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Database: UniProt/SWISS-PROT
Entry: PLCD3_MOUSE
LinkDB: PLCD3_MOUSE
Original site: PLCD3_MOUSE 
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-OCT-2014, entry version 108.
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 IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. {ECO:0000269|PubMed:16314520}.
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). {ECO:0000250}.
CC   -!- ENZYME REGULATION: Strongly activated by phosphatidic acid.
CC       Inhibited by phosphatidylethanolamine (PtdEtn),
CC       phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine
CC       (PtdSer) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Cytoplasm {ECO:0000250}. 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. {ECO:0000250}.
CC   -!- DOMAIN: The PH domain mediates interaction with the surface
CC       membrane by binding to PIP2. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Plcd1 and Plcd3 die between
CC       11.5 and 13.5 dpc. They exhibit severe disruption of the normal
CC       labyrinth architecture in the placenta and decreased placental
CC       vascularization, as well as abnormal proliferation and apoptosis
CC       of trophoblasts in the labyrinth area. Furthermore, Plcd1 and
CC       Plcd3 double knockout embryos supplied with a normal placenta by
CC       the tetraploid aggregation method survive beyond 14.5 dpc,
CC       indicating that the embryonic lethality is caused by a defect in
CC       trophoblasts. {ECO:0000269|PubMed:16314520}.
CC   -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00041}.
CC   -!- SIMILARITY: Contains 3 EF-hand domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00270}.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00271}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD32589.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAM22088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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   CCDS; CCDS25512.1; -.
DR   RefSeq; NP_690026.2; NM_152813.3.
DR   UniGene; Mm.264743; -.
DR   ProteinModelPortal; Q8K2J0; -.
DR   SMR; Q8K2J0; 51-784.
DR   PhosphoSite; Q8K2J0; -.
DR   PaxDb; Q8K2J0; -.
DR   PRIDE; Q8K2J0; -.
DR   Ensembl; ENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
DR   GeneID; 72469; -.
DR   KEGG; mmu:72469; -.
DR   UCSC; uc007ltf.2; mouse.
DR   CTD; 113026; -.
DR   MGI; MGI:107451; Plcd3.
DR   eggNOG; NOG149692; -.
DR   GeneTree; ENSGT00740000114979; -.
DR   HOGENOM; HOG000006871; -.
DR   HOVERGEN; HBG053610; -.
DR   InParanoid; Q8K2J0; -.
DR   KO; K05857; -.
DR   OMA; HWGQTLQ; -.
DR   OrthoDB; EOG7V49XT; -.
DR   PhylomeDB; Q8K2J0; -.
DR   TreeFam; TF313216; -.
DR   Reactome; REACT_196473; Synthesis of IP3 and IP4 in the cytosol.
DR   NextBio; 336294; -.
DR   PRO; PR:Q8K2J0; -.
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:Ensembl.
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:UniProtKB-EC.
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; 2.60.40.150; -; 1.
DR   Gene3D; 3.20.20.190; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR028406; PLC-delta3.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
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   PANTHER; PTHR10336:SF33; PTHR10336:SF33; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; EF-hand_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; 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   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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00270}.
FT   DOMAIN      524    640       PI-PLC Y-box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00271}.
FT   DOMAIN      643    748       C2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00041}.
FT   CA_BIND     191    202       1. {ECO:0000255}.
FT   CA_BIND     227    238       2. {ECO:0000255}.
FT   REGION       69     97       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    348    348       {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT   ACT_SITE    393    393       {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT   METAL       349    349       Calcium 1; catalytic. {ECO:0000250}.
FT   METAL       378    378       Calcium 1; catalytic. {ECO:0000250}.
FT   METAL       380    380       Calcium 1; catalytic. {ECO:0000250}.
FT   METAL       427    427       Calcium 1; catalytic. {ECO:0000250}.
FT   METAL       679    679       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       681    681       Calcium 2. {ECO:0000250}.
FT   METAL       705    705       Calcium 2. {ECO:0000250}.
FT   METAL       734    734       Calcium 3. {ECO:0000250}.
FT   METAL       735    735       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       736    736       Calcium 3. {ECO:0000250}.
FT   BINDING     476    476       Substrate. {ECO:0000250}.
FT   BINDING     478    478       Substrate. {ECO:0000250}.
FT   BINDING     553    553       Substrate. {ECO:0000250}.
FT   BINDING     580    580       Substrate. {ECO:0000250}.
FT   MOD_RES     101    101       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     492    492       Phosphoserine.
FT                                {ECO:0000269|PubMed:19144319}.
FT   CONFLICT    199    199       S -> N (in Ref. 2; BAE26150).
FT                                {ECO:0000305}.
FT   CONFLICT    301    302       AK -> GE (in Ref. 1; BAD32589).
FT                                {ECO:0000305}.
FT   CONFLICT    378    378       E -> K (in Ref. 2; BAE26150).
FT                                {ECO:0000305}.
FT   CONFLICT    540    540       D -> E (in Ref. 4; AAH31392).
FT                                {ECO:0000305}.
FT   CONFLICT    659    659       A -> T (in Ref. 2; BAE26150).
FT                                {ECO:0000305}.
FT   CONFLICT    660    660       I -> V (in Ref. 2; BAE26150).
FT                                {ECO:0000305}.
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
//
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