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Q8K2J0 (PLCD3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-delta-3
Phospholipase C-delta-3
Short name=PLC-delta-3
Gene names
Name:Plcd3
Synonyms:Kiaa1964
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca2+ from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow. Ref.5

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactor

Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain By similarity.

Enzyme regulation

Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer) By similarity.

Subcellular location

Membrane; Peripheral membrane protein By similarity. Cytoplasm By similarity. Cleavage furrow. Note: Localizes at the cleavage furrow during cytokinesis.

Domain

The C2 domain is a Ca2+-dependent membrane-targeting module By similarity.

The PH domain mediates interaction with the surface membrane by binding to PIP2 By similarity.

Disruption phenotype

Mice lacking Plcd1 and Plcd3 die between 11.5 and 13.5 dpc. They exhibit severe disruption of the normal labyrinth architecture in the placenta and decreased placental vascularization, as well as abnormal proliferation and apoptosis of trophoblasts in the labyrinth area. Furthermore, Plcd1 and Plcd3 double knockout embryos supplied with a normal placenta by the tetraploid aggregation method survive beyond 14.5 dpc, indicating that the embryonic lethality is caused by a defect in trophoblasts. Ref.5

Sequence similarities

Contains 1 C2 domain.

Contains 3 EF-hand domains.

Contains 1 PH domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Sequence caution

The sequence BAC32829.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD32589.1 differs from that shown. Reason: Intron retention.

The sequence CAM22088.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7857851-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
PRO_0000306822

Regions

Domain65 – 168104PH
Domain178 – 21336EF-hand 1
Domain214 – 24936EF-hand 2
Domain246 – 28136EF-hand 3
Domain333 – 478146PI-PLC X-box
Domain524 – 640117PI-PLC Y-box
Domain643 – 748106C2
Calcium binding191 – 202121 Potential
Calcium binding227 – 238122 Potential
Region69 – 9729Substrate binding By similarity

Sites

Active site3481 By similarity
Active site3931 By similarity
Metal binding3491Calcium 1; catalytic By similarity
Metal binding3781Calcium 1; catalytic By similarity
Metal binding3801Calcium 1; catalytic By similarity
Metal binding4271Calcium 1; catalytic By similarity
Metal binding6791Calcium 2; via carbonyl oxygen By similarity
Metal binding6811Calcium 2 By similarity
Metal binding7051Calcium 2 By similarity
Metal binding7341Calcium 3 By similarity
Metal binding7351Calcium 3; via carbonyl oxygen By similarity
Metal binding7361Calcium 3 By similarity
Binding site4761Substrate By similarity
Binding site4781Substrate By similarity
Binding site5531Substrate By similarity
Binding site5801Substrate By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity
Modified residue4921Phosphoserine Ref.6

Experimental info

Sequence conflict1991S → N in BAE26150. Ref.2
Sequence conflict301 – 3022AK → GE in BAD32589. Ref.1
Sequence conflict3781E → K in BAE26150. Ref.2
Sequence conflict5401D → E in AAH31392. Ref.4
Sequence conflict6591A → T in BAE26150. Ref.2
Sequence conflict6601I → V in BAE26150. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8K2J0 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 8B3DE84FB7A52238

FASTA78588,607
        10         20         30         40         50         60 
MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM GLTEDEDVQA 

        70         80         90        100        110        120 
MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA SKHIFFVQHI EAVREGHQSE 

       130        140        150        160        170        180 
GLRRFGGAFA PACCLTIAFK GRRKNLDLAA PTAEEAQRWV RGLAKLRARL DAMSQRERLD 

       190        200        210        220        230        240 
HWIHSYLHRA DSDQDSKMSF KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE 

       250        260        270        280        290        300 
AFLRRLLKRP ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET 

       310        320        330        340        350        360 
AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT YLTDSQIGGT 

       370        380        390        400        410        420 
SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK ILFRDVIQAV RDHAFTSSPY 

       430        440        450        460        470        480 
PVILSLENHC GLEQQAVMAR HLRSILGDML VTQALDSQNP EELPSPEQLK GRILVKGKKL 

       490        500        510        520        530        540 
PAARSEDGRI LSDREEEEEE EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD 

       550        560        570        580        590        600 
PSPGPPQSCT VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN 

       610        620        630        640        650        660 
SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC PGPPRTTLAI 

       670        680        690        700        710        720 
QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET DYVLNNGFNP CWEQTLQFRL 

       730        740        750        760        770        780 
RAPELVLVRF VVEDYDTTSP NDFVGQSTLP LSSLKQGYRH IHLLSKDGAS LAPATLFVHI 


RIQNS 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic intestine.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adipose tissue and Mammary gland.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Phospholipase C-delta1 and -delta3 are essential in the trophoblast for placental development."
Nakamura Y., Hamada Y., Fujiwara T., Enomoto H., Hiroe T., Tanaka S., Nose M., Nakahara M., Yoshida N., Takenawa T., Fukami K.
Mol. Cell. Biol. 25:10979-10988(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK173311 Transcribed RNA. Translation: BAD32589.1. Sequence problems.
AK046669 mRNA. Translation: BAC32829.1. Different initiation.
AK144950 mRNA. Translation: BAE26150.1.
AL731805 Genomic DNA. Translation: CAM22088.1. Sequence problems.
AL731805 Genomic DNA. Translation: CAM22089.1.
BC031392 mRNA. Translation: AAH31392.1.
RefSeqNP_690026.2. NM_152813.3.
UniGeneMm.264743.

3D structure databases

ProteinModelPortalQ8K2J0.
SMRQ8K2J0. Positions 51-785.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K2J0.

Proteomic databases

PaxDbQ8K2J0.
PRIDEQ8K2J0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
GeneID72469.
KEGGmmu:72469.
UCSCuc007ltf.2. mouse.

Organism-specific databases

CTD113026.
MGIMGI:107451. Plcd3.
RougeSearch...

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00740000114979.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ8K2J0.
KOK05857.
OMAIPRAPSK.
OrthoDBEOG7V49XT.
PhylomeDBQ8K2J0.
TreeFamTF313216.

Gene expression databases

BgeeQ8K2J0.
CleanExMM_PLCD3.
GenevestigatorQ8K2J0.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336294.
PROQ8K2J0.
SOURCESearch...

Entry information

Entry namePLCD3_MOUSE
AccessionPrimary (citable) accession number: Q8K2J0
Secondary accession number(s): A2AHR0 expand/collapse secondary AC list , A2AHR1, Q3UME8, Q69Z55, Q8BL19
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot