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Database: UniProt
Entry: P11881
LinkDB: P11881
Original site: P11881 
ID   ITPR1_MOUSE             Reviewed;        2749 AA.
AC   P11881; P20943; Q99LG5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   13-FEB-2019, entry version 213.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1;
DE   AltName: Full=IP3 receptor isoform 1;
DE            Short=IP3R 1;
DE            Short=InsP3R1;
DE   AltName: Full=Inositol 1,4,5-trisphosphate-binding protein P400;
DE   AltName: Full=Protein PCD-6;
DE   AltName: Full=Purkinje cell protein 1;
DE   AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 1 InsP3 receptor;
GN   Name=Itpr1; Synonyms=Insp3r, Pcd6, Pcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Purkinje cell;
RX   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   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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, AND
RP   ALTERNATIVE SPLICING.
RC   STRAIN=ICR;
RX   PubMed=1648733; DOI=10.1073/pnas.88.14.6244;
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   [5]
RP   PROTEIN SEQUENCE OF 862-871, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2250-2749.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   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   [8]
RP   INTERACTION WITH AHCYL1.
RX   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   [9]
RP   INTERACTION WITH ERP44, 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [13]
RP   FUNCTION.
RX   PubMed=19752026; DOI=10.1083/jcb.200904060;
RA   Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R.,
RA   Tabas I.;
RT   "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-
RT   triphosphate receptor activity in endoplasmic reticulum stress-induced
RT   apoptosis.";
RL   J. Cell Biol. 186:783-792(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [15]
RP   FUNCTION, AND MUTAGENESIS OF TYR-167 AND LYS-168.
RX   PubMed=20813840; DOI=10.1074/jbc.M110.140129;
RA   Yamazaki H., Chan J., Ikura M., Michikawa T., Mikoshiba K.;
RT   "Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor
RT   mediates functional coupling between ligand binding and channel
RT   opening.";
RL   J. Biol. Chem. 285:36081-36091(2010).
RN   [16]
RP   INTERACTION WITH TESPA1.
RX   PubMed=23650607; DOI=10.1016/j.fob.2012.08.005;
RA   Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K.,
RA   Hamabashiri M., Tanaka M., Shirasawa S.;
RT   "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding
RT   protein in T and B lymphocytes.";
RL   FEBS Open Bio 2:255-259(2012).
RN   [17]
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).
RN   [18]
RP   INTERACTION WITH AHCYL1, MUTAGENESIS OF SER-1588 AND SER-1755,
RP   PHOSPHORYLATION, AND FUNCTION.
RX   PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
RA   Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K.,
RA   Ando H., Mizutani A., Abe T., Kiyonari H., Seki G., Yule D.,
RA   Mikoshiba K., Muallem S.;
RT   "Irbit mediates synergy between ca(2+) and cAMP signaling pathways
RT   during epithelial transport in mice.";
RL   Gastroenterology 145:232-241(2013).
RN   [19]
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).
RN   [20]
RP   PALMITOYLATION AT CYS-56 AND CYS-849, AND MUTAGENESIS OF CYS-56;
RP   CYS-849 AND CYS-2215.
RX   PubMed=25368151; DOI=10.1073/pnas.1417176111;
RA   Fredericks G.J., Hoffmann F.W., Rose A.H., Osterheld H.J., Hess F.M.,
RA   Mercier F., Hoffmann P.R.;
RT   "Stable expression and function of the inositol 1,4,5-triphosphate
RT   receptor requires palmitoylation by a DHHC6/selenoprotein K complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16478-16483(2014).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 224-604 IN COMPLEX WITH
RP   INOSITOL 1,4,5-TRISPHOSPHATE, AND MUTAGENESIS OF THR-267 AND TYR-567.
RX   PubMed=12442173; DOI=10.1038/nature01268;
RA   Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K.,
RA   Tong K.I., Yoshikawa F., Furuichi T., Iwai M., Michikawa T.,
RA   Mikoshiba K., Ikura M.;
RT   "Structure of the inositol 1,4,5-trisphosphate receptor binding core
RT   in complex with its ligand.";
RL   Nature 420:696-700(2002).
RN   [22]
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).
CC   -!- FUNCTION: Intracellular channel that mediates calcium release from
CC       the endoplasmic reticulum following stimulation by inositol 1,4,5-
CC       trisphosphate. Involved in the regulation of epithelial secretion
CC       of electrolytes and fluid through the interaction with AHCYL1
CC       (PubMed:23542070). Plays a role in ER stress-induced apoptosis.
CC       Cytoplasmic calcium released from the ER triggers apoptosis by the
CC       activation of CaM kinase II, eventually leading to the activation
CC       of downstream apoptosis pathways. {ECO:0000269|PubMed:19752026,
CC       ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:23542070,
CC       ECO:0000269|PubMed:2554142}.
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 ERP44 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 MRVI1. Interacts with CABP1 (By similarity).
CC       Interacts with TESPA1. Interacts (when not phosphorylated) with
CC       AHCYL1 (when phosphorylated); the interaction suppresses inositol
CC       1,4,5-trisphosphate binding to ITPR1 (PubMed:23542070). Interacts
CC       with AHCYL2 (with lower affinity than with AHCYL1) (By
CC       similarity). Interacts with BOK (via BH4 domain); protects ITPR1
CC       from proteolysis by CASP3 during apoptosis (PubMed:23884412).
CC       {ECO:0000250|UniProtKB:Q14643, ECO:0000269|PubMed:12442173,
CC       ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:15652484,
CC       ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16990611,
CC       ECO:0000269|PubMed:23542070, ECO:0000269|PubMed:23650607,
CC       ECO:0000269|PubMed:23884412}.
CC   -!- INTERACTION:
CC       Q8VDN2:Atp1a1; NbExp=3; IntAct=EBI-541478, EBI-444536;
CC       Q6PIE5:Atp1a2; NbExp=3; IntAct=EBI-541478, EBI-6665421;
CC       P10415:BCL2 (xeno); NbExp=3; IntAct=EBI-541478, EBI-77694;
CC       Q9D1Q6:Erp44; NbExp=5; IntAct=EBI-541478, EBI-541567;
CC       O35157:Slc8a1; NbExp=4; IntAct=EBI-541478, EBI-8351080;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:25368151}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and
CC       secretory granules (By similarity).
CC       {ECO:0000250|UniProtKB:Q9TU34}.
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 (PKA). Phosphorylation prevents
CC       the ligand-induced opening of the calcium channels.
CC       Phosphorylation by PKA increases the interaction with inositol
CC       1,4,5-trisphosphate and decreases the interaction with AHCYL1.
CC       {ECO:0000305|PubMed:23542070}.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC       {ECO:0000250|UniProtKB:Q14643}.
CC   -!- PTM: Ubiquitination at multiple lysines targets ITPR1 for
CC       proteasomal degradation. Approximately 40% of the ITPR1-associated
CC       ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-
CC       48'- and 'Lys-63'-linked (By similarity).
CC       {ECO:0000250|UniProtKB:P29994}.
CC   -!- PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulate
CC       ITPR1 stability and function (PubMed:25368151).
CC       {ECO:0000269|PubMed:25368151}.
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. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA88319.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAH03271.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; X15373; CAA33433.1; -; mRNA.
DR   EMBL; AC120411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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   CCDS; CCDS51869.1; -. [P11881-1]
DR   PIR; S04844; ACMSIT.
DR   RefSeq; NP_034715.3; NM_010585.5. [P11881-1]
DR   RefSeq; XP_006505693.1; XM_006505630.1. [P11881-2]
DR   RefSeq; XP_006505699.1; XM_006505636.1. [P11881-7]
DR   RefSeq; XP_006505700.1; XM_006505637.1. [P11881-8]
DR   RefSeq; XP_017176897.1; XM_017321408.1. [P11881-3]
DR   RefSeq; XP_017176899.1; XM_017321410.1. [P11881-4]
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   PDB; 5GUG; X-ray; 7.40 A; A/B=1-2217.
DR   PDB; 5X9Z; X-ray; 7.31 A; A/B=1-2217.
DR   PDB; 5XA0; X-ray; 5.81 A; A/B=1-1581.
DR   PDB; 5XA1; X-ray; 6.20 A; A/B=1-1581.
DR   PDBsum; 1N4K; -.
DR   PDBsum; 1XZZ; -.
DR   PDBsum; 5GUG; -.
DR   PDBsum; 5X9Z; -.
DR   PDBsum; 5XA0; -.
DR   PDBsum; 5XA1; -.
DR   ProteinModelPortal; P11881; -.
DR   SMR; P11881; -.
DR   BioGrid; 200847; 16.
DR   CORUM; P11881; -.
DR   DIP; DIP-32243N; -.
DR   IntAct; P11881; 20.
DR   MINT; P11881; -.
DR   STRING; 10090.ENSMUSP00000032192; -.
DR   iPTMnet; P11881; -.
DR   PhosphoSitePlus; P11881; -.
DR   SwissPalm; P11881; -.
DR   jPOST; P11881; -.
DR   MaxQB; P11881; -.
DR   PaxDb; P11881; -.
DR   PeptideAtlas; P11881; -.
DR   PRIDE; P11881; -.
DR   Ensembl; ENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
DR   Ensembl; ENSMUST00000203615; ENSMUSP00000144880; ENSMUSG00000030102. [P11881-3]
DR   GeneID; 16438; -.
DR   KEGG; mmu:16438; -.
DR   UCSC; uc033itt.1; mouse. [P11881-1]
DR   CTD; 3708; -.
DR   MGI; MGI:96623; Itpr1.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   GeneTree; ENSGT00940000155071; -.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; P11881; -.
DR   KO; K04958; -.
DR   OMA; PRHAPYK; -.
DR   OrthoDB; 94996at2759; -.
DR   PhylomeDB; P11881; -.
DR   TreeFam; TF312815; -.
DR   Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-MMU-418457; cGMP effects.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   ChiTaRS; Itpr1; mouse.
DR   EvolutionaryTrace; P11881; -.
DR   PRO; PR:P11881; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000030102; Expressed in 300 organ(s), highest expression level in cerebellar vermis.
DR   ExpressionAtlas; P11881; baseline and differential.
DR   Genevisible; P11881; MM.
DR   GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0031301; C:integral component of organelle membrane; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031088; C:platelet dense granule membrane; ISO:MGI.
DR   GO; GO:0031094; C:platelet dense tubular network; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR   GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0015278; F:calcium-release channel activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR   GO; GO:0098695; F:inositol 1,4,5-trisphosphate receptor activity involved in regulation of postsynaptic cytosolic calcium levels; IMP:SynGO.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR   GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
DR   GO; GO:0042045; P:epithelial fluid transport; IDA:UniProtKB.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; ISO:MGI.
DR   GO; GO:0050849; P:negative regulation of calcium-mediated signaling; ISO:MGI.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
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; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
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; SSF82109; SSF82109; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Calcium;
KW   Calcium channel; Calcium transport; Complete proteome; Cytoplasm;
KW   Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW   Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation.
FT   CHAIN         1   2749       Inositol 1,4,5-trisphosphate receptor
FT                                type 1.
FT                                /FTId=PRO_0000153921.
FT   TOPO_DOM      1   2273       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2274   2294       Helical. {ECO:0000255}.
FT   TOPO_DOM   2295   2305       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2306   2326       Helical. {ECO:0000255}.
FT   TOPO_DOM   2327   2352       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2353   2373       Helical. {ECO:0000255}.
FT   TOPO_DOM   2374   2396       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2397   2417       Helical. {ECO:0000255}.
FT   TOPO_DOM   2418   2439       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2440   2460       Helical. {ECO:0000255}.
FT   TOPO_DOM   2461   2569       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2570   2590       Helical. {ECO:0000255}.
FT   TOPO_DOM   2591   2749       Cytoplasmic. {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    373       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      379    435       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      265    269       Inositol 1,4,5-trisphosphate binding.
FT   REGION      508    511       Inositol 1,4,5-trisphosphate binding.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT   REGION     2463   2528       Interaction with ERP44.
FT                                {ECO:0000269|PubMed:15652484}.
FT   MOD_RES     482    482       Phosphotyrosine. {ECO:0000255}.
FT   MOD_RES    1588   1588       Phosphoserine.
FT                                {ECO:0000244|PubMed:17208939,
FT                                ECO:0000244|PubMed:18630941,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1755   1755       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:Q14643,
FT                                ECO:0000255}.
FT   MOD_RES    2655   2655       Phosphotyrosine. {ECO:0000255}.
FT   LIPID        56     56       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:25368151}.
FT   LIPID       849    849       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:25368151}.
FT   CROSSLNK    916    916       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK    962    962       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1571   1571       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1771   1771       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1884   1884       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1885   1885       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1886   1886       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1901   1901       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1924   1924       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   2118   2118       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   2257   2257       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   VAR_SEQ     318    332       Missing (in isoform 2, isoform 4, isoform
FT                                6 and isoform 8). {ECO:0000305}.
FT                                /FTId=VSP_002691.
FT   VAR_SEQ    1692   1714       Missing (in isoform 7 and isoform 8).
FT                                {ECO:0000305}.
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                                {ECO:0000305}.
FT                                /FTId=VSP_002693.
FT   VAR_SEQ    1716   1731       Missing (in isoform 5, isoform 6, isoform
FT                                7 and isoform 8). {ECO:0000305}.
FT                                /FTId=VSP_002694.
FT   MUTAGEN      56     56       C->A: Strongly reduced palmitoylation;
FT                                when associated with A-849 and A-2215.
FT                                {ECO:0000269|PubMed:25368151}.
FT   MUTAGEN     167    167       Y->A: Nearly abolishes calcium flux.
FT                                {ECO:0000269|PubMed:20813840}.
FT   MUTAGEN     168    168       K->A: Reduces calcium flux by about 50%.
FT                                {ECO:0000269|PubMed:20813840}.
FT   MUTAGEN     169    169       L->A: Reduces calcium flux by about 50%.
FT   MUTAGEN     267    267       T->A: Abolishes inositol 1,4,5-
FT                                triphosphate binding.
FT                                {ECO:0000269|PubMed:12442173}.
FT   MUTAGEN     567    567       Y->A,F: Abolishes inositol 1,4,5-
FT                                triphosphate binding.
FT                                {ECO:0000269|PubMed:12442173}.
FT   MUTAGEN     849    849       C->A: Strongly reduced palmitoylation;
FT                                when associated with A-56 and A-2215.
FT                                {ECO:0000269|PubMed:25368151}.
FT   MUTAGEN    1588   1588       S->A: Increases interaction with AHCYL1;
FT                                when associated with A-1755.
FT   MUTAGEN    1588   1588       S->E: Decreases interaction with AHCYL1;
FT                                when associated with A-1755.
FT   MUTAGEN    1755   1755       S->A: Increases interaction with AHCYL1;
FT                                when associated with A-1588.
FT   MUTAGEN    1755   1755       S->E: Decreases interaction with AHCYL1;
FT                                when associated with A-1588.
FT   MUTAGEN    2215   2215       C->A: Strongly reduced palmitoylation;
FT                                when associated with A-56 and A-849.
FT                                {ECO:0000269|PubMed:25368151}.
FT   MUTAGEN    2496   2496       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44. Complete loss of channel
FT                                inhibition by ERP44.
FT                                {ECO:0000269|PubMed:15652484}.
FT   MUTAGEN    2504   2504       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44. Complete loss of channel
FT                                inhibition by ERP44.
FT                                {ECO:0000269|PubMed:15652484}.
FT   MUTAGEN    2527   2527       C->S: Complete loss of channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44. {ECO:0000269|PubMed:15652484}.
FT   CONFLICT   1264   1264       N -> K (in Ref. 1; CAA33433).
FT                                {ECO:0000305}.
FT   CONFLICT   2675   2675       P -> L (in Ref. 1; CAA33433).
FT                                {ECO:0000305}.
FT   STRAND       14     23       {ECO:0000244|PDB:1XZZ}.
FT   STRAND       25     30       {ECO:0000244|PDB:1XZZ}.
FT   STRAND       36     39       {ECO:0000244|PDB:1XZZ}.
FT   HELIX        41     43       {ECO:0000244|PDB:1XZZ}.
FT   STRAND       46     48       {ECO:0000244|PDB:1XZZ}.
FT   HELIX        53     56       {ECO:0000244|PDB:1XZZ}.
FT   STRAND       58     61       {ECO:0000244|PDB:1XZZ}.
FT   HELIX        67     74       {ECO:0000244|PDB:1XZZ}.
FT   HELIX        86    109       {ECO:0000244|PDB:1XZZ}.
FT   TURN        110    112       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      120    125       {ECO:0000244|PDB:1XZZ}.
FT   TURN        126    129       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      130    139       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      141    143       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      146    154       {ECO:0000244|PDB:1XZZ}.
FT   HELIX       157    159       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      161    167       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      181    189       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      193    199       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      201    205       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      207    213       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      217    223       {ECO:0000244|PDB:1XZZ}.
FT   STRAND      239    244       {ECO:0000244|PDB:1N4K}.
FT   TURN        245    248       {ECO:0000244|PDB:1N4K}.
FT   STRAND      249    255       {ECO:0000244|PDB:1N4K}.
FT   STRAND      257    265       {ECO:0000244|PDB:1N4K}.
FT   STRAND      269    271       {ECO:0000244|PDB:1N4K}.
FT   HELIX       272    274       {ECO:0000244|PDB:1N4K}.
FT   HELIX       278    280       {ECO:0000244|PDB:1N4K}.
FT   STRAND      282    286       {ECO:0000244|PDB:1N4K}.
FT   STRAND      303    307       {ECO:0000244|PDB:1N4K}.
FT   TURN        308    310       {ECO:0000244|PDB:1N4K}.
FT   STRAND      313    318       {ECO:0000244|PDB:1N4K}.
FT   STRAND      353    359       {ECO:0000244|PDB:1N4K}.
FT   HELIX       364    366       {ECO:0000244|PDB:1N4K}.
FT   STRAND      368    371       {ECO:0000244|PDB:1N4K}.
FT   STRAND      388    392       {ECO:0000244|PDB:1N4K}.
FT   TURN        393    396       {ECO:0000244|PDB:1N4K}.
FT   STRAND      397    406       {ECO:0000244|PDB:1N4K}.
FT   STRAND      409    412       {ECO:0000244|PDB:1N4K}.
FT   STRAND      415    423       {ECO:0000244|PDB:1N4K}.
FT   STRAND      430    434       {ECO:0000244|PDB:1N4K}.
FT   HELIX       437    461       {ECO:0000244|PDB:1N4K}.
FT   HELIX       467    484       {ECO:0000244|PDB:1N4K}.
FT   TURN        485    487       {ECO:0000244|PDB:1N4K}.
FT   HELIX       495    499       {ECO:0000244|PDB:1N4K}.
FT   HELIX       504    512       {ECO:0000244|PDB:1N4K}.
FT   HELIX       515    524       {ECO:0000244|PDB:1N4K}.
FT   HELIX       525    527       {ECO:0000244|PDB:1N4K}.
FT   HELIX       547    564       {ECO:0000244|PDB:1N4K}.
FT   HELIX       568    585       {ECO:0000244|PDB:1N4K}.
FT   HELIX       589    599       {ECO:0000244|PDB:1N4K}.
SQ   SEQUENCE   2749 AA;  313167 MW;  FC4CF3ABB85EB82B 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
     LFLNPGILEA 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 LDWFPRMRAM SLVSSDSEGE QNELRNLQEK
     LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA
//
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