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   27-MAR-2024, entry version 242.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Purkinje cell;
RX   PubMed=2554142; DOI=10.1038/342032a0;
RA   Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N., 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., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, AND ALTERNATIVE
RP   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 project:
RT   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; DOI=10.1523/jneurosci.08-12-04780.1988;
RA   Nordquist D.T., Kozak C.A., Orr H.T.;
RT   "cDNA cloning and characterization of three genes uniquely expressed in
RT   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 CYS-2527.
RX   PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA   Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., 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   INTERACTION WITH IRAG1, AND SUBCELLULAR LOCATION.
RX   PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
RA   Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T.,
RA   Wilm M., Hofmann F., Massberg S., Schlossmann J.;
RT   "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and
RT   thrombus formation.";
RL   Blood 109:552-559(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION BY
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION BY
RP   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 affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [14]
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., Tabas I.;
RT   "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate
RT   receptor activity in endoplasmic reticulum stress-induced apoptosis.";
RL   J. Cell Biol. 186:783-792(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION BY
RP   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [16]
RP   FUNCTION, AND MUTAGENESIS OF TYR-167; LYS-168 AND LEU-169.
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 mediates
RT   functional coupling between ligand binding and channel opening.";
RL   J. Biol. Chem. 285:36081-36091(2010).
RN   [17]
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 protein in
RT   T and B lymphocytes.";
RL   FEBS Open Bio 2:255-259(2012).
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., Ando H.,
RA   Mizutani A., Abe T., Kiyonari H., Seki G., Yule D., Mikoshiba K.,
RA   Muallem S.;
RT   "Irbit mediates synergy between ca(2+) and cAMP signaling pathways during
RT   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 proteolytic
RT   cleavage.";
RL   J. Biol. Chem. 288:25340-25349(2013).
RN   [20]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24374158; DOI=10.1016/j.ydbio.2013.12.025;
RA   Kim B., Zhang X., Kan R., Cohen R., Mukai C., Travis A.J., Coonrod S.A.;
RT   "The role of MATER in endoplasmic reticulum distribution and calcium
RT   homeostasis in mouse oocytes.";
RL   Dev. Biol. 386:331-339(2014).
RN   [21]
RP   PALMITOYLATION AT CYS-56 AND CYS-849, AND MUTAGENESIS OF CYS-56; CYS-849
RP   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 receptor
RT   requires palmitoylation by a DHHC6/selenoprotein K complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16478-16483(2014).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 224-604 IN COMPLEX WITH INOSITOL
RP   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., Mikoshiba K.,
RA   Ikura M.;
RT   "Structure of the inositol 1,4,5-trisphosphate receptor binding core in
RT   complex with its ligand.";
RL   Nature 420:696-700(2002).
RN   [23]
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 the
CC       endoplasmic reticulum following stimulation by inositol 1,4,5-
CC       trisphosphate. Involved in the regulation of epithelial secretion of
CC       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 of
CC       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. Interacts with ERP44 in a pH-, redox state- and calcium-
CC       dependent manner which results in the inhibition the calcium channel
CC       activity. The strength of this interaction inversely correlates with
CC       calcium concentration. Part of cGMP kinase signaling complex at least
CC       composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban,
CC       PRKG1 and ITPR1. Interacts with IRAG1 (PubMed:16990611). Interacts with
CC       CABP1 (via N-terminus) (By similarity). Interacts with TESPA1.
CC       Interacts (when not phosphorylated) with AHCYL1 (when phosphorylated);
CC       the interaction suppresses inositol 1,4,5-trisphosphate binding to
CC       ITPR1 and is increased in the presence of BCL2L10 (PubMed:23542070).
CC       Interacts with AHCYL2 (with lower affinity than with AHCYL1) (By
CC       similarity). Interacts with BCL2L10; the interaction is increased in
CC       the presence of AHCLY1 (By similarity). Interacts with BOK (via BH4
CC       domain); protects ITPR1 from proteolysis by CASP3 during apoptosis
CC       (PubMed:23884412). {ECO:0000250|UniProtKB:P29994,
CC       ECO:0000250|UniProtKB:Q14643, ECO:0000250|UniProtKB:Q9TU34,
CC       ECO:0000269|PubMed:12442173, ECO:0000269|PubMed:12525476,
CC       ECO:0000269|PubMed:15652484, ECO:0000269|PubMed:16527252,
CC       ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:23542070,
CC       ECO:0000269|PubMed:23650607, ECO:0000269|PubMed:23884412}.
CC   -!- INTERACTION:
CC       P11881; Q8VDN2: Atp1a1; NbExp=3; IntAct=EBI-541478, EBI-444536;
CC       P11881; Q6PIE5: Atp1a2; NbExp=3; IntAct=EBI-541478, EBI-6665421;
CC       P11881; Q9D1Q6: Erp44; NbExp=5; IntAct=EBI-541478, EBI-541567;
CC       P11881; O35157: Slc8a1; NbExp=4; IntAct=EBI-541478, EBI-8351080;
CC       P11881; P10415: BCL2; Xeno; NbExp=3; IntAct=EBI-541478, EBI-77694;
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. {ECO:0000250|UniProtKB:Q9TU34,
CC       ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:24374158}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=There is a combination of two alternatively spliced domains
CC         at site SI and site SII (A, B and C). Experimental confirmation may
CC         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 the
CC       ligand-induced opening of the calcium channels. Phosphorylation by PKA
CC       increases the interaction with inositol 1,4,5-trisphosphate and
CC       decreases the interaction with AHCYL1. {ECO:0000305|PubMed:23542070}.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC       {ECO:0000250|UniProtKB:Q14643}.
CC   -!- PTM: Ubiquitination at multiple lysines targets ITPR1 for proteasomal
CC       degradation. Approximately 40% of the ITPR1-associated ubiquitin is
CC       monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-
CC       linked (By similarity). {ECO:0000250|UniProtKB:P29994}.
CC   -!- PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulation of
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-binding
CC       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=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH03271.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; -; 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   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   SASBDB; P11881; -.
DR   SMR; P11881; -.
DR   BioGRID; 200847; 42.
DR   CORUM; P11881; -.
DR   DIP; DIP-32243N; -.
DR   IntAct; P11881; 21.
DR   MINT; P11881; -.
DR   STRING; 10090.ENSMUSP00000032192; -.
DR   GlyConnect; 2438; 14 N-Linked glycans (1 site). [P11881-3]
DR   GlyGen; P11881; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P11881; -.
DR   PhosphoSitePlus; P11881; -.
DR   SwissPalm; P11881; -.
DR   EPD; P11881; -.
DR   jPOST; P11881; -.
DR   MaxQB; P11881; -.
DR   PaxDb; 10090-ENSMUSP00000032192; -.
DR   PeptideAtlas; P11881; -.
DR   ProteomicsDB; 269006; -. [P11881-1]
DR   ProteomicsDB; 269007; -. [P11881-2]
DR   ProteomicsDB; 269008; -. [P11881-3]
DR   ProteomicsDB; 269009; -. [P11881-4]
DR   ProteomicsDB; 269010; -. [P11881-5]
DR   ProteomicsDB; 269011; -. [P11881-6]
DR   ProteomicsDB; 269012; -. [P11881-7]
DR   ProteomicsDB; 269013; -. [P11881-8]
DR   Pumba; P11881; -.
DR   ABCD; P11881; 1 sequenced antibody.
DR   Antibodypedia; 5503; 520 antibodies from 41 providers.
DR   DNASU; 16438; -.
DR   Ensembl; ENSMUST00000032192.9; ENSMUSP00000032192.7; ENSMUSG00000030102.12. [P11881-1]
DR   Ensembl; ENSMUST00000203615.3; ENSMUSP00000144880.2; ENSMUSG00000030102.12. [P11881-3]
DR   GeneID; 16438; -.
DR   KEGG; mmu:16438; -.
DR   UCSC; uc033itt.1; mouse. [P11881-1]
DR   AGR; MGI:96623; -.
DR   CTD; 3708; -.
DR   MGI; MGI:96623; Itpr1.
DR   VEuPathDB; HostDB:ENSMUSG00000030102; -.
DR   eggNOG; KOG3533; Eukaryota.
DR   GeneTree; ENSGT00940000155071; -.
DR   HOGENOM; CLU_000206_1_0_1; -.
DR   InParanoid; P11881; -.
DR   OMA; KMERVIF; -.
DR   OrthoDB; 5480299at2759; -.
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   BioGRID-ORCS; 16438; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Itpr1; mouse.
DR   EvolutionaryTrace; P11881; -.
DR   PRO; PR:P11881; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P11881; Protein.
DR   Bgee; ENSMUSG00000030102; Expressed in cerebellar vermis and 268 other cell types or tissues.
DR   ExpressionAtlas; P11881; baseline and differential.
DR   GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0016020; C:membrane; 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; IBA:GO_Central.
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; IDA:SynGO.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IPI: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; IDA: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:0019904; F:protein domain specific binding; IPI: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:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP: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:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IMP:MGI.
DR   GO; GO:0097421; P:liver regeneration; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0050849; P:negative regulation of calcium-mediated signaling; ISO:MGI.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP: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:0032024; P:positive regulation of insulin secretion; IMP: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: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   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 1.25.10.30; IP3 receptor type 1 binding core, RIH domain; 1.
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_IP3_receptor.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR   PANTHER; PTHR45816:SF2; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; 1.
DR   PANTHER; PTHR45816; MIR DOMAIN-CONTAINING PROTEIN; 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; IP3 receptor type 1 binding core, domain 2; 2.
DR   SUPFAM; SSF82109; MIR domain; 2.
DR   PROSITE; PS50919; MIR; 5.
DR   Genevisible; P11881; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Calcium; Calcium channel;
KW   Calcium transport; Cytoplasm; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endoplasmic reticulum; Ion channel;
KW   Ion transport; Isopeptide bond; Ligand-gated ion channel; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..2749
FT                   /note="Inositol 1,4,5-trisphosphate receptor type 1"
FT                   /id="PRO_0000153921"
FT   TOPO_DOM        1..2273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2274..2294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2295..2305
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2306..2326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2327..2352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2353..2373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2374..2396
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2397..2417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2418..2439
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2440..2460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2461..2569
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2570..2590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2591..2749
FT                   /note="Cytoplasmic"
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..373
FT                   /note="MIR 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          379..435
FT                   /note="MIR 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   REGION          1005..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1695..1730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1881..1906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1932..1952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2463..2528
FT                   /note="Interaction with ERP44"
FT                   /evidence="ECO:0000269|PubMed:15652484"
FT   REGION          2721..2749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1705..1719
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   BINDING         508..511
FT                   /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:203600"
FT   BINDING         567..569
FT                   /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:203600"
FT   MOD_RES         482
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1755
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q14643, ECO:0000255"
FT   MOD_RES         2655
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   LIPID           56
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:25368151"
FT   LIPID           849
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:25368151"
FT   CROSSLNK        916
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        962
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1571
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1771
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1884
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1885
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1886
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1901
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        1924
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        2118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   CROSSLNK        2257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P29994"
FT   VAR_SEQ         318..332
FT                   /note="Missing (in isoform 2, isoform 4, isoform 6 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002691"
FT   VAR_SEQ         1692..1714
FT                   /note="Missing (in isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002692"
FT   VAR_SEQ         1715
FT                   /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT                   6, isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002693"
FT   VAR_SEQ         1716..1731
FT                   /note="Missing (in isoform 5, isoform 6, isoform 7 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002694"
FT   MUTAGEN         56
FT                   /note="C->A: Strongly reduced palmitoylation; when
FT                   associated with A-849 and A-2215."
FT                   /evidence="ECO:0000269|PubMed:25368151"
FT   MUTAGEN         167
FT                   /note="Y->A: Nearly abolishes calcium flux."
FT                   /evidence="ECO:0000269|PubMed:20813840"
FT   MUTAGEN         168
FT                   /note="K->A: Reduces calcium flux by about 50%."
FT                   /evidence="ECO:0000269|PubMed:20813840"
FT   MUTAGEN         169
FT                   /note="L->A: Reduces calcium flux by about 50%."
FT                   /evidence="ECO:0000269|PubMed:20813840"
FT   MUTAGEN         267
FT                   /note="T->A: Abolishes inositol 1,4,5-triphosphate
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:12442173"
FT   MUTAGEN         567
FT                   /note="Y->A,F: Abolishes inositol 1,4,5-triphosphate
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:12442173"
FT   MUTAGEN         849
FT                   /note="C->A: Strongly reduced palmitoylation; when
FT                   associated with A-56 and A-2215."
FT                   /evidence="ECO:0000269|PubMed:25368151"
FT   MUTAGEN         1588
FT                   /note="S->A: Increases interaction with AHCYL1; when
FT                   associated with A-1755."
FT                   /evidence="ECO:0000269|PubMed:23542070"
FT   MUTAGEN         1588
FT                   /note="S->E: Decreases interaction with AHCYL1; when
FT                   associated with A-1755."
FT                   /evidence="ECO:0000269|PubMed:23542070"
FT   MUTAGEN         1755
FT                   /note="S->A: Increases interaction with AHCYL1; when
FT                   associated with A-1588."
FT                   /evidence="ECO:0000269|PubMed:23542070"
FT   MUTAGEN         1755
FT                   /note="S->E: Decreases interaction with AHCYL1; when
FT                   associated with A-1588."
FT                   /evidence="ECO:0000269|PubMed:23542070"
FT   MUTAGEN         2215
FT                   /note="C->A: Strongly reduced palmitoylation; when
FT                   associated with A-56 and A-849."
FT                   /evidence="ECO:0000269|PubMed:25368151"
FT   MUTAGEN         2496
FT                   /note="C->S: No effect on channel activity. Significant
FT                   decrease of interaction with ERP44. Complete loss of
FT                   channel inhibition by ERP44."
FT                   /evidence="ECO:0000269|PubMed:15652484"
FT   MUTAGEN         2504
FT                   /note="C->S: No effect on channel activity. Significant
FT                   decrease of interaction with ERP44. Complete loss of
FT                   channel inhibition by ERP44."
FT                   /evidence="ECO:0000269|PubMed:15652484"
FT   MUTAGEN         2527
FT                   /note="C->S: Complete loss of channel activity. Significant
FT                   decrease of interaction with ERP44."
FT                   /evidence="ECO:0000269|PubMed:15652484"
FT   CONFLICT        1264
FT                   /note="N -> K (in Ref. 1; CAA33433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2675
FT                   /note="P -> L (in Ref. 1; CAA33433)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..23
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   HELIX           67..74
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   HELIX           86..109
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          146..154
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          161..167
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          181..189
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          207..213
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:1XZZ"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   TURN            245..248
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          249..255
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          257..265
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          282..286
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          353..359
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          368..371
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          388..392
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   TURN            393..396
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          397..406
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          409..412
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          415..423
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           437..461
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           467..484
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   TURN            485..487
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           495..499
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           504..512
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           515..524
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           525..527
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           547..564
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           568..585
FT                   /evidence="ECO:0007829|PDB:1N4K"
FT   HELIX           589..599
FT                   /evidence="ECO:0007829|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
//