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
//