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Database: UniProt
Entry: ITPR1_HUMAN
LinkDB: ITPR1_HUMAN
Original site: ITPR1_HUMAN 
ID   ITPR1_HUMAN             Reviewed;        2758 AA.
AC   Q14643; E7EPX7; E9PDE9; Q14660; Q99897;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 3.
DT   13-FEB-2019, entry version 211.
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=Type 1 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 1 InsP3 receptor;
GN   Name=ITPR1; Synonyms=INSP3R1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   TISSUE=Myeloid, and Uterus;
RX   PubMed=7945203; DOI=10.1042/bj3020781;
RA   Yamada N., Makino Y., Clark R.A., Pearson D.W., Mattei M.-G.,
RA   Guenet J.-L., Ohama E., Fujino I., Miyawaki A., Furuichi T.,
RA   Mikoshiba K.;
RT   "Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1:
RT   structure, function, regulation of expression and chromosomal
RT   localization.";
RL   Biochem. J. 302:781-790(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PHOSPHORYLATION.
RC   TISSUE=T-cell;
RX   PubMed=7852357; DOI=10.1074/jbc.270.6.2833;
RA   Harnick D.J., Jayaraman T., Ma Y., Mulieri P., Go L.O., Marks A.R.;
RT   "The human type 1 inositol 1,4,5-trisphosphate receptor from T
RT   lymphocytes. Structure, localization, and tyrosine phosphorylation.";
RL   J. Biol. Chem. 270:2833-2840(1995).
RN   [3]
RP   SEQUENCE REVISION TO 431; 1012-1017; 1460; 1823; 2324; 2330; 2334;
RP   2337; 2346; 2358; 2361; 2372; 2396; 2418; 2426; 2434 AND 2741.
RA   Marks A.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=7500840; DOI=10.1016/0169-328X(95)00089-B;
RA   Nucifora F.C. Jr., Li S.-H., Danoff S., Ullrich A., Ross C.A.;
RT   "Molecular cloning of a cDNA for the human inositol 1,4,5-
RT   trisphosphate receptor type 1, and the identification of a third
RT   alternatively spliced variant.";
RL   Brain Res. Mol. Brain Res. 32:291-296(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1548-1723 (ISOFORMS 3 AND 4).
RX   PubMed=8648241; DOI=10.1080/095530096145544;
RA   Yan J., Khanna K.K., Lavin M.F.;
RT   "Induction of inositol 1,4,5 trisphosphate receptor genes by ionizing
RT   radiation.";
RL   Int. J. Radiat. Biol. 69:539-546(1996).
RN   [7]
RP   INTERACTION WITH CABP1.
RX   PubMed=12032348; DOI=10.1073/pnas.102006299;
RA   Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K.,
RA   Haeseleer F., Foskett J.K.;
RT   "Identification of a family of calcium sensors as protein ligands of
RT   inositol trisphosphate receptor Ca(2+) release channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN   [8]
RP   INTERACTION WITH CABP1.
RX   PubMed=14685260; DOI=10.1038/sj.emboj.7600037;
RA   Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D.,
RA   Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J.,
RA   Holmes A.B., Berridge M.J., Roderick H.L.;
RT   "Regulation of InsP3 receptor activity by neuronal Ca2+-binding
RT   proteins.";
RL   EMBO J. 23:312-321(2004).
RN   [9]
RP   INTERACTION WITH ERP44.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   INTERACTION WITH AHCYL1, AND MUTAGENESIS OF ARG-241; LYS-249; ARG-265;
RP   THR-267; ARG-269; ARG-504; ARG-506; LYS-508; ARG-511; TYR-567; ARG-568
RP   AND LYS-569.
RX   PubMed=16793548; DOI=10.1016/j.molcel.2006.05.017;
RA   Ando H., Mizutani A., Kiefer H., Tsuzurugi D., Michikawa T.,
RA   Mikoshiba K.;
RT   "IRBIT suppresses IP3 receptor activity by competing with IP3 for the
RT   common binding site on the IP3 receptor.";
RL   Mol. Cell 22:795-806(2006).
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).
RN   [13]
RP   INVOLVEMENT IN SCA15.
RX   PubMed=17590087; DOI=10.1371/journal.pgen.0030108;
RA   van de Leemput J., Chandran J., Knight M.A., Holtzclaw L.A.,
RA   Scholz S., Cookson M.R., Houlden H., Gwinn-Hardy K., Fung H.-C.,
RA   Lin X., Hernandez D., Simon-Sanchez J., Wood N.W., Giunti P.,
RA   Rafferty I., Hardy J., Storey E., Gardner R.J.M., Forrest S.M.,
RA   Fisher E.M.C., Russell J.T., Cai H., Singleton A.B.;
RT   "Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia
RT   15 in humans.";
RL   PLoS Genet. 3:1076-1082(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598 AND SER-1764, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [15]
RP   INTERACTION WITH AHCYL1 AND AHCYL2.
RX   PubMed=19220705; DOI=10.1111/j.1471-4159.2009.05979.x;
RA   Ando H., Mizutani A., Mikoshiba K.;
RT   "An IRBIT homologue lacks binding activity to inositol 1,4,5-
RT   trisphosphate receptor due to the unique N-terminal appendage.";
RL   J. Neurochem. 109:539-550(2009).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2512.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598 AND SER-1764, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [22]
RP   VARIANT SCA15 LEU-1083.
RX   PubMed=18579805; DOI=10.1212/01.wnl.0000311277.71046.a0;
RA   Hara K., Shiga A., Nozaki H., Mitsui J., Takahashi Y., Ishiguro H.,
RA   Yomono H., Kurisaki H., Goto J., Ikeuchi T., Tsuji S., Nishizawa M.,
RA   Onodera O.;
RT   "Total deletion and a missense mutation of ITPR1 in Japanese SCA15
RT   families.";
RL   Neurology 71:547-551(2008).
RN   [23]
RP   VARIANTS SCA29 ASP-602 AND MET-1562.
RX   PubMed=22986007; DOI=10.1186/1750-1172-7-67;
RA   Huang L., Chardon J.W., Carter M.T., Friend K.L., Dudding T.E.,
RA   Schwartzentruber J., Zou R., Schofield P.W., Douglas S., Bulman D.E.,
RA   Boycott K.M.;
RT   "Missense mutations in ITPR1 cause autosomal dominant congenital
RT   nonprogressive spinocerebellar ataxia.";
RL   Orphanet J. Rare Dis. 7:67-67(2012).
RN   [24]
RP   VARIANT SCA29 MET-1562.
RX   PubMed=26770814; DOI=10.1186/s40673-016-0040-8;
RA   Shadrina M.I., Shulskaya M.V., Klyushnikov S.A., Nikopensius T.,
RA   Nelis M., Kivistik P.A., Komar A.A., Limborska S.A.,
RA   Illarioshkin S.N., Slominsky P.A.;
RT   "ITPR1 gene p.Val1553Met mutation in Russian family with mild
RT   Spinocerebellar ataxia.";
RL   Cerebellum Ataxias 3:2-2(2016).
RN   [25]
RP   INVOLVEMENT IN GLSP, VARIANTS GLSP LEU-2601 AND LYS-2611 DEL,
RP   CHARACTERIZATION OF VARIANT GLSP LYS-2611 DEL, AND FUNCTION.
RX   PubMed=27108797; DOI=10.1016/j.ajhg.2016.03.004;
RA   Gerber S., Alzayady K.J., Burglen L., Bremond-Gignac D., Marchesin V.,
RA   Roche O., Rio M., Funalot B., Calmon R., Durr A.,
RA   Gil-da-Silva-Lopes V.L., Ribeiro Bittar M.F., Orssaud C., Heron B.,
RA   Ayoub E., Berquin P., Bahi-Buisson N., Bole C., Masson C., Munnich A.,
RA   Simons M., Delous M., Dollfus H., Boddaert N., Lyonnet S., Kaplan J.,
RA   Calvas P., Yule D.I., Rozet J.M., Fares Taie L.;
RT   "Recessive and dominant de novo ITPR1 mutations cause Gillespie
RT   syndrome.";
RL   Am. J. Hum. Genet. 98:971-980(2016).
RN   [26]
RP   INVOLVEMENT IN GLSP, VARIANTS GLSP GLN-2109; ARG-2554 AND LYS-2611
RP   DEL, AND SUBCELLULAR LOCATION.
RX   PubMed=27108798; DOI=10.1016/j.ajhg.2016.03.018;
RG   DDD Study;
RA   McEntagart M., Williamson K.A., Rainger J.K., Wheeler A.,
RA   Seawright A., De Baere E., Verdin H., Bergendahl L.T., Quigley A.,
RA   Rainger J., Dixit A., Sarkar A., Lopez Laso E., Sanchez-Carpintero R.,
RA   Barrio J., Bitoun P., Prescott T., Riise R., McKee S., Cook J.,
RA   McKie L., Ceulemans B., Meire F., Temple I.K., Prieur F., Williams J.,
RA   Clouston P., Nemeth A.H., Banka S., Bengani H., Handley M., Freyer E.,
RA   Ross A., van Heyningen V., Marsh J.A., Elmslie F., FitzPatrick D.R.;
RT   "A restricted repertoire of de novo mutations in ITPR1 cause Gillespie
RT   syndrome with evidence for dominant-negative effect.";
RL   Am. J. Hum. Genet. 98:981-992(2016).
CC   -!- FUNCTION: Intracellular channel that mediates calcium release from
CC       the endoplasmic reticulum following stimulation by inositol 1,4,5-
CC       trisphosphate (PubMed:27108797). Involved in the regulation of
CC       epithelial secretion of electrolytes and fluid through the
CC       interaction with AHCYL1 (By similarity). Plays a role in ER
CC       stress-induced apoptosis. Cytoplasmic calcium released from the ER
CC       triggers apoptosis by the activation of CaM kinase II, eventually
CC       leading to the activation of downstream apoptosis pathways (By
CC       similarity). {ECO:0000250|UniProtKB:P11881,
CC       ECO:0000269|PubMed:27108797}.
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
CC       channel activity. The strength of this interaction inversely
CC       correlates with calcium concentration. Part of cGMP kinase
CC       signaling complex at least composed of ACTA2/alpha-actin,
CC       CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. Interacts
CC       with MRVI1 and CABP1 (via N-terminus). Interacts with TESPA1.
CC       Interacts (when not phosphorylated) with AHCYL1 (when
CC       phosphorylated); the interaction suppresses inositol 1,4,5-
CC       trisphosphate binding to ITPR1 (PubMed:16793548). Interacts with
CC       AHCYL2 (with lower affinity than with AHCYL1) (PubMed:19220705).
CC       Interacts with BOK (via BH4 domain); protects ITPR1 from
CC       proteolysis by CASP3 during apoptosis (PubMed:23884412).
CC       {ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:14685260,
CC       ECO:0000269|PubMed:15652484, ECO:0000269|PubMed:16793548,
CC       ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:19220705,
CC       ECO:0000269|PubMed:23650607, ECO:0000269|PubMed:23884412}.
CC   -!- INTERACTION:
CC       P31749:AKT1; NbExp=2; IntAct=EBI-465548, EBI-296087;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:27108798}; 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:0000269|PubMed:27108798}. 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 three alternatively spliced
CC         domains at site SI, SIII and site SII (A and C). Experimental
CC         confirmation may be lacking for some isoforms.;
CC       Name=1; Synonyms=SISIIISIIAC;
CC         IsoId=Q14643-1; Sequence=Displayed;
CC       Name=2; Synonyms=SI-SIIISIIAC;
CC         IsoId=Q14643-2; Sequence=VSP_002687;
CC       Name=3; Synonyms=SISIII-SII;
CC         IsoId=Q14643-3; Sequence=VSP_002688, VSP_002689, VSP_002690;
CC       Name=4; Synonyms=SI-SIII-SII;
CC         IsoId=Q14643-4; Sequence=VSP_002687, VSP_002688, VSP_002689,
CC                                  VSP_002690;
CC       Name=5; Synonyms=SI-SIII-SIIAC;
CC         IsoId=Q14643-5; Sequence=VSP_002687, VSP_002688;
CC       Name=6; Synonyms=SISIIISIIA;
CC         IsoId=Q14643-6; Sequence=VSP_002690;
CC       Name=7; Synonyms=SI-SIII-SIIA;
CC         IsoId=Q14643-7; Sequence=VSP_002687, VSP_002690;
CC       Name=8; Synonyms=SI-SIII-SIIA;
CC         IsoId=Q14643-8; Sequence=VSP_002687, VSP_002688, VSP_002690;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
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 on tyrosine residues.
CC       {ECO:0000269|PubMed:7852357}.
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: 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:0000250|UniProtKB:P11881}.
CC   -!- PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulate
CC       ITPR1 stability and function. {ECO:0000250|UniProtKB:P11881}.
CC   -!- DISEASE: Spinocerebellar ataxia 15 (SCA15) [MIM:606658]:
CC       Spinocerebellar ataxia is a clinically and genetically
CC       heterogeneous group of cerebellar disorders. Patients show
CC       progressive incoordination of gait and often poor coordination of
CC       hands, speech and eye movements, due to degeneration of the
CC       cerebellum with variable involvement of the brainstem and spinal
CC       cord. SCA15 is an autosomal dominant cerebellar ataxia (ADCA). It
CC       is very slow progressing form with a wide range of onset, ranging
CC       from childhood to adult. Most patients remain ambulatory.
CC       {ECO:0000269|PubMed:17590087, ECO:0000269|PubMed:18579805}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Spinocerebellar ataxia 29 (SCA29) [MIM:117360]: An
CC       autosomal dominant, congenital spinocerebellar ataxia
CC       characterized by early motor delay, hypotonia and mild cognitive
CC       delay. Affected individuals develop a very slowly progressive or
CC       non-progressive gait and limb ataxia associated with cerebellar
CC       atrophy on brain imaging. Additional variable features include
CC       nystagmus, dysarthria, and tremor. {ECO:0000269|PubMed:22986007,
CC       ECO:0000269|PubMed:26770814}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Gillespie syndrome (GLSP) [MIM:206700]: A rare disease
CC       characterized by bilateral iris hypoplasia, congenital hypotonia,
CC       non-progressive ataxia, progressive cerebellar atrophy, and mental
CC       retardation. {ECO:0000269|PubMed:27108797,
CC       ECO:0000269|PubMed:27108798}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
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   -!- CAUTION: Alternative splice sites (AA 1053-1054) represent a non-
CC       canonical GA-AG donor-acceptor pair, but are well-supported by all
CC       available human transcripts, and by homologous transcripts in
CC       mouse, rat and cow. {ECO:0000305}.
DR   EMBL; D26070; BAA05065.1; -; mRNA.
DR   EMBL; L38019; AAB04947.2; -; mRNA.
DR   EMBL; U23850; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC018816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S82269; AAD14386.1; -; mRNA.
DR   CCDS; CCDS46740.2; -. [Q14643-3]
DR   CCDS; CCDS54550.1; -. [Q14643-4]
DR   CCDS; CCDS54551.1; -. [Q14643-2]
DR   PIR; A55713; A55713.
DR   PIR; S54974; S54974.
DR   RefSeq; NP_001093422.2; NM_001099952.2. [Q14643-3]
DR   RefSeq; NP_001161744.1; NM_001168272.1. [Q14643-2]
DR   RefSeq; NP_002213.5; NM_002222.5. [Q14643-4]
DR   RefSeq; XP_011531985.1; XM_011533683.2. [Q14643-1]
DR   UniGene; Hs.567295; -.
DR   UniGene; Hs.715765; -.
DR   ProteinModelPortal; Q14643; -.
DR   SMR; Q14643; -.
DR   BioGrid; 109913; 52.
DR   CORUM; Q14643; -.
DR   DIP; DIP-29714N; -.
DR   ELM; Q14643; -.
DR   IntAct; Q14643; 23.
DR   STRING; 9606.ENSP00000306253; -.
DR   BindingDB; Q14643; -.
DR   ChEMBL; CHEMBL4046; -.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB04077; Glycerol.
DR   GuidetoPHARMACOLOGY; 743; -.
DR   TCDB; 1.A.3.2.6; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
DR   GlyConnect; 1399; -.
DR   iPTMnet; Q14643; -.
DR   PhosphoSitePlus; Q14643; -.
DR   SwissPalm; Q14643; -.
DR   BioMuta; ITPR1; -.
DR   DMDM; 519668682; -.
DR   EPD; Q14643; -.
DR   jPOST; Q14643; -.
DR   MaxQB; Q14643; -.
DR   PaxDb; Q14643; -.
DR   PeptideAtlas; Q14643; -.
DR   PRIDE; Q14643; -.
DR   ProteomicsDB; 60081; -.
DR   ProteomicsDB; 60082; -. [Q14643-2]
DR   ProteomicsDB; 60083; -. [Q14643-3]
DR   ProteomicsDB; 60084; -. [Q14643-4]
DR   ProteomicsDB; 60085; -. [Q14643-5]
DR   ProteomicsDB; 60086; -. [Q14643-6]
DR   ProteomicsDB; 60087; -. [Q14643-7]
DR   ProteomicsDB; 60088; -. [Q14643-8]
DR   Ensembl; ENST00000302640; ENSP00000306253; ENSG00000150995. [Q14643-2]
DR   Ensembl; ENST00000357086; ENSP00000349597; ENSG00000150995. [Q14643-3]
DR   Ensembl; ENST00000443694; ENSP00000401671; ENSG00000150995. [Q14643-2]
DR   Ensembl; ENST00000456211; ENSP00000397885; ENSG00000150995. [Q14643-4]
DR   Ensembl; ENST00000648309; ENSP00000497026; ENSG00000150995. [Q14643-5]
DR   Ensembl; ENST00000649015; ENSP00000497605; ENSG00000150995. [Q14643-1]
DR   GeneID; 3708; -.
DR   KEGG; hsa:3708; -.
DR   UCSC; uc003bqc.3; human. [Q14643-1]
DR   CTD; 3708; -.
DR   DisGeNET; 3708; -.
DR   EuPathDB; HostDB:ENSG00000150995.18; -.
DR   GeneCards; ITPR1; -.
DR   GeneReviews; ITPR1; -.
DR   HGNC; HGNC:6180; ITPR1.
DR   HPA; HPA014765; -.
DR   HPA; HPA016487; -.
DR   MalaCards; ITPR1; -.
DR   MIM; 117360; phenotype.
DR   MIM; 147265; gene.
DR   MIM; 206700; phenotype.
DR   MIM; 606658; phenotype.
DR   neXtProt; NX_Q14643; -.
DR   OpenTargets; ENSG00000150995; -.
DR   Orphanet; 1065; Aniridia-cerebellar ataxia-intellectual disability syndrome.
DR   Orphanet; 98769; Spinocerebellar ataxia type 15/16.
DR   Orphanet; 208513; Spinocerebellar ataxia type 29.
DR   PharmGKB; PA29978; -.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   GeneTree; ENSGT00940000155071; -.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q14643; -.
DR   KO; K04958; -.
DR   OMA; PRHAPYK; -.
DR   OrthoDB; 94996at2759; -.
DR   PhylomeDB; Q14643; -.
DR   TreeFam; TF312815; -.
DR   Reactome; R-HSA-112043; PLC beta mediated events.
DR   Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-HSA-1489509; DAG and IP3 signaling.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-HSA-4086398; Ca2+ pathway.
DR   Reactome; R-HSA-418457; cGMP effects.
DR   Reactome; R-HSA-422356; Regulation of insulin secretion.
DR   Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   SignaLink; Q14643; -.
DR   SIGNOR; Q14643; -.
DR   ChiTaRS; ITPR1; human.
DR   GeneWiki; ITPR1; -.
DR   GenomeRNAi; 3708; -.
DR   PRO; PR:Q14643; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000150995; Expressed in 227 organ(s), highest expression level in cauda epididymis.
DR   ExpressionAtlas; Q14643; baseline and differential.
DR   Genevisible; Q14643; HS.
DR   GO; GO:0005955; C:calcineurin complex; IEA:Ensembl.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031088; C:platelet dense granule membrane; IDA:BHF-UCL.
DR   GO; GO:0031094; C:platelet dense tubular network; IDA:BHF-UCL.
DR   GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IDA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0042045; P:epithelial fluid transport; IEA:Ensembl.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IDA:GO_Central.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IEA:Ensembl.
DR   InterPro; IPR016024; ARM-type_fold.
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; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Calcium; Calcium channel;
KW   Calcium transport; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW   Disease mutation; Endoplasmic reticulum; Glycoprotein; Ion channel;
KW   Ion transport; Isopeptide bond; Ligand-gated ion channel; Lipoprotein;
KW   Membrane; Mental retardation; Neurodegeneration; Palmitate;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Spinocerebellar ataxia; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN         1   2758       Inositol 1,4,5-trisphosphate receptor
FT                                type 1.
FT                                /FTId=PRO_0000153920.
FT   TOPO_DOM      1   2282       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2283   2303       Helical. {ECO:0000255}.
FT   TOPO_DOM   2304   2314       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2315   2335       Helical. {ECO:0000255}.
FT   TOPO_DOM   2336   2361       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2362   2382       Helical. {ECO:0000255}.
FT   TOPO_DOM   2383   2405       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2406   2426       Helical. {ECO:0000255}.
FT   TOPO_DOM   2427   2448       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2449   2469       Helical. {ECO:0000255}.
FT   TOPO_DOM   2470   2577       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2578   2598       Helical. {ECO:0000255}.
FT   TOPO_DOM   2599   2758       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                                {ECO:0000250}.
FT   REGION      508    511       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION     2472   2537       Interaction with ERP44. {ECO:0000250}.
FT   MOD_RES     482    482       Phosphotyrosine. {ECO:0000255}.
FT   MOD_RES    1598   1598       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1764   1764       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    2664   2664       Phosphotyrosine. {ECO:0000255}.
FT   LIPID        56     56       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:P11881}.
FT   LIPID       850    850       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:P11881}.
FT   CARBOHYD   2512   2512       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CROSSLNK    917    917       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK    972    972       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1581   1581       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1780   1780       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1893   1893       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1894   1894       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1895   1895       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1910   1910       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   1933   1933       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   2127   2127       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   CROSSLNK   2266   2266       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P29994}.
FT   VAR_SEQ     322    336       Missing (in isoform 2, isoform 4, isoform
FT                                5, isoform 7 and isoform 8).
FT                                {ECO:0000303|PubMed:7500840,
FT                                ECO:0000303|PubMed:7945203,
FT                                ECO:0000303|PubMed:8648241}.
FT                                /FTId=VSP_002687.
FT   VAR_SEQ     919    927       Missing (in isoform 3, isoform 4, isoform
FT                                5 and isoform 8).
FT                                {ECO:0000303|PubMed:7852357,
FT                                ECO:0000303|PubMed:7945203,
FT                                ECO:0000303|PubMed:8648241}.
FT                                /FTId=VSP_002688.
FT   VAR_SEQ    1702   1724       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:7852357,
FT                                ECO:0000303|PubMed:7945203,
FT                                ECO:0000303|PubMed:8648241}.
FT                                /FTId=VSP_002689.
FT   VAR_SEQ    1725   1740       Missing (in isoform 3, isoform 4, isoform
FT                                6, isoform 7 and isoform 8).
FT                                {ECO:0000303|PubMed:7852357,
FT                                ECO:0000303|PubMed:7945203,
FT                                ECO:0000303|PubMed:8648241}.
FT                                /FTId=VSP_002690.
FT   VARIANT     602    602       N -> D (in SCA29; dbSNP:rs397514536).
FT                                {ECO:0000269|PubMed:22986007}.
FT                                /FTId=VAR_069567.
FT   VARIANT     769    769       M -> V (in dbSNP:rs35789999).
FT                                /FTId=VAR_037005.
FT   VARIANT    1083   1083       P -> L (in SCA15; dbSNP:rs121912425).
FT                                {ECO:0000269|PubMed:18579805}.
FT                                /FTId=VAR_081167.
FT   VARIANT    1430   1430       I -> V (in dbSNP:rs3749383).
FT                                /FTId=VAR_037006.
FT   VARIANT    1562   1562       V -> M (in SCA29; dbSNP:rs397514535).
FT                                {ECO:0000269|PubMed:22986007,
FT                                ECO:0000269|PubMed:26770814}.
FT                                /FTId=VAR_069569.
FT   VARIANT    2109   2109       E -> Q (in GLSP).
FT                                {ECO:0000269|PubMed:27108798}.
FT                                /FTId=VAR_077462.
FT   VARIANT    2554   2554       G -> R (in GLSP; dbSNP:rs752281590).
FT                                {ECO:0000269|PubMed:27108798}.
FT                                /FTId=VAR_077463.
FT   VARIANT    2601   2601       F -> L (in GLSP; dbSNP:rs878853176).
FT                                {ECO:0000269|PubMed:27108797}.
FT                                /FTId=VAR_077464.
FT   VARIANT    2611   2611       Missing (in GLSP; alters calcium release
FT                                of isoform 3).
FT                                {ECO:0000269|PubMed:27108797,
FT                                ECO:0000269|PubMed:27108798}.
FT                                /FTId=VAR_077465.
FT   MUTAGEN     241    241       R->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     249    249       K->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     265    265       R->Q: No effect on interaction with
FT                                AHCYL1. {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     267    267       T->A: No effect on interaction with
FT                                AHCYL1. {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     269    269       R->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     504    504       R->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     506    506       R->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     508    508       K->A: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     511    511       R->A: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     567    567       Y->A: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     568    568       R->Q: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   MUTAGEN     569    569       K->A: Abolishes interaction with AHCYL1.
FT                                {ECO:0000269|PubMed:16793548}.
FT   CONFLICT   1557   1581       AIAIPVDLDSQVNNLFLKSHSIVQK -> HCHSRGPGQPSQ
FT                                QPLSQVPQHCAE (in Ref. 6; AAD14386).
FT                                {ECO:0000305}.
FT   CONFLICT   2302   2302       F -> L (in Ref. 2; AAB04947).
FT                                {ECO:0000305}.
FT   CONFLICT   2305   2305       F -> L (in Ref. 2; AAB04947).
FT                                {ECO:0000305}.
FT   CONFLICT   2448   2448       S -> A (in Ref. 4; U23850).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2758 AA;  313929 MW;  D29B072252B0D8E7 CRC64;
     MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PETGDLNNPP 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
     SPVKEDKEAF 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 SSTGENALEA GEDEEEVWLF WRDSNKEIRS KSVRELAQDA
     KEGQKEDRDV LSYYRYQLNL FARMCLDRQY LAINEISGQL DVDLILRCMS DENLPYDLRA
     SFCRLMLHMH VDRDPQEQVT PVKYARLWSE IPSEIAIDDY DSSGASKDEI KERFAQTMEF
     VEEYLRDVVC QRFPFSDKEK NKLTFEVVNL ARNLIYFGFY NFSDLLRLTK ILLAILDCVH
     VTTIFPISKM AKGEENKGNN DVEKLKSSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA
     PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQTSE
     TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH
     DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE
     LWVYKGQGPD ETMDGASGEN EHKKTEEGNN KPQKHESTSS 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 LFLKSHSIVQ KTAMNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL
     EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL
     CIKVLQTLRE MMTKDRGYGE KLISIDELDN AELPPAPDSE NATEELEPSP PLRQLEDHKR
     GEALRQVLVN RYYGNVRPSG RRESLTSFGN GPLSAGGPGK PGGGGGGSGS SSMSRGEMSL
     AEVQCHLDKE GASNLVIDLI MNASSDRVFH ESILLAIALL EGGNTTIQHS FFCRLTEDKK
     SEKFFKVFYD RMKVAQQEIK ATVTVNTSDL GNKKKDDEVD RDAPSRKKAK EPTTQITEEV
     RDQLLEASAA TRKAFTTFRR EADPDDHYQP GEGTQATADK AKDDLEMSAV ITIMQPILRF
     LQLLCENHNR DLQNFLRCQN NKTNYNLVCE TLQFLDCICG STTGGLGLLG LYINEKNVAL
     INQTLESLTE YCQGPCHENQ NCIATHESNG IDIITALILN DINPLGKKRM DLVLELKNNA
     SKLLLAIMES RHDSENAERI LYNMRPKELV EVIKKAYMQG EVEFEDGENG EDGAASPRNV
     GHNIYILAHQ LARHNKELQS MLKPGGQVDG DEALEFYAKH TAQIEIVRLD RTMEQIVFPV
     PSICEFLTKE SKLRIYYTTE RDEQGSKIND FFLRSEDLFN EMNWQKKLRA QPVLYWCARN
     MSFWSSISFN LAVLMNLLVA FFYPFKGVRG GTLEPHWSGL LWTAMLISLA IVIALPKPHG
     IRALIASTIL RLIFSVGLQP TLFLLGAFNV CNKIIFLMSF VGNCGTFTRG YRAMVLDVEF
     LYHLLYLVIC AMGLFVHEFF YSLLLFDLVY REETLLNVIK SVTRNGRSII LTAVLALILV
     YLFSIVGYLF FKDDFILEVD RLPNETAVPE TGESLASEFL FSDVCRVESG ENCSSPAPRE
     ELVPAEETEQ DKEHTCETLL MCIVTVLSHG LRSGGGVGDV LRKPSKEEPL FAARVIYDLL
     FFFMVIIIVL NLIFGVIIDT FADLRSEKQK KEEILKTTCF ICGLERDKFD NKTVTFEEHI
     KEEHNMWHYL CFIVLVKVKD STEYTGPESY VAEMIKERNL DWFPRMRAMS LVSSDSEGEQ
     NELRNLQEKL ESTMKLVTNL SGQLSELKDQ MTEQRKQKQR IGLLGHPPHM NVNPQQPA
//
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