PIP1_DROME
ID PIP1_DROME Reviewed; 1318 AA.
AC P25455; A4UZX5; M9PC05; Q0E8V1; Q7KTZ7; Q961D5; Q9VPN9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C;
GN Name=Plc21C; Synonyms=plc-21; ORFNames=CG4574;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND A), AND TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=2061323; DOI=10.1016/s0021-9258(18)98923-4;
RA Shortridge R.D., Yoon J., Lending C.R., Bloomquist B.T., Perdew M.H.,
RA Pak W.L.;
RT "A Drosophila phospholipase C gene that is expressed in the central nervous
RT system.";
RL J. Biol. Chem. 266:12474-12480(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=D;
CC IsoId=P25455-3; Sequence=Displayed;
CC Name=1; Synonyms=Class-I;
CC IsoId=P25455-2; Sequence=VSP_021970, VSP_004727;
CC Name=A; Synonyms=B, Class-II;
CC IsoId=P25455-1; Sequence=VSP_021970;
CC Name=C;
CC IsoId=P25455-4; Sequence=VSP_004727;
CC Name=H;
CC IsoId=P25455-5; Sequence=VSP_053950, VSP_004727;
CC Name=G;
CC IsoId=P25455-6; Sequence=VSP_053949, VSP_004727;
CC -!- TISSUE SPECIFICITY: Expressed in neuronal cell bodies of the optic
CC lobe, central brain, and thoracic ganglia in adults, and the brain of
CC larvae. {ECO:0000269|PubMed:2061323}.
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DR EMBL; M60452; AAA28819.1; -; mRNA.
DR EMBL; M60453; AAA28820.1; -; mRNA.
DR EMBL; AE014134; AAN10493.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64631.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64632.2; -; Genomic_DNA.
DR EMBL; AE014134; AAS64633.1; -; Genomic_DNA.
DR EMBL; AE014134; AGB92355.1; -; Genomic_DNA.
DR EMBL; AY051657; AAK93081.1; -; mRNA.
DR PIR; A40879; A40879.
DR PIR; B40879; B40879.
DR RefSeq; NP_001259818.1; NM_001272889.1. [P25455-6]
DR RefSeq; NP_476851.2; NM_057503.5. [P25455-1]
DR RefSeq; NP_476852.1; NM_057504.5. [P25455-1]
DR RefSeq; NP_995604.2; NM_205882.2. [P25455-5]
DR RefSeq; NP_995605.1; NM_205883.2. [P25455-3]
DR RefSeq; NP_995606.1; NM_205884.3. [P25455-4]
DR AlphaFoldDB; P25455; -.
DR SMR; P25455; -.
DR BioGRID; 59460; 4.
DR IntAct; P25455; 4.
DR STRING; 7227.FBpp0089226; -.
DR PaxDb; P25455; -.
DR PRIDE; P25455; -.
DR DNASU; 33204; -.
DR EnsemblMetazoa; FBtr0078047; FBpp0077710; FBgn0004611. [P25455-1]
DR EnsemblMetazoa; FBtr0078048; FBpp0077711; FBgn0004611. [P25455-1]
DR EnsemblMetazoa; FBtr0078049; FBpp0089225; FBgn0004611. [P25455-4]
DR EnsemblMetazoa; FBtr0078050; FBpp0089226; FBgn0004611. [P25455-3]
DR EnsemblMetazoa; FBtr0330673; FBpp0303523; FBgn0004611. [P25455-6]
DR EnsemblMetazoa; FBtr0330674; FBpp0303524; FBgn0004611. [P25455-5]
DR GeneID; 33204; -.
DR KEGG; dme:Dmel_CG4574; -.
DR CTD; 33204; -.
DR FlyBase; FBgn0004611; Plc21C.
DR VEuPathDB; VectorBase:FBgn0004611; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000173822; -.
DR InParanoid; P25455; -.
DR OMA; PNMEVDI; -.
DR PhylomeDB; P25455; -.
DR Reactome; R-DME-112043; PLC beta mediated events.
DR Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-DME-500657; Presynaptic function of Kainate receptors.
DR SignaLink; P25455; -.
DR BioGRID-ORCS; 33204; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33204; -.
DR PRO; PR:P25455; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004611; Expressed in brain and 24 other tissues.
DR Genevisible; P25455; DM.
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:0043153; P:entrainment of circadian clock by photoperiod; IGI:FlyBase.
DR GO; GO:0007629; P:flight behavior; IGI:FlyBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:FlyBase.
DR CDD; cd13361; PH_PLC_beta; 1.
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; 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; PTHR10336; 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; 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 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Transducer.
FT CHAIN 1..1318
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase classes I and II"
FT /id="PRO_0000088511"
FT DOMAIN 318..466
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 599..715
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 715..843
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 466..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 655
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 300..360
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_053949"
FT VAR_SEQ 907..913
FT /note="FVFVQVG -> C (in isoform 1 and isoform A)"
FT /evidence="ECO:0000303|PubMed:2061323"
FT /id="VSP_021970"
FT VAR_SEQ 907..912
FT /note="FVFVQV -> L (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_053950"
FT VAR_SEQ 1063..1069
FT /note="Missing (in isoform 1, isoform C, isoform G and
FT isoform H)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2061323"
FT /id="VSP_004727"
FT CONFLICT 508
FT /note="G -> A (in Ref. 1; AAA28819/AAA28820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1318 AA; 146391 MW; 95C14A73843A325E CRC64;
MMSAGGTYIS TASVEVPQAL QDGEKFIRWD DDSGTGTPVT MRVDAKGFFL YWVDQNNELD
ILDIATIRDV RTGQYAKRPK DNKLRQIVTL GPQDTLEEKT VTVCHGSDFV NMTFVNFCCT
RRDIAQLWTD GLIKLAYSLA QLNGSAIMFL QKAHTKLCLQ VDKSGRIPVK NIIKLFAQNK
EDRKRVEKAL DVTGLPSGKV DSISVSKFQF EDFYNLYKYL TQRSEVERLF DSIVGNSKRK
CMSIAQLVEF LNKTQRDPRL NEILYPYANP ARAKELIQQY EPNKFNAQKG QLSLDGFLRY
LMGDDNPIMA PSKLDLCDDM DQPMSHYFIN SSHNTYLTGH QLTGKSSVEI YRQCLLAGCR
CVELDFWNGR TEEPVIVHGY TFVPEIFAKD VLEAIAESAF KTSEYPVILS FENHCNPRQQ
AKIANYCREI FGDMLLDKPL DSHPLEPNMD LPPPAMLRRK IIIKNKKKHH HHHHHHHHKK
PAQVGTPAAN NKLTTANSVD AKAAQQVGLS ASHEDGGVTR STANGDVATG TGTGSAAGTA
GHAPPLQQIR QSSKDSTGSS DSDSSSEDES LPNTTPNLPS GNEPPPEKAQ KETEAGAEIS
ALVNYVQPIH FSSFENAEKK NRCYEMSSFD EKQATTLLKE RPIEFVNYNK HQLSRVYPAG
TRFDSSNFMP QLFWNAGCQL VALNFQTLDL AMQLNLGIFE YNARSGYLLK PEFMRRSDRR
LDPFAESTVD GIIAGTVSIT VLSGQFLTDK RANTFVEVDM YGLPADTVRK KFRTKTVRDN
GMNPLYDEEP FVFKKVVLPE LASIRIAAYE EGGKLIGHRV LPVIGLCPGY RHVNLRSEVG
QPIALASLFL CVVVKDYVPD DLSNFAEALA NPIKYQSELE KRDIQLSVLT DEAEALGSAD
EDLSKSFVFV QVGGQKKELR PVESLATSPK HRPSISAAAA MSVDVTVDRT DGGRGEDSIS
IVAPSIQHQH SLDQSVSTSI RQVESSQFDV DLVLAEPLEK ILDHKSVKEK RLEMEKKLES
LRKKHDKEKI KIAGQKSSPL EGKKPKFAIT NKLVKRLSNK SLNCLSPHSE PGVEIPACPL
DLGDSSEESA AADAGEDLAG GSSSLDGRTQ ESRLRSACRE YTSQYRELQE KYHEAIYSAA
EKVLKTSQTG QTKQLKASLD KVTGEVMHQL QEARRNEVKN LATVHRDRDE LIRMKREVAS
SVVERGVAER VRLKQTFDRR TDELQKQHDS VRNALAEHRS KARQILDKEA ESRSCVSSNG
FLVLFHGPHH HGCTGSGSSA LSGNNLTLNL DAGAAGSHSA ISPAKSHNSI AAAAEMKT
