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Database: UniProt
Entry: ITPR3_BOVIN
LinkDB: ITPR3_BOVIN
Original site: 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   16-JAN-2019, entry version 113.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   Ca2+ 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
CC       messenger that mediates the release of intracellular calcium.
CC       {ECO:0000269|PubMed:11584008}.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3 and TRPC4.
CC       Interacts with TRPV4 (By similarity). Interacts with SIGMAR1 (By
CC       similarity). Interacts with PML and AKT1 (By similarity).
CC       Interacts with LRMP (via coiled-coil domain) (By similarity).
CC       Interacts with CABP1. Interacts with TMBIM4/LFG4. Interacts with
CC       CEMIP (By similarity). Interacts with TESPA1 (By similarity).
CC       Interacts with TMEM203 (By similarity). Interacts with BOK;
CC       regulates ITPR3 expression (By similarity).
CC       {ECO:0000250|UniProtKB:P70227, ECO:0000250|UniProtKB:Q14573,
CC       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
CC       vesicle membrane {ECO:0000269|PubMed:11584008}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:11584008}. Note=Endoplasmic
CC       reticulum and secretory 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
CC       on serine and/or threonine residues (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
DR   EMBL; AF402601; AAL39078.1; -; mRNA.
DR   RefSeq; NP_776795.1; NM_174370.3.
DR   UniGene; Bt.9025; -.
DR   ProteinModelPortal; 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   eggNOG; ENOG410XR97; LUCA.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q8WN95; -.
DR   KO; K04960; -.
DR   OrthoDB; 94996at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IDA:CACAO.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IDA:CACAO.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0006816; P:calcium ion transport; ISS:AgBase.
DR   GO; GO:0060402; P:calcium ion transport into cytosol; ISS:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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_recept-rel.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR   PANTHER; PTHR13715; PTHR13715; 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; SSF100909; 2.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Complete proteome;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   2664       Inositol 1,4,5-trisphosphate receptor
FT                                type 3.
FT                                /FTId=PRO_0000153927.
FT   TOPO_DOM      1   2227       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2228   2248       Helical. {ECO:0000255}.
FT   TOPO_DOM   2249   2256       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2257   2277       Helical. {ECO:0000255}.
FT   TOPO_DOM   2278   2286       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2287   2304       Helical. {ECO:0000255}.
FT   TOPO_DOM   2305   2318       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2319   2339       Helical. {ECO:0000255}.
FT   TOPO_DOM   2340   2361       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2362   2382       Helical. {ECO:0000255}.
FT   TOPO_DOM   2383   2489       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2490   2510       Helical. {ECO:0000255}.
FT   TOPO_DOM   2511   2664       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      113    173       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      174    224       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      232    288       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      295    372       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      266    270       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      507    510       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   MOD_RES     909    909       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES     927    927       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1806   1806       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1825   1825       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1827   1827       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2602   2602       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2663   2663       Phosphoserine.
FT                                {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
//
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