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 03-AUG-2022, entry version 120.
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; 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 (PubMed:11584008).
CC This release is regulated by cAMP both dependently and independently of
CC PKA (By similarity). {ECO:0000250|UniProtKB:Q9Z329,
CC ECO:0000269|PubMed:11584008}.
CC -!- SUBUNIT: Homotetramer. Interacts with CABP1. Interacts with BOK;
CC regulates ITPR2 expression. Interacts with BCL2L10 (By similarity).
CC Interacts with TRPC4 (By similarity). {ECO:0000250|UniProtKB:P29995,
CC ECO:0000250|UniProtKB:Q14571}.
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: Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium
CC release. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; AF402600; AAL39077.1; -; mRNA.
DR RefSeq; NP_776794.1; NM_174369.2.
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 InParanoid; Q8WN96; -.
DR OrthoDB; 94996at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0030667; C:secretory granule membrane; IDA:CACAO.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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; 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; 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; 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..2701
FT /note="Inositol 1,4,5-trisphosphate receptor type 2"
FT /id="PRO_0000153923"
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..2260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2261..2281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2282..2307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2308..2328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2329..2351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2352..2372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2373..2394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2395..2415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2416..2520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2521..2541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2542..2701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..166
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 173..223
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 231..287
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 294..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 324..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2678..2701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..269
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 937
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14571"
FT MOD_RES 1711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2636
FT /note="Phosphoserine"
FT /evidence="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
