ITPR_CAEEL
ID ITPR_CAEEL Reviewed; 2892 AA.
AC Q9Y0A1; D3NQ87; G5EBF6; Q8MXI9; Q9U3B3; Q9Y0A0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor itr-1 {ECO:0000303|PubMed:10499793};
DE AltName: Full=IP3 receptor {ECO:0000303|PubMed:10499793};
DE Short=IP3R {ECO:0000303|PubMed:10499793};
DE Short=InsP3R {ECO:0000303|PubMed:10610772};
DE AltName: Full=LET-23 fertility effector 1 {ECO:0000303|PubMed:9491893};
GN Name=itr-1 {ECO:0000312|EMBL:CCD63763.1, ECO:0000312|WormBase:F33D4.2a};
GN Synonyms=dec-4 {ECO:0000303|PubMed:10499793},
GN lfe-1 {ECO:0000303|PubMed:9491893}; ORFNames=F33D4.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF05302.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLY-103 AND CYS-1571.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10499793};
RX PubMed=10499793; DOI=10.1016/s0092-8674(00)81510-x;
RA Dal Santo P., Logan M.A., Chisholm A.D., Jorgensen E.M.;
RT "The inositol trisphosphate receptor regulates a 50-second behavioral
RT rhythm in C. elegans.";
RL Cell 98:757-767(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB45861.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; D; E AND F), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB45861.1};
RX PubMed=10610772; DOI=10.1006/jmbi.1999.3229;
RA Baylis H.A., Furuichi T., Yoshikawa F., Mikoshiba K., Sattelle D.B.;
RT "Inositol 1,4,5-trisphosphate receptors are strongly expressed in the
RT nervous system, pharynx, intestine, gonad and excretory cell of
RT Caenorhabditis elegans and are encoded by a single gene (itr-1).";
RL J. Mol. Biol. 294:467-476(1999).
RN [3] {ECO:0000312|EMBL:CCD63763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63763.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-371; ARG-557 AND SER-900.
RX PubMed=9491893; DOI=10.1016/s0092-8674(00)80945-9;
RA Clandinin T.R., DeModena J.A., Sternberg P.W.;
RT "Inositol trisphosphate mediates a RAS-independent response to LET-23
RT receptor tyrosine kinase activation in C. elegans.";
RL Cell 92:523-533(1998).
RN [5] {ECO:0000305}
RP ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
RX PubMed=11237590; DOI=10.1006/jmbi.2000.4388;
RA Gower N.J., Temple G.R., Schein J.E., Marra M., Walker D.S., Baylis H.A.;
RT "Dissection of the promoter region of the inositol 1,4,5-trisphosphate
RT receptor gene, itr-1, in C. elegans: a molecular basis for cell-specific
RT expression of IP3R isoforms.";
RL J. Mol. Biol. 306:145-157(2001).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-371; SER-900 AND CYS-1571.
RX PubMed=11553721; DOI=10.1091/mbc.12.9.2835;
RA Park B.J., Lee D.G., Yu J.R., Jung S.K., Choi K., Lee J., Lee J., Kim Y.S.,
RA Lee J.I., Kwon J.Y., Lee J., Singson A., Song W.K., Eom S.H., Park C.S.,
RA Kim D.H., Bandyopadhyay J., Ahnn J.;
RT "Calreticulin, a calcium-binding molecular chaperone, is required for
RT stress response and fertility in Caenorhabditis elegans.";
RL Mol. Biol. Cell 12:2835-2845(2001).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH MYO-1; MYO-2; UNC-54 AND NMY-2.
RX PubMed=12062062; DOI=10.1016/s0960-9822(02)00868-0;
RA Walker D.S., Ly S., Lockwood K.C., Baylis H.A.;
RT "A direct interaction between IP(3) receptors and myosin II regulates IP(3)
RT signaling in C. elegans.";
RL Curr. Biol. 12:951-956(2002).
RN [8] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-557; LYS-625;
RP ARG-628 AND CYS-1571.
RX PubMed=11950942; DOI=10.1091/mbc.01-08-0422;
RA Walker D.S., Gower N.J., Ly S., Bradley G.L., Baylis H.A.;
RT "Regulated disruption of inositol 1,4,5-trisphosphate signaling in
RT Caenorhabditis elegans reveals new functions in feeding and
RT embryogenesis.";
RL Mol. Biol. Cell 13:1329-1337(2002).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15498499; DOI=10.1016/j.cub.2004.10.001;
RA Thomas-Virnig C.L., Sims P.A., Simske J.S., Hardin J.;
RT "The inositol 1,4,5-trisphosphate receptor regulates epidermal cell
RT migration in Caenorhabditis elegans.";
RL Curr. Biol. 14:1882-1887(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF CYS-1571.
RX PubMed=15013747; DOI=10.1016/s0014-5793(04)00107-3;
RA Jee C., Lee J., Lee J.I., Lee W.H., Park B.J., Yu J.R., Park E., Kim E.,
RA Ahnn J.;
RT "SHN-1, a Shank homologue in C. elegans, affects defecation rhythm via the
RT inositol-1,4,5-trisphosphate receptor.";
RL FEBS Lett. 561:29-36(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH IRI-1.
RX PubMed=15133127; DOI=10.1091/mbc.e04-01-0039;
RA Walker D.S., Ly S., Gower N.J., Baylis H.A.;
RT "IRI-1, a LIN-15B homologue, interacts with inositol-1,4,5-triphosphate
RT receptors and regulates gonadogenesis, defecation, and pharyngeal pumping
RT in Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:3073-3082(2004).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-945 AND CYS-1571.
RX PubMed=15194811; DOI=10.1091/mbc.e04-03-0198;
RA Yin X., Gower N.J., Baylis H.A., Strange K.;
RT "Inositol 1,4,5-trisphosphate signaling regulates rhythmic contractile
RT activity of myoepithelial sheath cells in Caenorhabditis elegans.";
RL Mol. Biol. Cell 15:3938-3949(2004).
RN [13]
RP FUNCTION.
RX PubMed=16267094; DOI=10.1242/dev.02083;
RA Corrigan C., Subramanian R., Miller M.A.;
RT "Eph and NMDA receptors control Ca2+/calmodulin-dependent protein kinase II
RT activation during C. elegans oocyte meiotic maturation.";
RL Development 132:5225-5237(2005).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ARG-557; LEU-945 AND CYS-1571.
RX PubMed=16186564; DOI=10.1085/jgp.200509355;
RA Espelt M.V., Estevez A.Y., Yin X., Strange K.;
RT "Oscillatory Ca2+ signaling in the isolated Caenorhabditis elegans
RT intestine: role of the inositol-1,4,5-trisphosphate receptor and
RT phospholipases C beta and gamma.";
RL J. Gen. Physiol. 126:379-392(2005).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-1571.
RX PubMed=15958491; DOI=10.1091/mbc.e05-02-0096;
RA Gower N.J., Walker D.S., Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signaling regulates mating behavior in
RT Caenorhabditis elegans males.";
RL Mol. Biol. Cell 16:3978-3986(2005).
RN [16]
RP FUNCTION.
RX PubMed=18369461; DOI=10.1371/journal.pgen.1000043;
RA Vazquez-Manrique R.P., Nagy A.I., Legg J.C., Bales O.A., Ly S.,
RA Baylis H.A.;
RT "Phospholipase C-epsilon regulates epidermal morphogenesis in
RT Caenorhabditis elegans.";
RL PLoS Genet. 4:E1000043-E1000043(2008).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-1571.
RX PubMed=19730689; DOI=10.1371/journal.pgen.1000636;
RA Walker D.S., Vazquez-Manrique R.P., Gower N.J., Gregory E., Schafer W.R.,
RA Baylis H.A.;
RT "Inositol 1,4,5-trisphosphate signalling regulates the avoidance response
RT to nose touch in Caenorhabditis elegans.";
RL PLoS Genet. 5:E1000636-E1000636(2009).
RN [18]
RP FUNCTION.
RX PubMed=21191812; DOI=10.1007/s10059-011-0007-9;
RA Oh W.C., Song H.O., Cho J.H., Park B.J.;
RT "ANK repeat-domain of SHN-1 is indispensable for in vivo SHN-1 function in
RT C. elegans.";
RL Mol. Cells 31:79-84(2011).
RN [19]
RP FUNCTION.
RX PubMed=23671426; DOI=10.1371/journal.pgen.1003510;
RA Kovacevic I., Orozco J.M., Cram E.J.;
RT "Filamin and phospholipase C-epsilon are required for calcium signaling in
RT the Caenorhabditis elegans spermatheca.";
RL PLoS Genet. 9:E1003510-E1003510(2013).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF ARG-557 AND CYS-1571.
RX PubMed=32905769; DOI=10.1016/j.celrep.2020.108125;
RA Burkewitz K., Feng G., Dutta S., Kelley C.A., Steinbaugh M., Cram E.J.,
RA Mair W.B.;
RT "Atf-6 Regulates Lifespan through ER-Mitochondrial Calcium Homeostasis.";
RL Cell Rep. 32:108125-108125(2020).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that regulates intracellular calcium homeostasis (PubMed:10499793,
CC PubMed:10610772, PubMed:15194811, PubMed:16186564, PubMed:23671426).
CC Binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and
CC inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity and does
CC not discriminate between the phosphate at 1 or 2 position
CC (PubMed:10610772). Can also bind inositol 1,3,4,5-tetrakisphosphate
CC (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with
CC lower affinity (PubMed:10610772). Acts as a timekeeper/rhythm generator
CC via calcium signaling, affecting the defecation cycle and pharyngeal
CC pumping (PubMed:10499793, PubMed:11553721, PubMed:12062062,
CC PubMed:11950942, PubMed:15013747, PubMed:15133127, PubMed:16186564,
CC PubMed:21191812). Affects normal hermaphrodite and male fertility as a
CC participant in intracellular signaling by acting downstream of let-
CC 23/lin-3 which regulates ovulation, spermathecal valve dilation and
CC male mating behavior (PubMed:9491893, PubMed:15194811, PubMed:16267094,
CC PubMed:15958491). Important for early embryonic development; controls
CC epidermal cell migration and may also regulate filopodial protrusive
CC activity during epithelial morphogenesis (PubMed:11950942,
CC PubMed:15498499, PubMed:18369461). Component of inositol trisphosphate
CC (IP3)-mediated downstream signaling pathways that controls amphid
CC sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde
CC but not other ASH-mediated responses (PubMed:19730689). Involved in
CC modulating lifespan, acting downstream of transcription factor atf-6
CC (PubMed:32905769). {ECO:0000269|PubMed:10499793,
CC ECO:0000269|PubMed:10610772, ECO:0000269|PubMed:11553721,
CC ECO:0000269|PubMed:11950942, ECO:0000269|PubMed:12062062,
CC ECO:0000269|PubMed:15013747, ECO:0000269|PubMed:15133127,
CC ECO:0000269|PubMed:15194811, ECO:0000269|PubMed:15498499,
CC ECO:0000269|PubMed:15958491, ECO:0000269|PubMed:16186564,
CC ECO:0000269|PubMed:16267094, ECO:0000269|PubMed:18369461,
CC ECO:0000269|PubMed:19730689, ECO:0000269|PubMed:21191812,
CC ECO:0000269|PubMed:23671426, ECO:0000269|PubMed:9491893}.
CC -!- SUBUNIT: Interacts with myo-1, myo-2, unc-54/myo-4 and nmy-2. Also
CC interacts with iri-1. {ECO:0000269|PubMed:12062062,
CC ECO:0000269|PubMed:15133127}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10610772, ECO:0000269|PubMed:15498499}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P11881,
CC ECO:0000269|PubMed:10610772, ECO:0000269|PubMed:15498499}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=a {ECO:0000269|PubMed:11237590};
CC IsoId=Q9Y0A1-1; Sequence=Displayed;
CC Name=d {ECO:0000269|PubMed:11237590};
CC IsoId=Q9Y0A1-2; Sequence=VSP_053337;
CC Name=e {ECO:0000269|PubMed:10610772, ECO:0000269|PubMed:11237590};
CC IsoId=Q9Y0A1-3; Sequence=VSP_053338, VSP_053339, VSP_053340,
CC VSP_053343, VSP_053344;
CC Name=f {ECO:0000269|PubMed:10610772, ECO:0000269|PubMed:11237590};
CC IsoId=Q9Y0A1-4; Sequence=VSP_053338, VSP_053339;
CC Name=g {ECO:0000305};
CC IsoId=Q9Y0A1-5; Sequence=VSP_053338, VSP_053339, VSP_053342,
CC VSP_053345;
CC Name=h {ECO:0000305};
CC IsoId=Q9Y0A1-6; Sequence=VSP_053338, VSP_053339, VSP_053341;
CC -!- TISSUE SPECIFICITY: Isoform a is expressed in the anterior cells of the
CC pharyngeal terminal bulb, vulva, rectal epithelial cells, spicule
CC protractor muscles of the proctodeum and male-specific neuron CP8 or
CC CP9. Isoform d is expressed in the spermatheca, excretory cell, amphid
CC socket cells, PDA motor neuron, spicule retractor muscles, gubernaculum
CC retractor muscles, posterior oblique muscles, diagonal muscles and the
CC vas deferens. Also expressed in the intestine, pharynx, pharyngeal
CC isthmus, pharyngeal intestinal valve, somatic gonad, hypodermal cells
CC of the vulva, uterine sheath cells, tail, head, LUA motor neuron and
CC the embryonic epidermis (at protein level).
CC {ECO:0000269|PubMed:10499793, ECO:0000269|PubMed:10610772,
CC ECO:0000269|PubMed:11237590, ECO:0000269|PubMed:15498499,
CC ECO:0000269|PubMed:15958491}.
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 {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:10610772,
CC ECO:0000269|PubMed:11950942}.
CC -!- DISRUPTION PHENOTYPE: Disrupted defecation rhythm with reduced
CC pharyngeal pumping in the presence of food resulting in constipation.
CC Disrupted reversal/avoidance response to nose touch. Hermaphrodites
CC display endomitotic oocytes following spermathecal dilation defect and
CC defective ovulation. Loss of male fertility due to defects in turning
CC behavior, spicule insertion and sperm transfer.
CC {ECO:0000269|PubMed:11950942, ECO:0000269|PubMed:15194811,
CC ECO:0000269|PubMed:15958491, ECO:0000269|PubMed:19730689}.
CC -!- MISCELLANEOUS: [Isoform a]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:11237590}.
CC -!- MISCELLANEOUS: [Isoform d]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:11237590}.
CC -!- MISCELLANEOUS: [Isoform e]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000269|PubMed:10610772,
CC ECO:0000269|PubMed:11237590}.
CC -!- MISCELLANEOUS: [Isoform f]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000269|PubMed:10610772,
CC ECO:0000269|PubMed:11237590}.
CC -!- MISCELLANEOUS: [Isoform g]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform h]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000255}.
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DR EMBL; AF168688; AAF05302.1; -; mRNA.
DR EMBL; AJ243179; CAB45860.1; -; mRNA.
DR EMBL; AJ243180; CAB45861.1; -; mRNA.
DR EMBL; AJ243181; CAB45862.1; -; mRNA.
DR EMBL; AJ243182; CAB45863.1; -; mRNA.
DR EMBL; FO080445; CCD63763.1; -; Genomic_DNA.
DR EMBL; FO080445; CCD63764.1; -; Genomic_DNA.
DR EMBL; FO080445; CCD63765.1; -; Genomic_DNA.
DR EMBL; FO080445; CCD63766.1; -; Genomic_DNA.
DR EMBL; FO080445; CCD63767.1; -; Genomic_DNA.
DR EMBL; FO080445; CCD63775.1; -; Genomic_DNA.
DR RefSeq; NP_001023170.1; NM_001027999.3. [Q9Y0A1-1]
DR RefSeq; NP_001023171.1; NM_001028000.3. [Q9Y0A1-2]
DR RefSeq; NP_001023172.1; NM_001028001.2. [Q9Y0A1-3]
DR RefSeq; NP_001023173.1; NM_001028002.2. [Q9Y0A1-4]
DR RefSeq; NP_001023174.1; NM_001028003.2.
DR RefSeq; NP_001255305.1; NM_001268376.1. [Q9Y0A1-6]
DR SMR; Q9Y0A1; -.
DR BioGRID; 42664; 21.
DR STRING; 6239.F33D4.2a; -.
DR TCDB; 1.A.3.2.16; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
DR EPD; Q9Y0A1; -.
DR PaxDb; Q9Y0A1; -.
DR PeptideAtlas; Q9Y0A1; -.
DR PRIDE; Q9Y0A1; -.
DR EnsemblMetazoa; F33D4.2a.1; F33D4.2a.1; WBGene00002173. [Q9Y0A1-1]
DR EnsemblMetazoa; F33D4.2d.1; F33D4.2d.1; WBGene00002173. [Q9Y0A1-2]
DR EnsemblMetazoa; F33D4.2e.1; F33D4.2e.1; WBGene00002173. [Q9Y0A1-3]
DR EnsemblMetazoa; F33D4.2f.1; F33D4.2f.1; WBGene00002173. [Q9Y0A1-4]
DR EnsemblMetazoa; F33D4.2g.1; F33D4.2g.1; WBGene00002173. [Q9Y0A1-5]
DR EnsemblMetazoa; F33D4.2h.1; F33D4.2h.1; WBGene00002173. [Q9Y0A1-6]
DR GeneID; 177546; -.
DR KEGG; cel:CELE_F33D4.2; -.
DR UCSC; F33D4.2a.2; c. elegans.
DR CTD; 177546; -.
DR WormBase; F33D4.2a; CE37905; WBGene00002173; itr-1. [Q9Y0A1-1]
DR WormBase; F33D4.2d; CE37906; WBGene00002173; itr-1. [Q9Y0A1-2]
DR WormBase; F33D4.2e; CE28017; WBGene00002173; itr-1. [Q9Y0A1-3]
DR WormBase; F33D4.2f; CE28018; WBGene00002173; itr-1. [Q9Y0A1-4]
DR WormBase; F33D4.2g; CE31690; WBGene00002173; itr-1. [Q9Y0A1-5]
DR WormBase; F33D4.2h; CE44684; WBGene00002173; itr-1. [Q9Y0A1-6]
DR eggNOG; KOG3533; Eukaryota.
DR GeneTree; ENSGT00940000167397; -.
DR InParanoid; Q9Y0A1; -.
DR OMA; GLIDKTW; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; Q9Y0A1; -.
DR Reactome; R-CEL-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-CEL-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-CEL-5578775; Ion homeostasis.
DR Reactome; R-CEL-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-CEL-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:Q9Y0A1; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002173; Expressed in larva and 3 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
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; IDA:WormBase.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:WormBase.
DR GO; GO:0017022; F:myosin binding; IPI:WormBase.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0048815; P:hermaphrodite genitalia morphogenesis; IGI:UniProtKB.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IMP:WormBase.
DR GO; GO:0060179; P:male mating behavior; IMP:WormBase.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IGI:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0001556; P:oocyte maturation; IGI:WormBase.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:WormBase.
DR GO; GO:1903746; P:positive regulation of pharyngeal pumping; IPI:WormBase.
DR GO; GO:0012501; P:programmed cell death; IGI:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0007622; P:rhythmic behavior; IMP:WormBase.
DR GO; GO:0042713; P:sperm ejaculation; IMP:WormBase.
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; IPR035910; RyR/IP3R_RIH_dom_sf.
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; 3.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 4.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Developmental protein;
KW Endoplasmic reticulum; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2892
FT /note="Inositol 1,4,5-trisphosphate receptor itr-1"
FT /id="PRO_0000424150"
FT TOPO_DOM 1..2475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2476..2496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2497..2514
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2515..2535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2536..2572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2573..2593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2594..2615
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2616..2636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2637..2735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2736..2756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2757..2892
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 192..246
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 319..379
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 386..466
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 490..551
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1030..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2655..2685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357..361
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250|UniProtKB:P11881"
FT BINDING 625..628
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000269|PubMed:10610772"
FT BINDING 689..691
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250|UniProtKB:P11881"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:10610772"
FT /id="VSP_053337"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform e, isoform f, isoform g and
FT isoform h)"
FT /evidence="ECO:0000303|PubMed:10499793,
FT ECO:0000303|PubMed:10610772"
FT /id="VSP_053338"
FT VAR_SEQ 47..61
FT /note="FDFDDFEEQIMRKSS -> MDYDYRRRVLERNIG (in isoform e,
FT isoform f, isoform g and isoform h)"
FT /evidence="ECO:0000303|PubMed:10499793,
FT ECO:0000303|PubMed:10610772"
FT /id="VSP_053339"
FT VAR_SEQ 423..430
FT /note="RASLIYSK -> PPLLSALSQKSRPMLER (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10610772"
FT /id="VSP_053340"
FT VAR_SEQ 1730
FT /note="K -> KMSQDSQSDYDSDSSQGPCQIS (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_053341"
FT VAR_SEQ 1731..1759
FT /note="RLNRQNTLNPGHRLYGTSNSMTEHTSANV -> PVITLVVETQSSKYAQSWS
FT STLWNIKLYD (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_053342"
FT VAR_SEQ 1760..2892
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_053345"
FT VAR_SEQ 1853
FT /note="G -> GHRVYNSSVEKG (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10610772"
FT /id="VSP_053343"
FT VAR_SEQ 1998..2006
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10610772"
FT /id="VSP_053344"
FT MUTAGEN 103
FT /note="G->E: In n2559; slow developmental rate to
FT adulthood, absence of ovulation, sterility, absence of
FT defecation cycle and intestinal calcium oscillations."
FT /evidence="ECO:0000269|PubMed:10499793"
FT MUTAGEN 371
FT /note="R->K: In sy331; reduced fertility and brood size."
FT /evidence="ECO:0000269|PubMed:11553721,
FT ECO:0000269|PubMed:9491893"
FT MUTAGEN 557
FT /note="R->C: In sy290; gain of function. 2-fold increase in
FT ligand affinity. Increased velocity of posterior-to-
FT anterior calcium wave. Reduced fertility, hyperactive
FT spermathecal dilation leading to decreased brood size.
FT Extended lifespan."
FT /evidence="ECO:0000269|PubMed:11950942,
FT ECO:0000269|PubMed:16186564, ECO:0000269|PubMed:32905769,
FT ECO:0000269|PubMed:9491893"
FT MUTAGEN 625
FT /note="K->Q: Abolishes ligand binding; when associated with
FT Q-628."
FT /evidence="ECO:0000269|PubMed:11950942"
FT MUTAGEN 628
FT /note="R->Q: Abolishes ligand binding; when associated with
FT Q-625."
FT /evidence="ECO:0000269|PubMed:11950942"
FT MUTAGEN 900
FT /note="S->F: In sy328; reduced fertility and brood size."
FT /evidence="ECO:0000269|PubMed:11553721,
FT ECO:0000269|PubMed:9491893"
FT MUTAGEN 945
FT /note="L->F: In sy327; gain of function. Increased velocity
FT of posterior-to-anterior calcium wave and enhanced sheath
FT contractile activity."
FT /evidence="ECO:0000269|PubMed:15194811,
FT ECO:0000269|PubMed:16186564"
FT MUTAGEN 1571
FT /note="C->Y: In sa73; slow developmental rate to adulthood,
FT reduced brood size, slow intestinal calcium oscillations,
FT slower pharyngeal pumping, longer defecation cycle,
FT defective ovulation, reduced myoepithelial sheath
FT contractility and reduced efficiency of sperm transfer.
FT Causes gross mitochondrial morphological changes,
FT consistent with enhanced mitochondrial fusion. Elevated
FT levels of phosphorylation of AMP-activated protein kinase.
FT At semi-permissive temperature of 20 degrees Celsius,
FT suppresses longevity in an atf-6 mutant background."
FT /evidence="ECO:0000269|PubMed:10499793,
FT ECO:0000269|PubMed:11553721, ECO:0000269|PubMed:11950942,
FT ECO:0000269|PubMed:15013747, ECO:0000269|PubMed:15194811,
FT ECO:0000269|PubMed:15958491, ECO:0000269|PubMed:16186564,
FT ECO:0000269|PubMed:19730689, ECO:0000269|PubMed:32905769"
SQ SEQUENCE 2892 AA; 330837 MW; B1C598FE554B83CF CRC64;
MNPSYGRVRK KVSIISIPEF VPEHYEYENE TTASGGASGG GSTRIEFDFD DFEEQIMRKS
SMALPSRKLT IANSIDHGNN GNLHIGDIIS LYTESSSNQE QRGFLSTLGL VDDRCIVELK
DGRPESPPKK FRDCLFKVCP VNRYAAQKHL WTEQKRFQTG DSMFDDDLMN KLKVAADKER
EENESEFQKT LGNVIQYGSM VQLLHVKSNK YITVQKNSPA KRERNAMKVY LDRAGNEGSW
FIIEPAYKHY AIGDNVSAGN KISLIPNSVS TTQAGHVKSQ LHLSSFNLLD HQSAAEVNCL
NEPTEWQVFM FLLFDENQQN SVKSGDVVRL FHADQQTFLT LDTIPKQNPP TDVVFLRMTN
RPSAADATSS RALWEVQVVQ TNAYRGGTAK WNKAYRFKHL ATDMYLSAEP SQVQVKPAMN
GRRASLIYSK TNNPMAMYSD GPNGVTNEST DTTQQNIPSV WVLGPTKSEF PEEDANLLFQ
LDPSTFMKSN KEVPRRSYVR LLHQSSDKWV HATNATEKQN LHYSSKNEKG WVKVICEKNR
VDKETFALLP VNPDEVRDLD FANDACKALR NFIKLIKIGQ VISKESINST TQLLIDCILF
VTNSSDHLAD PLKISDFSPS RDRQKLLREQ EVLNQVFLLL KAPFLPRQGT TELGPLLSSP
SELSDSRNEI FKTMFQLCYC LLKYSQVSYR KNQEFLAEKF GEIQEQIGFD LMAEDTMTAV
LHNNPKLLEK YVKTPHVERF VELVRNNRQG KFLDYLADLC VCRGEANKKI QELICTSVLS
SKHRDIFMDT KIIDGEIEVG WAPNFRKLVD IAEGAKSNSD DAEHLDYYRH QLDLLSQMCQ
EQQYLAIDPP PERRLMNISQ QLPAELVLQC MSDNRLPYDL RGSFTRLMLH LHVVRGSPMS
AIRHARLWWS IPENVNVSTY ESVSVEAYSD GSRMRIGEGI AHKVLATVET YLMGLRNQSM
EERQSVNSSK LTYEIVNLAK ALAQFNFYSF NDLLQLTQNL LAIINEGPAT EQVPSHRAMV
NAIRNMSKSM MRGGNKENSK DLAKTPSVTA EEAGRTKEGR ALNVKTKLIV AEILQFVMDV
RRDYRITMAL SWFKNVFPCD EDGSLMHSAS INERMASELY DAIYRSSGHE LHLDGRDGQL
LLAILLQMTM SDYPPLTSIA LKVFFRHFTQ YQELLEDLKQ VQLLVSNNDV ENYRQIDRDL
FILKNLTEKS ELWVHGDRHH SIDTKEVDEK ERTTEHDLLD HDLKSPRAFD SGDSMEALMA
VLNEHYPSIR NECLQLLNRL LIKDDRNDAA VALQELSDKA PLIAYPLIRQ MLVRLTGMCY
RKGDPKPDTM NQQLLKNMRV YEVVLEFISV PHDKKHDHDM MKLITLSHEF LRSFCKTNKE
NQSRLYKFIS YEKDAKEGML RVETIEEVGT LVAIFRNNRE LASNVPEELI AHIVGLIEHN
SRNPIFLELL QALVCVYDKE IESGQEKVAN EICAASDEVR QLYVDNASFE ELEAMMKDEK
ESKGRSSDSR RKLKYHIELV RLLAMCTRGK NGNTELKCAS QIPMDHIVRV VTAKQCLVEV
KTVYLQLLLH CYIDTDAEMK DAYKTEYVDH ILNNLLEDIR SLRVEKLTGA ETATLEHYIC
HTVTEVLIKF FEAPYSALQQ AKVDVHHHKK TFSEVLLELT YLEKGKLRGS KSSRNWYRVA
ECIKRLTKWA EEHNITLPAT LAGPQMSGQT SVRQKWQQAA SSAKWIGIGK RLNRQNTLNP
GHRLYGTSNS MTEHTSANVV TCYHMMIGEF KFYLHPLHAA EGSVLVEVLH TPELLFPEGS
ALRDQCARGG VVAKLIQHCK TLMQNKQDNL CARVLQTLCK MCDCTKQQLT HQGQQLRQLL
LQRYFGHHNN HHPPLDRQQS KIGEVIEAVK EKKEETWSQE RDLYAIQCKL NDAGASDLVT
DIIIMEPSRE IFLKAIHLAR ALLHEGNDKV QHSFYMRMKQ KDIHEPFFKA ILTRIQTAQN
RLKSDMMSCS DSKPKVSLSA TVSRRSSTVL TPLIDAGDTG FNGALFEVPQ QVRHPSISEM
SQLSNDLTHS IPDLAPYQDE EKSTDALPPE VALVEPILRV LQLLCENHNS LLQNFLRKQS
DRTNHNLVSE TLSFLDTVCG STKGSLGVFG EIGEHNFSLI TQTLATLTEF CQGPCHENQN
TMAMQENGLN IIISLVLNEI KPLADDHMEL ALEIKSQASK LLLAIMESRH DGENANRVLR
NMANMSGGPK QLVHAIKQAY EMTNSNHHML KSISRDLFRQ AEDDLKKKSG PQITVNTVTL
PEINVDASGI VSIHTEKNIS SSLDDKFNDD DIPSVDPREV GHNIYILAHQ LAIHDGELEI
WLDGSDEKKD DLTREALNYY KERTAQIEIV RRDRTLERVV FPINDICSYL TKDTKDYVYN
NTERDNQGSK VTEFFDEWET MYHEMIWQRK LQDRKWLSWC AFRLPLWTRL SFHFAFIVNA
LVARYYPLPE HSNSSISLGN LYSWFAVFSS FLLAHYLRHD KIYLHKTSLL ILASLCFLLL
SSIGVTLTLY IFGILQLVNK IVHVVAFVSN KGLEDRPIAE ILACRNLHYL LVYLFICILG
LLVHPMIYCI LLFDIIFTEE TLQNVIASVT RNYQSIVWTG LLALILLYFF SILGFLYFRH
DFYLEVDPVE NDSSATISSG IPSETCPSEG CPGLQPSEKD DNDDEKKVKS CETLWMCILQ
TGYQGLRNGG GIGDVLRNPA PWEDMFIWRV AYDMTFFVVL IVIVLNLIFG VIIDTFGDLR
AEKNEKEQIL KNNCFICGLD RSRFDNRSVT FETHRETEHN IWHYLYYIVM LQIKDETEFT
GPESYVAQCV KDRNLDWFPR MQALSLQDSE LDTDQSEVKQ MKDQLLQMMT LMREIISQNE
ESRAFMEQFQ PR
