PLCB4_BOVIN
ID PLCB4_BOVIN Reviewed; 1023 AA.
AC Q07722; Q07721; Q07723; Q07724;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000305|PubMed:8407970};
DE AltName: Full=PCL-C1;
DE AltName: Full=Phosphoinositide phospholipase C-beta-4;
DE AltName: Full=Phospholipase C-beta-4;
DE Short=PLC-beta-4;
DE Flags: Fragment;
GN Name=PLCB4;
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] (ISOFORMS 1A; 1B; 2A AND 2B).
RC TISSUE=Retina;
RX PubMed=8327481; DOI=10.1073/pnas.90.13.6042;
RA Ferreira P.A., Shortridge R.D., Pak W.L.;
RT "Distinctive subtypes of bovine phospholipase C that have preferential
RT expression in the retina and high homology to the norpA gene product of
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6042-6046(1993).
RN [2]
RP PROTEIN SEQUENCE OF 20-37; 259-269; 315-337; 386-391; 604-623 AND 634-639.
RC TISSUE=Cerebellum;
RX PubMed=8389372; DOI=10.1016/s0021-9258(19)50327-1;
RA Min D.S., Kim D.M., Lee Y.H., Seo J., Suh P.-G., Ryu S.H.;
RT "Purification of a novel phospholipase C isozyme from bovine cerebellum.";
RL J. Biol. Chem. 268:12207-12212(1993).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8407970; DOI=10.1016/s0021-9258(19)36926-1;
RA Lee C.-W., Park D.J., Lee K.-H., Kim C.G., Rhee S.G.;
RT "Purification, molecular cloning, and sequencing of phospholipase C-beta
RT 4.";
RL J. Biol. Chem. 268:21318-21327(1993).
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 This form has a role in retina signal transduction.
CC {ECO:0000269|PubMed:8407970}.
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:0000305|PubMed:8407970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:8407970};
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:0000269|PubMed:8407970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000305|PubMed:8407970};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1B;
CC IsoId=Q07722-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=Q07722-2; Sequence=VSP_004720;
CC Name=2A;
CC IsoId=Q07722-3; Sequence=VSP_004719, VSP_004720;
CC Name=2B;
CC IsoId=Q07722-4; Sequence=VSP_004719;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the retina.
CC {ECO:0000269|PubMed:8407970}.
CC -!- PTM: The N-terminus is blocked.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13936; AAA30699.1; -; mRNA.
DR EMBL; L13935; AAC37304.1; -; mRNA.
DR EMBL; L13937; AAA30700.1; -; mRNA.
DR EMBL; L13938; AAA30701.1; -; mRNA.
DR PIR; B38932; B38932.
DR AlphaFoldDB; Q07722; -.
DR SMR; Q07722; -.
DR STRING; 9913.ENSBTAP00000017447; -.
DR SwissLipids; SLP:000000950; -.
DR PaxDb; Q07722; -.
DR PRIDE; Q07722; -.
DR eggNOG; KOG1265; Eukaryota.
DR InParanoid; Q07722; -.
DR OrthoDB; 368239at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Transducer.
FT CHAIN <1..1023
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-4"
FT /id="PRO_0000088494"
FT DOMAIN 149..299
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 413..529
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 532..657
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 711..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15147"
FT VAR_SEQ <1..104
FT /note="Missing (in isoform 2A and isoform 2B)"
FT /evidence="ECO:0000303|PubMed:8327481"
FT /id="VSP_004719"
FT VAR_SEQ 372..383
FT /note="Missing (in isoform 1A and isoform 2A)"
FT /evidence="ECO:0000303|PubMed:8327481"
FT /id="VSP_004720"
FT CONFLICT 24
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="E -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="M -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1023 AA; 117110 MW; 416D700C2095748C CRC64;
PVRSITRTFA SGKTEKVIFQ ALKELGLPSG KNDEIEPAAF TYEKFYELTQ KICPRTDIED
LFKKINGDKT DYLTVDQLVS FLNEHQRDPR LNEILFPFYD AKRAMQIIEM YEPDEDLKKQ
GLISSDGFCR YLMSDENAPV FLDRLELYQE MDHPLAHYFI SSSHNTYLTG RQFGGKSSVE
MYRQVLLAGC RCVELDCWDG KGEDQEPIIT HGKAMCTDIL FKDVIQAIKE TAFVTSEYPV
ILSFENHCSK YQQYKMSKYC EDLFGDLLLK QALESHPLEP GRPLPSPNDL KRKILIKKQT
TETEVEKKQL EALKSMMEAG ESAAPVNMLE DDNEEEIESA EQEEEAHPEY KYGNELSADD
LGHKEAIANS VKKASDDLEH ENSKKGLVTV EDEQAWMASY KYVGATTNIH PYLSTMINYA
QPVKFQGFHV AEERNIHYNM SSFNESVGLG YLKTHAIEFV NYNKRQMSRI YPKGGRVDSS
NYMPQIFWNS GCQMVSLNYQ TPDLAMQLNQ GKFEYNGSCG YLLKPDFMRR PDRTFDPFSE
TPVDGVIAAT CSVQVISGQF LSDKKIGTYV EVDMYGLPTD TIRKEFRTRM VMNNGLNPVY
NEESFVFRKV ILPDLAVLRI AVYDDNNKLI GQRILPLDGL QAGYRHISLR NEGNKPLSLP
TIFCNIVLKT YVPDGFGDIV DALSDPKKFL SITEKRADQM RAMGIETSDI ADVPSDTSKN
DKKGKANTAK ANVTPQSSSE LRPTTTAALG AGLEAKKGIE LIPQVRIEDL KQMKAYLKHL
KKQQKELSSL KKKHAKEHST MQKLHCTQVD KIVAQYDKEK LTHEKILEKA MKKKGGSNCL
EMKKETEIKI QTLTSDHKSK VKEIVAQHTK EWSDMINTHS AEEQEIRDLL LSQQCELLRK
LLISAHEQQT QQLKLSHDRE SKEMRAHQAK ISMENSKAIS QDKSIKNKAE RERRVRELNS
SNTKKFLEER KRLAMKQSKE MDQLKKVQLE HLEFVEKQNE QAKEMQQMVK LEAEMDRRPA
TVV
