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Database: UniProt
Entry: U3JED2_FICAL
LinkDB: U3JED2_FICAL
Original site: U3JED2_FICAL 
ID   U3JED2_FICAL            Unreviewed;      1211 AA.
AC   U3JED2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase {ECO:0000256|PIRNR:PIRNR000956};
DE            EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000956};
GN   Name=PLCB2 {ECO:0000313|Ensembl:ENSFALP00000001136.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001136.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000001136.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000001136.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC       by activated phosphatidylinositol-specific phospholipase C enzymes.
CC       {ECO:0000256|PIRNR:PIRNR000956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC         1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC         Evidence={ECO:0000256|ARBA:ARBA00023726};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000256|ARBA:ARBA00023726};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000956-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000956-2};
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DR   RefSeq; XP_005046731.1; XM_005046674.2.
DR   AlphaFoldDB; U3JED2; -.
DR   STRING; 59894.ENSFALP00000001136; -.
DR   Ensembl; ENSFALT00000001142.2; ENSFALP00000001136.1; ENSFALG00000001068.2.
DR   GeneID; 101806047; -.
DR   KEGG; fab:101806047; -.
DR   CTD; 5330; -.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000159326; -.
DR   HOGENOM; CLU_002738_2_0_1; -.
DR   OMA; RLAKCQD; -.
DR   OrthoDB; 2900494at2759; -.
DR   Proteomes; UP000016665; Chromosome 5.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16209; EFh_PI-PLCbeta2; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08624; PI-PLCc_beta2; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR028403; PLC-beta2_cat.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR015359; PLC_EF-hand-like.
DR   InterPro; IPR046969; PLCbeta2_EF.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; EF-hand_like; 1.
DR   Pfam; PF17787; PH_14; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000956-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000956, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR000956,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000956,
KW   ECO:0000256|RuleBase:RU361133};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000956-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT   DOMAIN          544..660
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          660..788
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          464..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          894..927
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        836..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT   BINDING         408
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ   SEQUENCE   1211 AA;  138666 MW;  374AF9AA3646CE0B CRC64;
     MSVLNPILQP TEVKEYLCKG DRFIKWDDET SNASPVILRV DPQGFYVYWT YQSTEREILD
     ITSIRDTRAG RFAKMPKSLK LREVFNLDHP YSTFLLKTLT IVSGPDMVDL TFHNFVSYKE
     NICKDWAEDI MAIARNPLTY NAPRYTFLEK ILVKLKLQLN EEGKIPVRNI FQMFPADKKR
     VEEALSACHL PNGKNDAINP EDFPEPVYKT FLMNLCPRPE IDEIFTSHHL KAKPYMTKEH
     LAKFINKKQR DTRLNDILFP PAKPEQVQSL IEKYEPSGFN IQRGQLSPEG MVWFLCGPEN
     NLIVLDKLML YQDMTQPLSH YYINSSHNTY LTAGQFSGTS SPEMYRQTLL AGCRCVELDC
     WKGRPPDEEP IITHGFTMTT EILFKDAIEA IAESAFKTSP YPVILSFENH VDSPKQQAKM
     AEYCRTIFGD MLLTEPLEKY PLKPGVPLPS PKDLLRKILI KNKKNQSMSG KRQSSLKKGK
     NMEPETTEQP TSVDAEDTVW AGDVAEEEPE EEDDQLRNLD EEEIKKMQSD EGTAGLEVTA
     YEEMSSLVNY IQPIKFNSFE VSAKKNRSYV ISSFTEMKAG DLLSKFPMQF VEYNKWQMSR
     IYPKGTRMDS SNYQPQMFWN VGCQMVALNF QTMDVPMQQN MALFEFNGQC GYLLKHEFMR
     RPDKQFDPFS VDRIDGLVAT TVCVTVLSGQ FLSDRSVKTY VEVELLGLPR DAKRKHRTKL
     TSTANSINPV WKEEAFVFEK IMMPELASLK IVAWEEGGKF IGQRIIPIIA MHPGYHHVCL
     RSESNMPLTL PALFVFLEIK DYVPDAWADL TIALSNPIKF FNLQDKRLVK LKDTSGERPG
     TQTNLSSAET NGVAGFTGKP SIPPSNGSTG AAVFTKDEAL LEVKQMAEPE TITLAELQQK
     KRFLKLLKRQ EKELRELEQK GSKQREEVLQ KYSALFSEHA FPGGKKRTIR TRKTQKKRSV
     TPSDAGTSAN PVRAAESIDH HCLVELRERL EMDLIHLGEE HHNRIRRKKE QHATEQVARI
     LELAREKQAA ELRVLRDTSE SNIKDIKKRM EAKRVERVQA MLRNTSDKAA QERLKKEINN
     SHIQEVVQTV KRMTEKTGRF QQKLEEKQAA SLQSIKERES QLQQQVRVEY EERLRALNTE
     VQEMVKNYIK ASFPGEPQTG KEAGQSIPEG EQGFTDQLEA NTPVAEVSRL TLAMTEPLGA
     GMDVEIEESI F
//
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