ID A0A3P8SU81_AMPPE Unreviewed; 2701 AA.
AC A0A3P8SU81;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
GN Name=ITPR1 {ECO:0000313|Ensembl:ENSAPEP00000015880.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000015880.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000015880.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000015880.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 161767.ENSAPEP00000015880; -.
DR Ensembl; ENSAPET00000016298.1; ENSAPEP00000015880.1; ENSAPEG00000011081.1.
DR GeneTree; ENSGT00940000155071; -.
DR OMA; KMERVIF; -.
DR Proteomes; UP000265080; Chromosome 6.
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 SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50919; MIR; 4.
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:UP000265080};
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 2231..2249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2261..2279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2307..2325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2345..2372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2393..2415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2522..2545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT DOMAIN 110..164
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 229..285
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 292..356
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 362..418
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1119..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2676..2701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2701 AA; 308201 MW; 154E8517EBD262D6 CRC64;
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PDAGDLNNPP KKFRDCLFRL
CPMNRYSAQK QFWKAAKPGG NTDTVLLNKL HHAADLEKKQ NDSENKKLLG TVIQYGNVIQ
LLHLKSNKYL TVNKRLPALL EKNAMRVMLD TAGNEGSWFY IQPFYKLRSI GDSVVIGDKV
VLNPVNAGQP LHASTHQLVD NPGCNEVNSV NCNTSWKIVL FMKWSDNQEI ILKGGDVVRL
FHAEQEKFLT CDDHRKKQYV FLRTTGRQSA TSATSSKALW EIEVVQHDPC RGGAGYWNSL
FRFKHLATGH YLAAELDSEQ EALRARLRNV QDKVMYTLVS VPDGNDISSI FELDPTTLRG
GDSLVPRNSY VRLRHLCTNT WVHSTNQPID KEEEKPVMLR IGTSALKEDK EAFAIVPVSP
AEVRDLDFAN DASKVLASIA GKLEKGTITQ NERRAVTKLL EDLVFFVVDI PNNGQDVLEI
MVNKPNRERQ KLMREQNILK QIFKLLQAPF TDSGDGPMLR LEELADQRHA PFRHICRLCY
RVLRHSQQDY RKNQEYIAKQ FRFMQKQIGY DVLAEDTITA LLHNNRKLLE KHITAAEIDT
FVSLVRKNRE PRFLDYLSDL CVSMNKSIPV TQELICNAVL DPANADILIE TKLVLSRFEI
EGAPLGENSV ESEEDEEEVW LFWKDSNKEI RSKSIRELAQ DAKEGQKEDQ EVISYYRYQL
NLFARMCLDR QYLAINKISG QLDVDLILRC MSDEDLPYDL RASFCRMMLH MHVDRDPQEQ
VTPVKYARLW SEIPSEIAID DYDNDGTSKD EIKERFSQTM EFVENYLRDV VCQSFPFADK
EKNKLTFEVV NLARNLIYFG FYNFSDLLRL TKILLAILDC VHVSTIFPFN KLDKGDESKG
SNVMRSIHGV GELMSQVVLR GGGFLPTTSN NSSNGGTVKT QTEPEKQDIL VMDTKLKIIE
ILQFILNVRL DYRISCLLSI FKREFDESNS QSELSVTGAV EGPNNMPGAL DFEHIEEQAE
GIFGGSEENT PLDLDDHGGR TFLRVLLHLT MHDYPPLVSR ALHLLFRHFS QRQEVLQAFK
QVQLLVTSQD VENYKQIKSD LDQLRSIVEK SELWVYKRQG PDEGMDAGEG LSTEPEHKKG
DSGGTDKPKK PESTSSYNYR VVKEILLRLS RLCVQEGLSG RKSKKQQQRL LRNMGAHAVV
LELLQIPYEK GEDLRMQDIM KLAHQFLQNF CAGNQQNQAL LHKHINLFLN PGILEAITMQ
HIFMNNFQLC SEINERVVQH FVHCIETHGR NVQYLKFLQT IVKAENKFIK KCQDIVMAEL
VNAGEDVLVF YNDRASFQTL VQMMRSERDR MDENSPLMYH MHLVELLAVC TEGKNVYTEI
KCNSLLPLDD IVRVVTHEDC IPEVKIAYIN FLNHCYVDTE VEMKEIYTSN HMWKLFENFL
VDICRVCNNT SDRKHADTIL ERYVTETVMS IVTTFFSSPF SDQSTSLQTR QPVFVQLLQA
VFRVYHCNWL IPVQKGSVES CIKVLSDVAK GRAIAIPVDL DNQVNNLFVK SNNIVQKTAM
SWRLSARNAA RRDSVVTASR DYRNIIERLQ DIVSALEDRL RPLVQAELSV LVDVLHRPEL
LFPENTDSRK KCESGGFICK LIKHTKQLLE ENEERLCIKV LQTLREMMTK DRGYGEKGEA
LRQILVNRYY GNFHRSGGRR ESLTSFSNGP LSPVGPGKNP SGGGLSSLSR GEMSLAEVQC
HLDKEGASDL VIDLIMNTTS DRVFQESILL AIALLEGGNT TIQRSFFCRL TEDKKSEKFF
RVFYDRMKSA QLEIKATVTV NTSDLGNKKR DDETQDKDVP VRKKARDSAV VMTEDVKEQL
IEASSATKKA FNSYRREADP EDHFTSADGQ PSSGDKNQDE GEMSFVIVIM QPILRFLQLL
CENHNRDLQN FLRSQNNKNN YNLVCETLQF LDCICGSTTG GLGLLGLYIN EKNVALINQT
LESLTEYCQG PCHENQNCIA THESNGIDII IALILNDINP LGKKRMDLVL ELKNNASKLL
LAIMESRHDS ENAERILYNM RPKELVEVIK KAYLQGEVEF EDTKEEEDNG EEEEHDAASP
RNVGHNIYIL AHQLARHNKE LSMMLKPGGA SGEGDEALEF YAKHTAQIEI VRQDRTMEEI
VFPVPNICEF LTSESKLRVY YTTERDEQGS KINDFFLRAE DLFNEMNWQK KLRAQQVLYW
CSRNMSVWSN VSFNLAVLMN LLVCFFYPLE GVHGDMLDSH LSALLWMGVL ATLVIVIIMP
QPLGIRALVI VTILRLIFSV GLEPTLFLLG ACNVCNKIIF LISFVGNRGT FTRGYRAMVM
DFEFLYHLIY LIICCLGVFG HVFFYSLLLF DLVYREETLL NVIKSVTRNG RSIVLTAVLA
LILVYLFSIV GYIFFKDDFI LEVDRIPNTT LKSGASLADE FLSAGMCRGS IDDENCTTEA
QQGDLGMDSE EDSDMERTCD SLLMCIVTVL SHGLRSGGGV GDVLRKPSKE EPLFAARVIY
DLLFFFMVII IVLNLIFGVI IDTFADLRSE KQKKEEVLKT TCFICGLERD KFDNKTVTFE
EHIKEEHNMW HYLFFIVLVK VKDSTEYTGP ESYVAEMIKE HNLDWFPRMR AMSLVSSDAE
GEQNEIRNLQ EKLESTMRLV ANLSGQLTEL KEQMTEQRKQ KQRIGLLGHP PHMNINPQQP
A
//
