ID A0A1I8IAB8_9PLAT Unreviewed; 1814 AA.
AC A0A1I8IAB8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0011226-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0011226-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium.
CC {ECO:0000256|RuleBase:RU368044}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU368044}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU368044}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU368044}.
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:0000256|RuleBase:RU368044}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family.
CC {ECO:0000256|RuleBase:RU368044}.
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DR WBParaSite; maker-uti_cns_0011226-snap-gene-0.2-mRNA-1; maker-uti_cns_0011226-snap-gene-0.2-mRNA-1; maker-uti_cns_0011226-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:UniProtKB-UniRule.
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; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR015925; Ryanodine_IP3_receptor.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR PANTHER; PTHR13715:SF100; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; 1.
DR PANTHER; PTHR13715; RYANODINE RECEPTOR AND IP3 RECEPTOR; 1.
DR Pfam; PF08709; Ins145_P3_rec; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR PRINTS; PR00779; INSP3RECEPTR.
DR SMART; SM00472; MIR; 2.
DR SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 1.
DR SUPFAM; SSF82109; MIR domain; 2.
DR PROSITE; PS50919; MIR; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU368044};
KW Calcium channel {ECO:0000256|RuleBase:RU368044};
KW Calcium transport {ECO:0000256|RuleBase:RU368044};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU368044};
KW Ion channel {ECO:0000256|RuleBase:RU368044};
KW Ion transport {ECO:0000256|RuleBase:RU368044};
KW Ligand-gated ion channel {ECO:0000256|RuleBase:RU368044};
KW Membrane {ECO:0000256|RuleBase:RU368044};
KW Receptor {ECO:0000256|RuleBase:RU368044};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|RuleBase:RU368044}.
FT DOMAIN 9..63
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1767..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1814 AA; 207988 MW; D4C2A2349691B5FD CRC64;
MAEQRRNLGK RVRYGEIVQL KHVFTGKYVH VNTNHTSQHD KNNMLLSLHE YNSKNAQFRI
LPRYKVKSEG EHVQLLDQIS LESIKSPGHY FHSSKGFKIG PESRPTFVSE LNLGVEQTGF
TIIKSHGFSG DHEAYARGGQ FVQLFHKELE AYVVAEGLFD QDVTEDVHLR IREIDQLNPR
TLHSSTSAVT YWQVEPESTV LDGEVLTWDQ QFRFRHATTR KYLCVKQASE AYSVTLTEDA
TDPHTVFKMH PVLQDSPELK FESYARIEHV ITGCWLHAIK GVELNDFFNF FDWSEFNKSY
QRKEFLNMED EKSMRALRWD GGELREITCC FDRRYDDAYT IQKVDSEHVM NFNFVAGVVP
TLQDLIDARQ IGRPLTSKET FRICHALREL RNFMLVNGEP CKARQKLLRN LRVIDLLVTL
LKFPLKAVQD EHNLTKVFSE AYDILHTYMM GNSRKNALYF AKYIEFFQTQ MVDKSELALK
VTKMLVELMK DNRKIVDRIS NAQIEVFVEL LRKNEHHSYL ELLKVLCVCN GVAITENQNF
IAQKWLLEDT RGVYMTNRGQ NIDRKPNETY VSYDQQHSWL PLVDFVQPDE YDTEAVERCL
FLHTQLDLFI ALCHGRNEDC IRLITKDLSY LTWEEAYLGL SSESLPHEFR AKYCEIIIGL
FVNVGNNYSV VESPQLCFIY EYIGTKDFTY QTSSPEQYKQ GRKVGEPSRL EQQRAAKDLV
TIFPVIRDWI AEFLDQNRMM VASQVANNIL IEQVLKLLHY LVKFGYYGEV HDLARLLPAL
RNLLDGQNDI PFPPDRMPAR EFSKERKKAV LRFKQTERFR RSPETQAIVR AKHAALQVLD
LVMTFQENAR LASFIKKFKD SEISEVATRR KHIHPLVPAL YDSFDPFDTR KSALQVQKRM
KKELRIMFEE SSRHVDNIAL TSILIDLAHY EYDPMVQLSL QLLNKLHSAK SSMFNLAVNS
LVLITPDSCR VHREVGKQVP LLKMMIRSKW TSDQAVKIET ILSELRELCH LPKAEEEPHP
MNQRLMLSHN VLGVVFDILS TETDVQLTEK YHETVGVLRK AVRLMKALTI RYEDVQNQVF
NNLDSMLRVR LVEPDLALAL KEVFVNNQEL CLKILPRQIS RIVGLVAENQ ERAPEFLELL
SAIVKVEGPG LALKRNQTLV MKYIMQNYSK VGYVLEQCTT KDRMEVLNGN RGASHCQYLI
SLVDLLATCA EGENRYIESL CQTIISVEEI LCILNDPNVE NHLKKPFLRY MFYAYMKTSG
STAENRSPDI IQDRLVWEYV RHLTLEFDGL TRWIRNDAAR DTVYFMSMRP FPKILRLHDA
CPLCSTLVAE DETQPLKLNL ENAVVRMRED DFRGHASLHY VFDAVLPFLQ AFANKFYQTE
EDKDTQSERD MFDRLTLSAI GLCSELAAIV VEPRILTQMV ACLSALVRKS SHRPTIMEPV
VENIGKGTKL QDTVSQMKSG NKEYYEQEII LNSKLKTLAV NMSLLWGGQN TVRAQLKYSS
DREYTVIGGE ESLPLDEEFQ DHVRCFISAG SRKPEGRYRL AGLLVNGLRI TAVSSTASAS
HAAAAAADPG AGGRGDTERL AIRILQILRA FIHNEERKLP EDWEVRMSEF RVKRGLKNIA
EIQNTLNSFD LMKHALPHLA STSGLVAKEV LSLLGIMLFN ANEKVQQSML KYFLNTKEEV
FFFAVRNRLQ VSTANIKEKR LLISQQKARQ MDARSQADDL KATMTLGVKA LQQIQQYHVE
MKIEQANSDL TRRVSLTQMQ SASITKKKSG VGGVASGSNG GSNGGTAAAA ARQLLVGKSP
LLTASKVGRT PLTA
//
