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Q8K2J0

- PLCD3_MOUSE

UniProt

Q8K2J0 - PLCD3_MOUSE

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Protein
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
Gene
Plcd3, Kiaa1964
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei348 – 3481 By similarity
Metal bindingi349 – 3491Calcium 1; catalytic By similarity
Metal bindingi378 – 3781Calcium 1; catalytic By similarity
Metal bindingi380 – 3801Calcium 1; catalytic By similarity
Active sitei393 – 3931 By similarity
Metal bindingi427 – 4271Calcium 1; catalytic By similarity
Binding sitei476 – 4761Substrate By similarity
Binding sitei478 – 4781Substrate By similarity
Binding sitei553 – 5531Substrate By similarity
Binding sitei580 – 5801Substrate By similarity
Metal bindingi679 – 6791Calcium 2; via carbonyl oxygen By similarity
Metal bindingi681 – 6811Calcium 2 By similarity
Metal bindingi705 – 7051Calcium 2 By similarity
Metal bindingi734 – 7341Calcium 3 By similarity
Metal bindingi735 – 7351Calcium 3; via carbonyl oxygen By similarity
Metal bindingi736 – 7361Calcium 3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi191 – 202121 Reviewed prediction
Add
BLAST
Calcium bindingi227 – 238122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. angiogenesis Source: MGI
  2. intracellular signal transduction Source: InterPro
  3. labyrinthine layer blood vessel development Source: MGI
  4. lipid catabolic process Source: UniProtKB-KW
  5. regulation of cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Plcd3
Synonyms:Kiaa1964
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:107451. Plcd3.

Subcellular locationi

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

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB-SubCell
  2. cytosol Source: Ensembl
  3. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7857851-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
PRO_0000306822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011Phosphoserine By similarity
Modified residuei492 – 4921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8K2J0.
PRIDEiQ8K2J0.

PTM databases

PhosphoSiteiQ8K2J0.

Expressioni

Gene expression databases

BgeeiQ8K2J0.
CleanExiMM_PLCD3.
GenevestigatoriQ8K2J0.

Structurei

3D structure databases

ProteinModelPortaliQ8K2J0.
SMRiQ8K2J0. Positions 51-784.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 168104PH
Add
BLAST
Domaini178 – 21336EF-hand 1
Add
BLAST
Domaini214 – 24936EF-hand 2
Add
BLAST
Domaini246 – 28136EF-hand 3
Add
BLAST
Domaini333 – 478146PI-PLC X-box
Add
BLAST
Domaini524 – 640117PI-PLC Y-box
Add
BLAST
Domaini643 – 748106C2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 9729Substrate binding By similarity
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 C2 domain.
Contains 3 EF-hand domains.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00740000114979.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8K2J0.
KOiK05857.
OMAiHWGQTLQ.
OrthoDBiEOG7V49XT.
PhylomeDBiQ8K2J0.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2J0-1 [UniParc]FASTAAdd to Basket

« Hide

MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM    50
GLTEDEDVQA MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA 100
SKHIFFVQHI EAVREGHQSE GLRRFGGAFA PACCLTIAFK GRRKNLDLAA 150
PTAEEAQRWV RGLAKLRARL DAMSQRERLD HWIHSYLHRA DSDQDSKMSF 200
KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE AFLRRLLKRP 250
ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET 300
AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT 350
YLTDSQIGGT SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK 400
ILFRDVIQAV RDHAFTSSPY PVILSLENHC GLEQQAVMAR HLRSILGDML 450
VTQALDSQNP EELPSPEQLK GRILVKGKKL PAARSEDGRI LSDREEEEEE 500
EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD PSPGPPQSCT 550
VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN 600
SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC 650
PGPPRTTLAI QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET 700
DYVLNNGFNP CWEQTLQFRL RAPELVLVRF VVEDYDTTSP NDFVGQSTLP 750
LSSLKQGYRH IHLLSKDGAS LAPATLFVHI RIQNS 785
Length:785
Mass (Da):88,607
Last modified:October 2, 2007 - v2
Checksum:i8B3DE84FB7A52238
GO

Sequence cautioni

The sequence BAD32589.1 differs from that shown. Reason: Intron retention.
The sequence BAC32829.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAM22088.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991S → N in BAE26150. 1 Publication
Sequence conflicti301 – 3022AK → GE in BAD32589. 1 Publication
Sequence conflicti378 – 3781E → K in BAE26150. 1 Publication
Sequence conflicti540 – 5401D → E in AAH31392. 1 Publication
Sequence conflicti659 – 6591A → T in BAE26150. 1 Publication
Sequence conflicti660 – 6601I → V in BAE26150. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS25512.1.
RefSeqiNP_690026.2. NM_152813.3.
UniGeneiMm.264743.

Genome annotation databases

EnsembliENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
GeneIDi72469.
KEGGimmu:72469.
UCSCiuc007ltf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS25512.1.
RefSeqi NP_690026.2. NM_152813.3.
UniGenei Mm.264743.

3D structure databases

ProteinModelPortali Q8K2J0.
SMRi Q8K2J0. Positions 51-784.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8K2J0.

Proteomic databases

PaxDbi Q8K2J0.
PRIDEi Q8K2J0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000103077 ; ENSMUSP00000099366 ; ENSMUSG00000020937 .
GeneIDi 72469.
KEGGi mmu:72469.
UCSCi uc007ltf.2. mouse.

Organism-specific databases

CTDi 113026.
MGIi MGI:107451. Plcd3.
Rougei Search...

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00740000114979.
HOGENOMi HOG000006871.
HOVERGENi HBG053610.
InParanoidi Q8K2J0.
KOi K05857.
OMAi HWGQTLQ.
OrthoDBi EOG7V49XT.
PhylomeDBi Q8K2J0.
TreeFami TF313216.

Enzyme and pathway databases

Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

NextBioi 336294.
PROi Q8K2J0.
SOURCEi Search...

Gene expression databases

Bgeei Q8K2J0.
CleanExi MM_PLCD3.
Genevestigatori Q8K2J0.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
Pfami PF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view ]
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiPLCD3_MOUSE
AccessioniPrimary (citable) accession number: Q8K2J0
Secondary accession number(s): A2AHR0
, A2AHR1, Q3UME8, Q69Z55, Q8BL19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: September 3, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi