ID A0A1S3EPM0_DIPOR Unreviewed; 2747 AA.
AC A0A1S3EPM0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
GN Name=Itpr1 {ECO:0000313|RefSeq:XP_012865910.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012865910.1};
RN [1] {ECO:0000313|RefSeq:XP_012865910.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012865910.1};
RG RefSeq;
RL Submitted (NOV-2023) 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|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368044}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368044}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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|ARBA:ARBA00009453, ECO:0000256|RuleBase:RU368044}.
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DR RefSeq; XP_012865910.1; XM_013010456.1.
DR STRING; 10020.ENSDORP00000025044; -.
DR GeneID; 105981338; -.
DR KEGG; dord:105981338; -.
DR CTD; 3708; -.
DR InParanoid; A0A1S3EPM0; -.
DR OrthoDB; 5480299at2759; -.
DR Proteomes; UP000081671; 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; 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; 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_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; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 2.
DR SUPFAM; SSF82109; MIR domain; 2.
DR PROSITE; PS50919; MIR; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU368044};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU368044};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU368044};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368044};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU368044};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU368044};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW ECO:0000256|RuleBase:RU368044};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368044};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU368044};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368044};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368044};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368044}.
FT TRANSMEM 2271..2293
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2305..2323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2392..2417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2437..2459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2568..2591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT DOMAIN 112..166
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 231..287
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 379..435
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1014..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2718..2747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2747 AA; 312785 MW; D21C0300C68EDBFE 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 DFEEECLEFP 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 STGENALEAG EDEEEVWLFW RDSDKEIRSK SVRELAQDAK
EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGASKDEIK ERFAQTMEFV
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
TTIFPITKIV KGEENKGNND EEKLKSSNVM RSIHGVGELM TQVVLRGGGF LPMTPMAAAP
EGNVKQAEPE KEDIMVMDTK LKIIEILQFI LNVRLDYRIS CLLCIFKREF DESNSQTSET
SSGNSSQEGP SSVPGALDFE HIEEQAEGIF GGSEENTPLD LDDHGGRTFL RVLLHLTMHD
YPPLVSGALQ LLFRHFSQRQ EVLQAFKQVQ LLVTSQDVDN YKQIKQDLDQ LRSIVEKSEL
WVYKGQGPDE PMEGASGENE HKKAEEGNNK SQKHESTSSY NYRVVKEILI RLSKLCVQES
ASVRKSRKQQ QRLLRNMGAH AVVLELLQIP YEKAEDTKMQ EIMRLAHEFL QNFCAGNQQN
QALLHKHINL FLNPGILEAV TMQHIFMNNF QLCSEINERV VQHFVHCIET HGRNVQYIKF
LQTIVKAEGK FIKKCQDMVM AELVNSGEDV LVFYNDRASF QTLIQMMRSE RDRMDENSPL
MYHIHLVELL AVCTEGKNVY TEIKCNSLLP LDDIVRVVTH EDCIPEVKIA YINFLNHCYV
DTEVEMKEIY TSNHMWKLFE NFLVDICRAC NNTSDRKHAD SILEKYVTEI VMSIVTTFFS
SPFSDQSTTL QTRQPVFVQL LQGVFRVYHC NWLMPSQKAS VESCIRVLSD VAKSRAIAIP
VDLDSQVNNL FLKSHNIVQK TAMNWRLSAR NAARRDSVLA ASRDYRNIIE RLQDIVSALE
DRLRPLVQAE LSVLVDVLHR PELLFPENTD ARRKCESGGF ICKLIKHTKQ LLEENEEKLC
IKVLQTLREM MTKDRGYGEK LPQTPESENS TEELESSPPL RQLEDHKRGE ALRQILVNRY
YGNIRPSGRR ESLTSLGNGP LSPGGPSKPG GGGGGSGSGS MSRGEMSLAE VQCHLDKEGA
SNLVIDLIMN ASSDRVFHES ILLAIALLEG GNTTIQHSFF CRLTEDKKSE KFFKVFYDRM
KVAQQEIKAT VTVNTSDLGN KKKDDEIDRD APSRKKAKEP SPQITEEVRD QLLEASAATR
KAFSTFRREA DPDDHYQPGE GAQAAADKAK DDLEMSAVIT IMQPILRFLQ LLCENHNRDL
QNFLRCQNNK TNYNLVCETL QFLDCICGST TGGLGLLGLY INEKNVALIN QTLESLTEYC
QGPCHENQNC IATHESNGID IITALILNDI NPLGKKRMDL VLELKNNASK LLLAIMESRH
DSENAERILY NMRPKELVEV IKKAYMQGEV EFEDGENGED GAASPRNVGH NIYILAHQLA
RHNKELQTML KPGGQVDGDE ALEFYAKHTA QIEIVRLDRT MEQIVFPVPS ICEFLTKESK
LRIYYTTERD EQGSKINDFF LRSEDLFNEM NWQKKLRAQP VLYWCARNMS FWSSISFNLA
VLMNLLVAFF YPFKGVRGGT LEPHWSGLLW TAMLISLAIV IALPKPHGIR ALIASTILRL
IFSVGLQPTL FLLGAFNVCN KIIFLMSFVG NCGTFTRGYR AMVLDVEFLY HLLYLLICAM
GLFVHEFFYS LLLFDLVYRE ETLLNVIKSV TRNGRSIILT AVLALILVYL FSIVGYLFFK
DDFILEVDKL PNETAVPETS ESLAREFLYS DVCRVETGEN CSSPAPKEAL VVPVEQTEQD
KEHTCETLLM CIVTVLSHGL RSGGGVGDVL RKPSKEEPLF AARVIYDLLF FFMVIIIVLN
LIFGVIIDTF ADLRSEKQKK EEILKTTCFI CGLERDKFDN KTVTFEEHIK EEHNMWHYLC
FIVLVKVKDS TEYTGPESYV AEMIKERNLD WFPRMRAMSL VSSDSEGEQN ELRNLQEKLE
STMKLVTNLS GQLSELKDQM TEQRKQKQRI GLLGHPPHMN VNPQQPA
//
