ID I3LPN5_PIG Unreviewed; 2702 AA.
AC I3LPN5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
GN Name=ITPR2 {ECO:0000313|Ensembl:ENSSSCP00000026062.2,
GN ECO:0000313|VGNC:VGNC:103294};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000026062.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000026062.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000026062.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB23998.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000026062.2}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; DQIR01168521; HDB23998.1; -; Transcribed_RNA.
DR EMBL; DQIR01189636; HDB45113.1; -; Transcribed_RNA.
DR STRING; 9823.ENSSSCP00000026062; -.
DR PaxDb; 9823-ENSSSCP00000000585; -.
DR Ensembl; ENSSSCT00000023164.3; ENSSSCP00000026062.2; ENSSSCG00000000555.5.
DR VGNC; VGNC:103294; ITPR2.
DR GeneTree; ENSGT00940000156039; -.
DR HOGENOM; CLU_2132754_0_0_1; -.
DR OMA; PLETRAC; -.
DR OrthoDB; 5480299at2759; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000555; Expressed in omentum and 43 other cell types or tissues.
DR Genevisible; I3LPN5; SS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:Ensembl.
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:0035091; F:phosphatidylinositol binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; 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_IP3_receptor.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR PANTHER; PTHR45816:SF3; 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; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 2.
DR SUPFAM; SSF82109; MIR domain; 2.
DR PROSITE; PS50919; MIR; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, 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:UP000008227};
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 2228..2250
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2262..2281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2302..2326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2346..2374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2395..2417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368044"
FT TRANSMEM 2523..2546
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 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 COILED 2633..2681
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1159..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2702 AA; 308252 MW; A8D54DA41A50DF00 CRC64;
MSDKMSSFLY IGDIVSLYAE GSVNGFINTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
CPMNRYSAQK QYWKAKQAKQ GNHTETALLK KLQHAAELEQ KQNESENKKL LGEIVKYSNV
IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
KVVLMPVNAG QPLHASNIEL LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV
RLFHAEQEKF LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGDLPTS KKKRQAGEKI MYTLVSVPHG
NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTDEE RPVMLKIGTC
QTKEDKEAFA IVSVPLSEVR DLDFANDANK VLATAVKKLE NGTITQNERR FVTKLLEDLI
FFVADVLNNG QEVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGPMLRLED
LGDQRYAPYK YMLRLCYRVL RHSQQDYRKN 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 AILDIVQVPM
SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MTVPEMQPSL HPSKQGSPPE
QEDVTVMDTK LKIIEILQFI LSVRLDYRIS YMLSIYKKEF GENNGNAETS TNGSPDTLLP
SAIVPDIDEI AAQAETMFAG RKEKNPVQLD DEGGRTFLRV LIHLIMHDYP PLLSGALQLL
FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKNSSYENGE
MGESQVKGGE EPIEDSNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR
NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP QNQVLLHKHL
NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLHMMC SERDRGDEGG ALAYHITLVE
LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLEKCVT ESIMNIVSGF FNSPFSDNST
SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA IPVDLDSQVN
TLFMKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPSWDYR NIIEKLQDVV ASLEQQFSPM
MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
MLEKKDSFVE EGNTLRKILL NRYFKGDYAV CMNGHLSGTY CKSAQGGGSF SGQDSDKMGI
SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ YSFYQQLHEQ
KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD NELMTSGPRM RVRDSSLHLK
EGMKGQLTEA SSATSKAYYV YRREMDPEID IMYMGSEAGN TEEKSAEEVT MSPAITIMQP
ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK
NVVLVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDGVS
PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDDGDEALK HYANHTAQIE IVRHDRTMEQ
IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFHQT EDLYNEMKWQ KKIRSNPALF
WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PLFSVLLWIA VAICTSMLFF
FSKPVGIRPF LVSIMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPTTGGSAV PTMTLTSAMM GTCEKDNCSP
TIPASNSADE EYEDGIERTC DTLLMCIVTV LNQGLRNGGG VGDVLRRPSK DEPLFAARVV
YDLLFYFIVI IIVLNLIFGV IIDTFADLRS EKQKKEEILK TTCFICGLER DKFDNKTVSF
EEHIKSEHNM WHYLYFLVLV KVKDPTEYTG PESYVAQMIV EKNLDWFPRM RAMSLVSNEG
DSEQNEIRNL QEKLESTMSL VKQLSGQLAE LKEQMTEQRK NKQRLGFLGS NTPHVNHHMP
PH
//
