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Database: UniProt
Entry: ITPR2_BOVIN
LinkDB: ITPR2_BOVIN
Original site: ITPR2_BOVIN 
ID   ITPR2_BOVIN             Reviewed;        2701 AA.
AC   Q8WN96;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JAN-2019, entry version 109.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 2;
DE   AltName: Full=IP3 receptor isoform 2;
DE            Short=IP3R 2;
DE            Short=InsP3R2;
DE   AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 2 InsP3 receptor;
GN   Name=ITPR2;
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       (PubMed:11584008). This release is regulated by cAMP both
CC       dependently and independently of PKA (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Z329, ECO:0000269|PubMed:11584008}.
CC   -!- SUBUNIT: Homotetramer. Interacts with CABP1. Interacts with BOK;
CC       regulates ITPR2 expression. {ECO:0000250|UniProtKB:P29995}.
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: Phosphorylation by cAMP-dependent PKA on Ser-937 increases
CC       calcium release. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
DR   EMBL; AF402600; AAL39077.1; -; mRNA.
DR   RefSeq; NP_776794.1; NM_174369.2.
DR   UniGene; Bt.66624; -.
DR   ProteinModelPortal; Q8WN96; -.
DR   SMR; Q8WN96; -.
DR   STRING; 9913.ENSBTAP00000002982; -.
DR   PaxDb; Q8WN96; -.
DR   PRIDE; Q8WN96; -.
DR   GeneID; 281878; -.
DR   KEGG; bta:281878; -.
DR   CTD; 3709; -.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q8WN96; -.
DR   KO; K04959; -.
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; IBA:GO_Central.
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:0030667; C:secretory granule membrane; IDA:CACAO.
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: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; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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_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; SSF48371; SSF48371; 1.
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   2701       Inositol 1,4,5-trisphosphate receptor
FT                                type 2.
FT                                /FTId=PRO_0000153923.
FT   TOPO_DOM      1   2227       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2228   2248       Helical. {ECO:0000255}.
FT   TOPO_DOM   2249   2260       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2261   2281       Helical. {ECO:0000255}.
FT   TOPO_DOM   2282   2307       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2308   2328       Helical. {ECO:0000255}.
FT   TOPO_DOM   2329   2351       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2352   2372       Helical. {ECO:0000255}.
FT   TOPO_DOM   2373   2394       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2395   2415       Helical. {ECO:0000255}.
FT   TOPO_DOM   2416   2520       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2521   2541       Helical. {ECO:0000255}.
FT   TOPO_DOM   2542   2701       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      112    166       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      173    223       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      231    287       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      294    372       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      265    269       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     937    937       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    1160   1160       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14571}.
FT   MOD_RES    1711   1711       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2607   2607       Phosphotyrosine. {ECO:0000255}.
FT   MOD_RES    2633   2633       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2636   2636       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
SQ   SEQUENCE   2701 AA;  307820 MW;  B574913EC55915A8 CRC64;
     MSDKMSSFLY IGDIVSLYAE GSVNGFINTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
     CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENKKL LGEIVKYSNV
     IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGG
     KVVLMPVNAG QPLHASNIEL LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV
     RLFHAEQEKF LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
     SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGDLPAS KKKRQAGEKI MYTLVSVPHG
     NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTDEE RPVMLKIGTC
     QTKEDKEAFA IVSVPPSEVR DLDFANDANK VLATTVKKLE NGTITQNERR FVTKLLEDLI
     FFVADVPNNG QDVLDVLITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
     LGDQRYAPYK YMLRLCYRVL GHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NTTAIPVTQE LICKFMLSPG
     NADILIQTKL VSMQGDNPME SAILSDDIDE EEVWLYWIDS NKEPHGKAIR HLAQEAKEGT
     KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCMSDESL PFDLRASFCR
     LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
     YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
     SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MSVPDIQPSL HPSKQGSPTD
     HEDVTVMDTK LKIIEILQFI LSVRLDYGIS YMLSIYKKEF GENNGNAEMS TNGSPDTLLP
     SAIVPDIDEI AAQAETMFAG RKEKNPVQLD DEGGRTFLRV LIHLIMHDYP PLLSGALQLL
     FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSSSYENGE
     MGENQVKGGE EPIEDSNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR
     NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP QNQVLLHKHL
     NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
     GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLHMMC SERDRGDESG PLAYHITLVE
     LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
     IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLEKCVT ESIMNIVSGF FNSPFSDNST
     SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA IPVDLDSQVN
     TLFLKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPSWDYR NIIEKLQDVV ASLEQQFSPM
     MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
     MLEKKDSFVE EGNTLRKILL NRYFKGDYGV SINGHLSGTY CKTAQVGGSF SGQDSDKMGI
     SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ YSFYQQLHEQ
     KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD TELMTSGPRM RVRDSSLHLK
     EGMKGQLTEA SSATSKAYCV YRREMDPEID IMCAGPEAGN AEDRSTEEVT MSPAIAIMQP
     ISRFLQLLCE NHNRELQHFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK
     NVVLVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
     KNNAPKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDDVS
     PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDDGDEALK YYANHTAQIE IVRHDRTMEQ
     IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRSNPALF
     WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PMFSILLWIA VAICTSMLFF
     FSKPVGIRPF LVSVMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
     ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
     LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPITGSNAV PTMTLTSILS TCEKDNCSPT
     IPASNTADEE YEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
     DLLFYFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE
     EHIKSEHNMW HYLYFLVLVK VKDPTEYTGP ESYVAQMIVE KNLDWFPRMR AMSLVSSEGD
     SEQNEVRNLQ EKLESTMSLV KQLSSQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP
     H
//
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