ID PLCD3_MOUSE Reviewed; 785 AA.
AC Q8K2J0; A2AHR0; A2AHR1; Q3UME8; Q69Z55; Q8BL19;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 01-MAY-2013, entry version 93.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C-delta-3;
DE AltName: Full=Phospholipase C-delta-3;
DE Short=PLC-delta-3;
GN Name=Plcd3; Synonyms=Kiaa1964;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT cDNAs identified by screening of terminal sequences of cDNA clones
RT randomly sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16314520; DOI=10.1128/MCB.25.24.10979-10988.2005;
RA Nakamura Y., Hamada Y., Fujiwara T., Enomoto H., Hiroe T., Tanaka S.,
RA Nose M., Nakahara M., Yoshida N., Takenawa T., Fukami K.;
RT "Phospholipase C-delta1 and -delta3 are essential in the trophoblast
RT for placental development.";
RL Mol. Cell. Biol. 25:10979-10988(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASS
RP SPECTROMETRY.
RC TISSUE=Macrophage;
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate
CC (PIP2) to generate 2 second messenger molecules diacylglycerol
CC (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the
CC activation of protein kinase C (PKC), while IP3 releases Ca(2+)
CC from intracellular stores. Essential for trophoblast and placental
CC development. May participate in cytokinesis by hydrolyzing PIP2 at
CC the cleavage furrow.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC diacylglycerol.
CC -!- COFACTOR: Binds 3 calcium ions per subunit. Two of the calcium
CC ions are bound to the C2 domain (By similarity).
CC -!- ENZYME REGULATION: Strongly activated by phosphatidic acid.
CC Inhibited by phosphatidylethanolamine (PtdEtn),
CC phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine
CC (PtdSer) (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity). Cytoplasm (By similarity). Cleavage furrow.
CC Note=Localizes at the cleavage furrow during cytokinesis.
CC -!- DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting
CC module (By similarity).
CC -!- DOMAIN: The PH domain mediates interaction with the surface
CC membrane by binding to PIP2 (By similarity).
CC -!- DISRUPTION PHENOTYPE: Mice lacking Plcd1 and Plcd3 die at
CC embryonic day 11.5 (E11.5) to E13.5 and exhibit severe disruption
CC of the normal labyrinth architecture in the placenta and decreased
CC placental vascularization, as well as abnormal proliferation and
CC apoptosis of trophoblasts in the labyrinth area. Furthermore,
CC Plcd1 and Plcd3 double-knockout embryos supplied with a normal
CC placenta by the tetraploid aggregation method survive beyond
CC E14.5, clearly indicating that the embryonic lethality is caused
CC by a defect in trophoblasts.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 3 EF-hand domains.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32829.1; Type=Erroneous initiation;
CC Sequence=BAD32589.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=CAM22088.1; Type=Erroneous gene model prediction;
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DR EMBL; AK173311; BAD32589.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK046669; BAC32829.1; ALT_INIT; mRNA.
DR EMBL; AK144950; BAE26150.1; -; mRNA.
DR EMBL; AL731805; CAM22088.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL731805; CAM22089.1; -; Genomic_DNA.
DR EMBL; BC031392; AAH31392.1; -; mRNA.
DR IPI; IPI00331040; -.
DR RefSeq; NP_690026.2; NM_152813.3.
DR UniGene; Mm.264743; -.
DR HSSP; P10688; 1DJX.
DR ProteinModelPortal; Q8K2J0; -.
DR SMR; Q8K2J0; 51-166, 196-784.
DR PhosphoSite; Q8K2J0; -.
DR PaxDb; Q8K2J0; -.
DR PRIDE; Q8K2J0; -.
DR Ensembl; ENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
DR GeneID; 72469; -.
DR KEGG; mmu:72469; -.
DR UCSC; uc007lte.2; mouse.
DR CTD; 113026; -.
DR MGI; MGI:107451; Plcd3.
DR eggNOG; NOG149692; -.
DR GeneTree; ENSGT00700000104181; -.
DR HOGENOM; HOG000006871; -.
DR HOVERGEN; HBG053610; -.
DR InParanoid; Q8K2J0; -.
DR KO; K05857; -.
DR OMA; HWGQTLQ; -.
DR OrthoDB; EOG45QHCM; -.
DR NextBio; 336294; -.
DR Bgee; Q8K2J0; -.
DR CleanEx; MM_PLCD3; -.
DR Genevestigator; Q8K2J0; -.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Compara.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IGI:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
DR Gene3D; 1.10.238.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_Ca-dep.
DR InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR InterPro; IPR018029; C2_membr_targeting.
DR InterPro; IPR011992; EF-hand-like_dom.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001192; Pinositol_PLipase_C.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR015359; PLipase_C_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; PF09279; efhand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF49562; C2_CaLB; 1.
DR SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Complete proteome; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1 785 1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-3.
FT /FTId=PRO_0000306822.
FT DOMAIN 65 168 PH.
FT DOMAIN 178 213 EF-hand 1.
FT DOMAIN 214 249 EF-hand 2.
FT DOMAIN 246 281 EF-hand 3.
FT DOMAIN 333 478 PI-PLC X-box.
FT DOMAIN 524 640 PI-PLC Y-box.
FT DOMAIN 643 748 C2.
FT CA_BIND 191 202 1 (Potential).
FT CA_BIND 227 238 2 (Potential).
FT REGION 69 97 Substrate binding (By similarity).
FT ACT_SITE 348 348 By similarity.
FT ACT_SITE 393 393 By similarity.
FT METAL 349 349 Calcium 1; catalytic (By similarity).
FT METAL 378 378 Calcium 1; catalytic (By similarity).
FT METAL 380 380 Calcium 1; catalytic (By similarity).
FT METAL 427 427 Calcium 1; catalytic (By similarity).
FT METAL 679 679 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 681 681 Calcium 2 (By similarity).
FT METAL 705 705 Calcium 2 (By similarity).
FT METAL 734 734 Calcium 3 (By similarity).
FT METAL 735 735 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 736 736 Calcium 3 (By similarity).
FT BINDING 476 476 Substrate (By similarity).
FT BINDING 478 478 Substrate (By similarity).
FT BINDING 553 553 Substrate (By similarity).
FT BINDING 580 580 Substrate (By similarity).
FT MOD_RES 101 101 Phosphoserine (By similarity).
FT MOD_RES 492 492 Phosphoserine.
FT CONFLICT 199 199 S -> N (in Ref. 2; BAE26150).
FT CONFLICT 301 302 AK -> GE (in Ref. 1; BAD32589).
FT CONFLICT 378 378 E -> K (in Ref. 2; BAE26150).
FT CONFLICT 540 540 D -> E (in Ref. 4; AAH31392).
FT CONFLICT 659 659 A -> T (in Ref. 2; BAE26150).
FT CONFLICT 660 660 I -> V (in Ref. 2; BAE26150).
SQ SEQUENCE 785 AA; 88607 MW; 8B3DE84FB7A52238 CRC64;
MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM GLTEDEDVQA
MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA SKHIFFVQHI EAVREGHQSE
GLRRFGGAFA PACCLTIAFK GRRKNLDLAA PTAEEAQRWV RGLAKLRARL DAMSQRERLD
HWIHSYLHRA DSDQDSKMSF KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE
AFLRRLLKRP ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET
AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT YLTDSQIGGT
SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK ILFRDVIQAV RDHAFTSSPY
PVILSLENHC GLEQQAVMAR HLRSILGDML VTQALDSQNP EELPSPEQLK GRILVKGKKL
PAARSEDGRI LSDREEEEEE EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD
PSPGPPQSCT VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN
SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC PGPPRTTLAI
QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET DYVLNNGFNP CWEQTLQFRL
RAPELVLVRF VVEDYDTTSP NDFVGQSTLP LSSLKQGYRH IHLLSKDGAS LAPATLFVHI
RIQNS
//
