ITPR3_BOVIN
ID ITPR3_BOVIN Reviewed; 2664 AA.
AC Q8WN95;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 3;
DE AltName: Full=IP3 receptor isoform 3;
DE Short=IP3R 3;
DE Short=InsP3R3;
DE AltName: Full=Type 3 inositol 1,4,5-trisphosphate receptor;
DE Short=Type 3 InsP3 receptor;
GN Name=ITPR3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Adrenal medulla;
RX PubMed=11584008; DOI=10.1074/jbc.m107532200;
RA Yoo S.H., Oh Y.S., Kang M.K., Huh Y.H., So S.H., Park H.S., Park H.Y.;
RT "Localization of three types of the inositol 1,4,5-trisphosphate
RT receptor/Ca2+ channel in the secretory granules and coupling with the Ca2+
RT storage proteins chromogranins A and B.";
RL J. Biol. Chem. 276:45806-45812(2001).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium.
CC {ECO:0000269|PubMed:11584008}.
CC -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3 and TRPC4. Interacts
CC with TRPV4 (By similarity). Interacts with SIGMAR1 (By similarity).
CC Interacts with PML and AKT1 (By similarity). Interacts with IRAG2 (via
CC coiled-coil domain) (By similarity). Interacts with CABP1. Interacts
CC with TMBIM4/LFG4. Interacts with CEMIP (By similarity). Interacts with
CC TESPA1 (By similarity). Interacts with TMEM203 (By similarity).
CC Interacts with BOK; regulates ITPR3 expression (By similarity).
CC Interacts with BCL2L10. {ECO:0000250|UniProtKB:P70227,
CC ECO:0000250|UniProtKB:Q14573, ECO:0000250|UniProtKB:Q63269}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11584008}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11584008}. Note=Endoplasmic reticulum and secretory
CC granules.
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 -!- PTM: Phosphorylated on tyrosine residues. Phosphorylated by AKT1 on
CC serine and/or threonine residues (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; AF402601; AAL39078.1; -; mRNA.
DR RefSeq; NP_776795.1; NM_174370.3.
DR AlphaFoldDB; Q8WN95; -.
DR SMR; Q8WN95; -.
DR STRING; 9913.ENSBTAP00000047648; -.
DR BindingDB; Q8WN95; -.
DR ChEMBL; CHEMBL2853; -.
DR PaxDb; Q8WN95; -.
DR PeptideAtlas; Q8WN95; -.
DR PRIDE; Q8WN95; -.
DR GeneID; 281879; -.
DR KEGG; bta:281879; -.
DR CTD; 3710; -.
DR eggNOG; KOG3533; Eukaryota.
DR InParanoid; Q8WN95; -.
DR OrthoDB; 94996at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0030141; C:secretory granule; IDA:CACAO.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:AgBase.
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; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2664
FT /note="Inositol 1,4,5-trisphosphate receptor type 3"
FT /id="PRO_0000153927"
FT TOPO_DOM 1..2227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2228..2248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2249..2256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2257..2277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2278..2286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2287..2304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2305..2318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2319..2339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2340..2361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2362..2382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2383..2489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2490..2510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2511..2664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 113..173
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 174..224
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 232..288
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 295..372
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 378..434
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 320..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1820..1837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..270
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 507..510
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 567..569
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 1806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 1825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 1827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 2602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 2663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
SQ SEQUENCE 2664 AA; 303040 MW; 9C2C9979146E19AB CRC64;
MSEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC
PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS
VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG
DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV
VRLFHAEQEK FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
NGLYRFKHLA TGNYLAAEEN PSYKGDASDP KAAGTGAQGR TGRRNAGEKI KYRLVAVPHG
NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNVPIDVEEE RPIRLMLGTC
PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLH EGFISQNDRR FVIQLLEDLV
FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE
LSDQKNAPYQ HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE LICKCVLDPK
NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN NEHHEKSVRQ LAQEARAGNA
HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISQQLGVDLI FLCMADEMLP FDLRASFCHL
MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY
LNNVVSEAVP FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQAYED
PGGKNVRRST QGVGHMMSTM VLNRKQSVFG GPSLPAGAGA PEPLDGSKFE ENEDIVVMET
KLKILEILQF ILNVRLDYRI SYLLSVFKKE FVEVFPMQDS GADGTAPAFD STTANMNLDR
IGEQAEAMFG VGKTSSMLEV DDEGGRMLLR VLIHLTMHDY APLVSGALQL LFKHFSQRQE
VMHTFKQVQL LISAQDVENY KVIKSELDRL RTMVEKSELW VDKKGASKGE EGEAGPAKDK
KERPTDEEGF LHPPGEKSSE NYQIVKGILE RLNKMCGVGE QMRKKQQRLL KNMDAHKVML
DLLQIPYDKG DAKMMEILRY THQFLQKFCA GNPGNQALLH KHLHLFLTPG LLEAETMQHI
FLNNYQLCSE IGEPVLQHFV HLLATHGHHV QYLDFLHTVI KAEGKYVKKC QDMIMTEPAN
AGDDVVVFYN DKASLAHLLD MMKAARDGVE DHSPLMYHIS LVDLLAACAE GKNVYTEIKC
TSLLPLEDVV SVVTHEDCIT EVKMAYVNFV NHCYVDTEVE MKEIYTSNHI WTLFENFTLD
MARVCSKREK RLADPALEKY VLTVVLDTIS AFFSSPFSEN STSLQTHQTI VVQLLQSTMR
LLECPWLQQQ HKGSVEACIR TLAMVAKGRA ISLPMDLDAH ISSLLSSGAS CVAAAQRNAS
NYKTATRAFP RVMPTANQWD YKNIIEKLQD IITALEERLR PLVQAELSVL VDVLHWPELL
FLEGSDAYQR CESGGFLSKL IQHTKDLMES EEKLCVKVLR TLQQMLLKKT KYGDRGNQLR
KMLLQNYLQN RKSSSRGDLP DPMGTGLDQD WSAIAATQCR LDKEGATKLV CDLITSTKNE
KIFQESIGLA IRLLDGGNTE IQKSFYNLMT SDKKSERFFK VLHDRMKRAQ QETKSTVAVN
MSDLGSQPRE DREQADPTSK GRVASFSMPS SSSRYALGPS LRRGHEVGER VQSNEMGTSV
LIMQPILRFL QLLCENHNRD LQNFLRCQNN KTNYNLVCET LQFLDIMCGS TTGGLGLLGL
YINEDNVGLV IQTLETLTEY CQGPCHENQT CIVTHESNGI DIITALILND ISPLCKYRMD
LVLQLKDNAS KLLLALMESR HDSENAERIL ISLRPQELVD VIKKAYLQEE ERENSDVSPR
EVGHNIYILA LQLSRHNKQL QHLLKPVKRI QEEEAEGISS MLSLNNKQLT QMLKSSAPVQ
EQEEDPLAYY ENHTSQIEIV RQDRSMEQIV FPVPGICQFL TEETKHRLFT TTEQDEQGSK
VSDLFDQPSF LHNEMEWQRK LRSMPLIYWF SRRMTLWGSI SFNLAVFINI IIAFFYPYVE
GASTGVLGSP LISLLFWILI CFSIAALFTK RYSVRPLIVA LILRSIYYLG IGPTLNILGA
LNLTNKIVFV VSFVGNRGTF IRGYKAMVMD MEFLYHVGYI LTSVLGLFAH ELFYSILLFD
LIYREETLFN VIKSVTRNGR SILLTALLAL ILVYLFSIVG FLFLKDDFIL EVDRLPGNHS
RANPLGMPHG AATFVNTCSG DNVDCVSGVS VPEVLAEDEE PDSTERACDT LLMCIVTVMN
HGLRNGGGVG DILRKPSKDE SLFPARVVYD LLFFFIVIII VLNLIFGVII DTFADLRSEK
QKKEEILKTT CFICGLERDK FDNKTVSFEE HIKFEHNMWN YLYFIVLVRV KNKTDYTGPE
SYVAQMIKNK NLDWFPRMRA MSLVSSEGEG EQNEIRILQD KLSATMKLVS HLTAQLSELK
EQMTEQRKRR QRLGFVDVQN CMSR
