8).
FT                                /FTId=VSP_002694.
FT   MUTAGEN    2496   2496       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                TXNDC4. Complete loss of channel
FT                                inhibition by TXNDC4.
FT   MUTAGEN    2504   2504       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                TXNDC4. Complete loss of channel
FT                                inhibition by TXNDC4.
FT   MUTAGEN    2527   2527       C->S: Complete loss of channel activity.
FT                                Significant decrease of interaction with
FT                                TXNDC4.
FT   CONFLICT   2675   2675       L -> P (in Ref. 5 and 6).
FT   STRAND       14     23
FT   STRAND       25     30
FT   STRAND       36     39
FT   HELIX        41     43
FT   STRAND       46     48
FT   HELIX        53     56
FT   STRAND       58     61
FT   HELIX        67     74
FT   HELIX        86    109
FT   TURN        110    112
FT   STRAND      120    125
FT   TURN        126    129
FT   STRAND      130    139
FT   STRAND      141    143
FT   STRAND      146    154
FT   HELIX       157    159
FT   STRAND      161    167
FT   STRAND      181    189
FT   STRAND      193    199
FT   STRAND      201    205
FT   STRAND      207    213
FT   STRAND      239    244
FT   TURN        245    248
FT   STRAND      249    255
FT   STRAND      257    265
FT   STRAND      269    271
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    359
FT   HELIX       364    366
FT   STRAND      368    371
FT   STRAND      388    392
FT   TURN        393    396
FT   STRAND      397    406
FT   STRAND      409    412
FT   STRAND      415    423
FT   STRAND      430    434
FT   HELIX       437    461
FT   HELIX       467    484
FT   TURN        485    487
FT   HELIX       495    499
FT   HELIX       504    512
FT   HELIX       515    524
FT   HELIX       525    527
FT   HELIX       547    564
FT   HELIX       568    585
FT   HELIX       589    599
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
//