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Database: UniProt
Entry: A0A1S3H8A9_LINUN
LinkDB: A0A1S3H8A9_LINUN
Original site: A0A1S3H8A9_LINUN 
ID   A0A1S3H8A9_LINUN        Unreviewed;      2777 AA.
AC   A0A1S3H8A9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor {ECO:0000256|RuleBase:RU368044};
GN   Name=LOC106152615 {ECO:0000313|RefSeq:XP_013381721.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013381721.1};
RN   [1] {ECO:0000313|RefSeq:XP_013381721.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26383154;
RA   Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA   Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT   "The Lingula genome provides insights into brachiopod evolution and the
RT   origin of phosphate biomineralization.";
RL   Nat. Commun. 6:8301-8301(2015).
RN   [2] {ECO:0000313|RefSeq:XP_013381721.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_013381721.1; XM_013526267.1.
DR   EnsemblMetazoa; XM_013526267.1; XP_013381721.1; LOC106152615.
DR   GeneID; 106152615; -.
DR   OrthoDB; 5403784at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0051209; P:release of sequestered calcium ion into cytosol; IEA:UniProtKB-UniRule.
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; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt.
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; PTHR13715:SF100; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; 1.
DR   PANTHER; PTHR13715; RYANODINE RECEPTOR AND IP3 RECEPTOR; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 1.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 2.
DR   SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 1.
DR   SUPFAM; SSF82109; MIR domain; 2.
DR   PROSITE; PS50919; MIR; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU368044};
KW   Calcium channel {ECO:0000256|RuleBase:RU368044};
KW   Calcium transport {ECO:0000256|RuleBase:RU368044};
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:UP000085678};
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        2217..2240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   TRANSMEM        2275..2297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   TRANSMEM        2346..2373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   TRANSMEM        2400..2421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   TRANSMEM        2433..2454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   TRANSMEM        2466..2496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368044"
FT   DOMAIN          113..167
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   REGION          2650..2777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2652..2678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2693..2711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2712..2728
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2729..2744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2777 AA;  320249 MW;  2D736BDA3493A2EB CRC64;
     MGEFLCIGDY ISLFCEETEG YVYSYQTSSS HNGLYIYQGQ DRKKPGKIPN PHAITFRVCI
     QNRYKLNKKY RKLLAASSKD PENLELKALV AQAKTSANAE NQDNISEQKR QHGKRVRYGE
     IIQLKHVFTD KYVHISTTQT SHRDKNNMLI SLHQYNGKHA QFRILPRYKV KSEGEYVQIL
     DQIVYESFKS QGHYFHSSVP WNIEKDMVGS ELNLGVAQTG FTVVRYYRPS DENEANVRGS
     SFIRLFHKEL EAYLVAEGLF GEPVQEEVHL RIREIDQLNP RTLSPPNSAI TYWQVEPEDT
     ILNGGVVRWE QQVRLRHVTT RRFLCLDADF EVCLTAEEND PRSVFRFHPV LSLREQDLDP
     DTPEQNEIDF ESYCRIEHVL TGNWLHALKD EPYQRRRDMG RENDRSMQAL RWDGGEVRKI
     SSTENRRYVD VFTIHEVEWE QIYSANFVAG MVPFLSKLIE SREECDYLNA MKTHQITTAL
     QELKQFMIIN GETYKDHQKL MRNFRIVDLL VQLLQSPLQD APDSNYLLSV FKEAYDILYT
     YMTGNSRKNA LYFAKYIEFF QTQLSLKAST SVMIKQYHLV VVDPTLKGDI GLNVAQMLVE
     LIRDNRQIVD RITHEQIDIF VDLLRQRKNY RFLDLLNVLC VCDGKTILEN QSYITETWLR
     HDKVSFDAKT CHIHLTGADV YLIERGQYIH KEHNVVYIST DAGHTWVPLH QFANADSPYY
     SEEEYLYLDR QLDLLGKLCK GRNQFSIRVI TKDLDILTWE NTFVCLRSEL LPPSLRAKYC
     SLIIDLFVDV GASHSVLDQH TLVFVYEDID NPRPLYSTKS QVATNVLFLA QELGTVFPVM
     RDWIQEFVES NPEMYSSQVG QNKLIEQVMR LLCYLVRFGC YCSADEIRIL LKPLMIMLDG
     RNDRPFPKNA EIQNSKEVKK LVKQYRETDR FEKSAETKAL VDAKYQGLSV LELLFTFQSN
     TRLESFVSKF KTAETTANAK KKKHRSVLSP LVDDSYDAFN TSKKNLRKQK KFLHELRAMF
     ESSSYFDVEY ITNISLDLSN YKYEKMLTQS LNILNKYYSS KTDMFKIAIP TLVLTTQESC
     KIHIDIMRQL PLVRHLAKCS YNMEQAEAMS VVFDQFVLFT HLRDEPTLRH PMNQKILINH
     GVLDLIFAIL SQEVDVQITE QAAPMELVFG KALNLLRFLA QGNEDVQAKM NDRLDSLMNI
     KLVPSHLAIA LREVFAGNQN NCLKIQPKQI LKIVHLAGEN QDRAPEFLDL LGSIVKVELL
     ELPLKRNQGL VMKYLMQNYH KAAYLFDQSQ EDRLRILTSK TGNSHQRYLI SLVDLLAKCA
     EGENRYIESL CQTIMPIEEI MDVLNNHFID NNLKSPYLRY LMWVYMKTAG TMIESGAGDL
     PHDRHVWIYI QALAREAESL KTYISENEVK TVEVMRAPPP KGAVAEMDDS DGAAHATLFY
     FFDAVLPFLQ TFFTKFYSPD KELYPDELEY VDQLAHSLVL WCDRVGAVLC NATHLKVLIG
     CVPSVLQSSS IPKNLSTESA LTNYPSLKPK QVQLWKNTYK VMEGFIEQYG NGRCLRDPTR
     ETIDTYTIYY QNEDELNKKF RAFSVNCSLV YGGHNTVTAQ LKHKSKREYT EIGGDEDLPL
     GEEFQAHVRC FVKHNEKNIA KRYQNVSKLV QQLAVSANAV NPKDGTYEND ELDIKSLQIL
     RAVIHNEERK LREDWEENTQ DKKVQKQLKV ILEVQNTLNS YSAVEEVLPH LGRPSNAIVR
     ESLAFLSIML FNANRNVQRT MLDVFKSMRT ETFFFAIRIR LEIAANGLKE RRALATQHEA
     RVKESMTQAK SLQTNLTVGR KAMKDIQAIE RSRRQSRLMK GARANSLRAL QRDRQSGLTS
     ISPASSKCNS LQRFKLPNGS LNEETPLVFG SNHNDIELNE VMVEGSDNLS VDVEEDDVLD
     GLEFKDEGYI VLVLRLLAAM CDGQNQSIQD YLRDQPDNIK SINVVADTAQ FVNVVYSNIT
     ASTIDLVIQL FSTLNEFTAG NQANRVVLLD NKVVDYINFI LRAGKYEGIS MEMQLELREV
     IANLLVSLIE ENGPEPIKVA REVKDTVDKE AVYRCMVDCY SIHQEKNKKN DLKDKAYEVG
     FLYFLLMARF YDIDPVLNEK AGLVITPDQM AAYNYYKKNS MSIELMKDGN LQKVHFRVKN
     KNVLREEVKE KLKWDVDRSS PSNKIRDLMA WSKDILKDIY YQRKMLRNPI AVFFTKFWLL
     WNYLVILLSV AINVLMLWAW KAPYDMSQAP ENMTHLDHAI YNPNPDTSSV EIYDLLLYAM
     GGTHNLFSLF VLISYFLSNH PKCPSLSAIP NLCRRLCGRK DEEEDEIAHE VDCEKAKRQS
     KLDVKFFSLA TFYYVIFVGM SVAGTFFHGY FFAFHLLNIV NNNQILQGVI KAVTQNGVSL
     LWVGILGVII FYIYALISFA FMRALFLPKD EEYCGTLLEC SVTVIRYGLI GAIFDRLTLP
     ESENNFIAFA VVAVFHLSFF ILITTIGLNV ILGIVVDTFS ELRDLKWTAE SDMRDTCFIC
     SRGSHDFEHH GNGFLKHARE EHNMWAYIFF FIHLDDTKSN DYTALDLHVA QALQREQYEF
     FPMNCALSLT GEEDGTDEKI DAVLEKVTEL LRRQREEESK RMREEEHRRQ KQWQEMYRKA
     LSGSHDTLAA AIEGPRRPED REGDAARYSD DDDSRGGVRT PETITLRDSA TSTEESPPRE
     SPRRTEEPPE TPRELLPPPP PPPSDGPHDV PPERPHDEPH ALDMAPHVSE VAFPLTAPED
     FPSPTFSDDD DFDDTRL
//
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