ID W5NI41_LEPOC Unreviewed; 1190 AA.
AC W5NI41;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=PLCB4 {ECO:0000313|Ensembl:ENSLOCP00000020300.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020300.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020300.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01008992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NI41; -.
DR STRING; 7918.ENSLOCP00000020300; -.
DR Ensembl; ENSLOCT00000020334.1; ENSLOCP00000020300.1; ENSLOCG00000016435.1.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000156426; -.
DR HOGENOM; CLU_002738_2_1_1; -.
DR InParanoid; W5NI41; -.
DR OMA; AMQKAHC; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000016435; Expressed in brain and 10 other cell types or tissues.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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 GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16211; EFh_PI-PLCbeta4; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08591; PI-PLCc_beta; 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; 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; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 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 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000956};
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:UP000018468};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000956}.
FT DOMAIN 579..695
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 696..823
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1134..1182
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 893..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT ACT_SITE 375
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-1"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000956-2"
SQ SEQUENCE 1190 AA; 136042 MW; 8ED7708B85D56383 CRC64;
MAKAYEFNWQ KPLPDFLQAG AVFDRFEEDP FVFEPSCHFK VDEFGFFLTW KSEGKEGQVL
ECSLINSIRS GAVPKDPKIL AALEAVGKTE NDLEGRIVCV CCGADLVNLN FIYMVADSTE
TAKQWMEGLK SVIHNFRANN VCPMTCLKKH WMKLSFLTNV NGKIPVRSIT RTFASGKTEK
GIFQALKELG LPSGKNDEIE HSAFTFEKFY ALTQKICPRT DIEELFKKLN GDKTDYLSVD
QLVSFLNENQ RDPRLNEILF PFYDAKRAMQ IIEIFETDEE LKKKGRMSCD GFCRYLMSDQ
NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS ESPVILSFEN HCSKPQQYKM
AKYCEEIFGD LLLKQPLEAY PIEPGRPLPS PNDLKRKILI KNKRLKPEVE QKEQLETFKK
LMEAGETTAP ANILEDENEE EIENEADVEE EAHPELKFGS DLSSDDLSQK EPHLNSVKKV
SDVSEQDNNK KGGITVEDEQ AWITSYKYVG ATTNIHPYLS AMINYAQPVK FQGFDVAEER
NVHHNMSSFN ESVGLGYLKT NAIEFVNYNK RQMSRIYPKG GRVDSSNYMP QIFWNAGCQM
VSLNFQTPDL AMQLNQGKFE YNGSCGYLLK PDFMRRPDRM FDPFSETPVD GVIAATCSVQ
VFSGQFLSDK KIGTYVEVDM YGLPTDTIRK EFRTRMVMNN GLNPVYNEEP FVFRKVILPD
LAVLRIAVYD DNNKLIGQRI LPLDGLQAGY RHISLRNEGN KPLSLPTIFC NIVLKTYVPD
GFGAIVDALS DPKKFLSITE KRADQMRAMG IETSDIADVP NDSSKNDKKG KVNQVKASVT
PQSSSELRQN STAGQTNVNE AKKDTAALVP QVNIDDLKQM KTYLKLIKKQ QKELNALKKK
HAKDHSAMQK SHCTQVDKIV AQHDKEKLTY EKLLEKAIKK KGENNCLELK KETEIKIQTL
TSDHKLKVKE IVAQHTKEWS EMINSLSSEE QELRDQHVLQ QCEHLKKLLI SVQEQQTQQL
KLIHDRQSKD MRANQAKTSM ENSKAISQDK SIKNKAERER RVRELNSSNT KKFLEERKRL
AMKQSKEMDQ LEKAQHEQLE YLEKLNEQAK EMQQMVKLEA EMDRRPATVV
//
