ID A0A1S3P4I5_SALSA Unreviewed; 2747 AA.
AC A0A1S3P4I5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
GN Name=LOC106583165 {ECO:0000313|RefSeq:XP_014022504.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014022504.1};
RN [1] {ECO:0000313|RefSeq:XP_014022504.1}
RP IDENTIFICATION.
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_014022504.1; XM_014167029.1.
DR STRING; 8030.ENSSSAP00000117773; -.
DR PaxDb; 8030-ENSSSAP00000117773; -.
DR KEGG; sasa:106583165; -.
DR OrthoDB; 5480299at2759; -.
DR Proteomes; UP000087266; Chromosome ssa22.
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; 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; 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|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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000087266};
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 2275..2297
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2309..2327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2355..2373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2393..2420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2441..2463
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 1141..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1923..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2127..2147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2720..2747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2678..2705
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1141..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2127..2141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2747 AA; 313698 MW; 85FD066CDAA3B060 CRC64;
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PDTGDLNNPP KKFRDCLFRL
CPMNRYSAQK QFWKAAKPGG NSTTDTVLLN KLHHAADLEK KQNDSENKKL LGTVIQYGNV
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVM LDTAGNEGSW FYIQPFYKLR SIGDSVVIGD
KVVLNPVNAG QPLHASTHQL VDNPGCNEVN SVNCNTSWKI VLFMKCGDNQ EIILKGGDVV
RLFHAEQEKF LTCDDHRKKQ YVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
SLFRFKHLAT GHYLAAEMNP DYEEERLEFR SSLDSEQVDL RARLRNPQEK VMYTLVSVPD
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNHPIDKEE EKPVMLRIGT
SALKEDKEAF AIVPVSPAEV RDLDFANDAS KVLASIAGKL EKGTITQNER RAVTKLLEDL
VFFVVDIPNN GQDVLEIMVN KPNRERQKLM REQNILKQIF KLLQAPFTDS GDGPMLRLEE
LADQRHTPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFRF MQKQIGYDVL AEDTITALLH
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICNAVLDPT
NGDILIETKL VLSRFEIEGA SIGENSVESE EDEEEVWLFW KDSSKEIRSK SIRELAQDAK
EGAKEDQDVV SYYRYQLNLF ARMCLDRQYL AINKISGQLD VDLILRCMSD EDLPYDLRAS
FCRMMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD NDGTSKDEIK ERFALTMEFV
ENYLRDVVCQ SFPFADKEKN KLTFEVVNLS RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
STIFPINKLE KGDETKGSNV MRSIHGVGEL MTQVVLRGGG FLPTNPINPP NGDQVKTQTE
PEKQDILVMD TKLKIIEILQ FILNVRLDYR ISCLLCIFKR EFDESNSQSD LSIAGTHEGP
NNMPGALDFE NIEEQAEGIF GGSEENTPLD LDDDGGRTFL RVLLHLTMHD YPPLVSRALH
LLFRHFSQRQ EVLQAFKQVQ LLVTSQDVEN YKQIKSDLDQ LRSIVEKSEL WVYKRLGPDE
GMDTGEHSAE SQHKKGDSNS SGSDKPKKPE STSSYNYRVV KEILLRLSRL CVQESLSGRK
SKKQQQRLLR NMGAHTVVLE LLQIPYEKGE DVRMQEIMKL AHQFLQNFCA GNQQNQALLH
KHINLFLNPG ILEAVTMQHI FMNNFQLCSE INERVVQHFV HCIETHGRNV QYLKFLQTIV
KAESKFIKKC QDIVMAELVN AGEDVLVFYN DRASFQTLVT MMRSERDRMD QNSPLMYHIH
LVELLAVCTE GKNVYTEIKC NSLLPLDDIV RVVTHEDCIP EVKIAYINFL NHCYVDTEVE
MKEIYTSNHM WKLFENFLVD ICRVCNNTSD RKHADTVLES YVTETVMGIV TTFFSSPFSD
QSTSLQTRQP VFVQQLQAVF RVYHCNWLVP VQKGSVESCI KVLSDVAKGR AIAIPVDLDS
QVNNLFVKSN NIIQKTAMSW RMSARNAARR DSVLTASRDY RNIIERLQDI VSALEDRLRP
LVQAELSVLV DVLHRPELLF PENTDSRRKC ESGGFICKLI KHTKQLLEEN EERLCIKVLQ
TLREMMTKDR GYGEKLRSFN DEMDMPEQLD LNQPQKILDD QRRGEALRQI LVNRYYGNFH
SRSAGRRDSL TAFSNATLVP VGPGKSQSGL GGMGALSRGE MSLSEVQCHL DKEGASDLVI
DLIMNTTSDR VFQESILLAI ALLEGGNTTI QRSFICRLTE DKKSEKFFRV FYDRMKLAQL
EIKATVTVNT SDLGNRKRDD DAPDKDVPVR KKAKDSPVLV TDEAREQLLE ASSATKKAFN
SYRREADPDD HFSTADGTPS TGDKGQDDGE MSFIIVIMQP ILRFLQLLCE NHNRDLQNFL
RCQNNKNNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK NVALINQTVE SLTEYCQGPC
HENQNCIATH ESNGIDIIIA LILNDINPLG KKRMDLVLEL KNNASKLLLA IMESRHDSEN
AERILYNMRP KELVEVIKKA YLQGEVEFED PEEEDDSGEE EEHDAASPRN VGHNIYILAH
QLARHNKELQ VMLKPGGTNG EGDEALEFYA KHTAQIEIVR HDRTMEEIVF PVPNICEFLT
CESKLRVYYT TERDEQGSKI NDFFLSAENL FNEMNWQKKL RAQPVLYWCS RNMSFWSNIS
FNLAVLMNLL VAFFYPLEGL REGTLEPQLS ALLWLGMLAS LAIVVAMPQH LGVRTLIIAT
ILRLIFSVGL EPTLFLLGAF NVCNKIIFLM SFVGNKGTFT RGYKAMILDV EFLYHLMYLI
ICSLGVFVHV FFYSLLLFDL VYREETLLNV IKSVTRNGRS IVLTAVLALI LVYLFSIVGY
IFFKDDFILE VDRIPNTTLE NGVSMPNKLV SDGICRSESG ENNCTAELQL DDLLEDMEDG
KERTCDSLLM CIVTVLSHGL RSGGGVGDVL RKPSKEEPLF AARVIYDLLF FFMVIIIVLN
LIFGVIIDTF ADLRSEKQKK EEVLKTTCFI CGLERDKFDN KTVTFEEHIK EEHNMWHYLF
FIVLVKVKDS TEYTGPESYV AEMIKEHNLD WFPRMRAMSL VSSDAEGEQN EIRNLQEKLE
SAMRLVCNLS GQLTELKEQM TEQRKQKQRI GLLGHPPHMN VNPQQPA
//