ITPR_PATPE
ID ITPR_PATPE Reviewed; 2698 AA.
AC Q8WSR4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000312|EMBL:BAB84088.1};
DE Short=ApIP3R {ECO:0000312|EMBL:BAB84088.1};
GN Name=IP3R {ECO:0000303|PubMed:11687583};
OS Patiria pectinifera (Starfish) (Asterina pectinifera).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=7594;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB84088.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000269|PubMed:11687583};
RX PubMed=11687583; DOI=10.1074/jbc.m108839200;
RA Iwasaki H., Chiba K., Uchiyama T., Yoshikawa F., Suzuki F., Ikeda M.,
RA Furuichi T., Mikoshiba K.;
RT "Molecular characterization of the starfish inositol 1,4,5-trisphosphate
RT receptor and its role during oocyte maturation and fertilization.";
RL J. Biol. Chem. 277:2763-2772(2002).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium (By similarity).
CC Involved in the induction of intracellular calcium increase in eggs
CC during fertilization and in the formation of the fertilization envelope
CC during oocyte maturation. {ECO:0000250|UniProtKB:Q9Z329,
CC ECO:0000269|PubMed:11687583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11687583}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P11881}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P11881}. Note=In immature
CC oocytes, distributed throughout the cytoplasm but not in the germinal
CC vesicle (GV). During GV disintegration, expression is concentrated at
CC the site where the GV was previously located. Following GV breakdown,
CC expressed evenly throughout the egg cytoplasm.
CC {ECO:0000250|UniProtKB:P11881, ECO:0000269|PubMed:11687583}.
CC -!- DEVELOPMENTAL STAGE: Expressed during oocyte maturation with levels
CC remaining constant throughout this period (at protein level).
CC {ECO:0000269|PubMed:11687583}.
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}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000255}.
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DR EMBL; AB071372; BAB84088.1; -; mRNA.
DR AlphaFoldDB; Q8WSR4; -.
DR SMR; Q8WSR4; -.
DR PRIDE; Q8WSR4; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IEA:InterPro.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
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; 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; 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 Calcium; Calcium channel; Calcium transport; Cytoplasm;
KW Developmental protein; Endoplasmic reticulum; Fertilization; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2698
FT /note="Inositol 1,4,5-trisphosphate receptor"
FT /id="PRO_0000415412"
FT TOPO_DOM 1..2218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2219..2239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2240..2245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2246..2266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2267..2307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2308..2328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2329..2336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2337..2357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2358..2383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2384..2404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2405..2520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2521..2541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2542..2698
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 230..286
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 293..359
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 365..421
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1116..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2675..2698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264..268
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 493..496
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 552..554
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2698 AA; 307591 MW; 32DB6EE508328B04 CRC64;
MSEMSASFLH FGDIVSLYAE GSVNGFISTL GLVDDRCVVQ PDFGDLNNPP KKFRDCLFKI
CPMNRYTAQK QFWKSAKPNV SSATDAVLLK KLQHAAEMEK KQNETENKKL MGSVIVYGNV
IQLLHIKSHK YMTVNKRLPA LLEKNAMRVT LDSSATEGSW FYIVPFYKLR SAGDNVVVGD
KVVLNPVNAG QPLHPSNYEL IDNPGCKEVN SVNCNTCWKV SLFMEHKENL DGLKGGDVVR
LFHAEQEKFL TCDEYKKKSY IFLRTTGRVS ATAATSSKAL WETEVVQHDP CRGGAGHWNS
LFRFKHLATG QYMAAEVDND NTKDHTREKL RGPHGGTVYQ MVPIIHGNDI ASIFELDPTT
LQGGDSMVPR SSYVRLRHLC TNTWVHSTSI PLDKGEDKPV MLKVGTAQIR EDREAFAIIP
VSPTEVRDLD FANDANKVLS AIASKLEKSS ITQNERFVTQ LLTDLVYFVS ILPNNGGDAL
NVVVQNPDRD RQKLMREQDI LKQIFKILKA PFTDNGDGAM LKMEELADPR HAPYRHICRL
CYRILRLSQQ AYRKNQEYIA KQFGFMQKQI GYDVLAEDTI TALLHNNRKL LEKHITATEI
ETFVNLVRKN GECRFLEYLS DLCVSNNQAI PVTQELICKS VLVERNSDIL IETKLVRTQM
EVEMEVEADD GTTEPVYTIE EEEEVVLFWK NGTKSKSIRS CHGGTENVKE DANVLKYYRY
QLDLFSQMCL DRQYLAINQI GPQLDIDLIH RCMSDESLPY DLRASFTRLM LHMHVDRDPK
EQVTPVKYAE LWSEIPTQIT IDDYDGANNL THAGKEDAQP KFSLTIKFVE EYLCNVVSGV
LVVYDKEQNK LTFEVVNLAK HLIYFGFYSF SELLRLTKTL LSILDCTALH GTAPGKLDPK
ADIGKGGVFR SIHGVGAVMT NMVLGKRLPT PVTRDPAWPL GWGLDNHNKQ DELVMETKLK
IIQILQFILN VRLDYRISCL LSIFKRDFDE SKDSTDEITT SGKVWTASDF EHIEEQAEGI
FGGSEENTPL DLDDDDGGRT FLRVLIHLTM HDYAPLVSGA LQLLFKHFSQ RQEVLEAFKQ
LQLLVSSQDV DNYKQIKQDL DQLRLVEKSE LWVYKGQGPD EPMDGASGEQ EHKKTEEGTS
KPLKHESTSS YNYRVVKEIL LRLSKLVCVE GNGTRKNRKH EQRLLRNMGA FTVVLELLQI
PYEKNHDTRM NELMRLAHEF LQNFCWANPS NQVLLHKHID LFLTPGLLEA QTMCHIFMNN
FQLCSEVTEQ VVQHFVHCIA THGRHVQYLK FLQAIVKADG QYIRKTQDMV MAELVNAGED
VLLFYNDKAS FQMFINMMRT ERERMDASSP SQYRHQPWTL LGLACTEGKN VYTEIKCHSL
LPLDDIVRVA THEDCLPEVK NAYINFLNHC YVDTEVEMKE IYTSNHVWNL FENFLVDMAM
VCNATHDRKH HDHMLEKTVT ETVMNIITMF FSSPFADQST TVQTRQPVFV RLLQGAFRVS
QCDWLTGHQK YHVENCIKTL TDIAKNRGIA IPVDLDSQVN TLFSKSIVMK HTRHWLAINP
NRSRDSMVAI SRDYRSIIEG LQDIVSLLED QLRPLVQAEL SVLVDVLHRP ELLFPFRHRA
RQKCESGAFI SKLIKHTEKL LEEKEEKLCI KVLQTLKEMM TVDIDYSEKG EDLRQCLLLR
YYGKSHLRMK HRGVVASGRG QTNVTSCGPG SRVLSRAEMT LAEVQCQLDK EGASSLVIDL
VIKNSSNRVF LESVELGIAL LEGGNTNIQK SIINCLMSDK NSEKFFKVFF DRMREASEIK
ATVTVNTGEG IGQTKPTEGR NGQHLRRRLT WPHEKGWTRP QRLNQRRAED QLLADAALHT
SKASRQSARV ATTTLLASCQ VLAGGAEKAK EEEKMSMEIA IMQPILRFLQ LLCENHNREL
QSYLRHQNNK TNYNLVCETL QFLDCICGST TGGLGLLGLY INENNVALIN QTLESLTEYC
QGACHENQNA IANHESNGLD IITALILNDI NPLGKNRMDL VLELKNNASK LLLAIMESRH
DSENAERILL NMSPKQLVDV IKQAYQQEDL ERDDDDELII EEDDEAISPR EVGHNIYILA
HQLAHHNKEL AALLKPTGPN SEYTDRALEY YFKHTAQIEI VRQDRTMEQI VFPVPQLCEY
LTAETKIKVF TKAERDDQGS KVADFFEKTE DMFMEMKWQK KLRAQPILFL ASSNMSKWSL
VCFNLAVIVN LLVAFFYPFD VTTTELDHGL SMLVWLMAAS LAAIVTLRRP SGIRPLVFAT
ILRMLIFSIG VEPTLLFLAV LTIFNKCIFI LSFLGNCGLL YKGVRGIFTD MEVLYHILYL
IICFLGLFVH EFFYSLLLLD VVYQEDTLIN VIHSVTRNWR SIAFTALLAL ILVYLFSIVG
YLFLQDDFVY EVNPLRPAIA TATATNKTGT SPPMPLPPES CPAGLEMEDC LKNNLSHVQA
KEVSYDSGIE VGTERERACE TLIMYIITTL NFGVRSGGGI GDVLRSPSTR EPLYMARVIY
DLLFFIVVII IVLNLIFGVI IDTFADLRSE KQQKEEILKN TCFICGLNRS SFDNKSVSFE
EHYKEEHSMW HYLYFIVLVK VKDPTEFTGP ESYVYNMTKE KNQDWFPRMR AMSLDSDEGE
SEQNEMRILQ NQLENTNSLV KVLSGQLREL KDQMTEQRKQ KQRINLLSSP SIPQMGGP
