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Q8R3B1

- PLCD1_MOUSE

UniProt

Q8R3B1 - PLCD1_MOUSE

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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1

Gene
Plcd1, Plcd
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei311 – 3111 By similarity
Metal bindingi312 – 3121Calcium 1; catalytic By similarity
Metal bindingi341 – 3411Calcium 1; catalytic By similarity
Metal bindingi343 – 3431Calcium 1; catalytic By similarity
Active sitei356 – 3561 By similarity
Metal bindingi390 – 3901Calcium 1; catalytic By similarity
Binding sitei438 – 4381Substrate By similarity
Binding sitei440 – 4401Substrate By similarity
Binding sitei522 – 5221Substrate By similarity
Binding sitei549 – 5491Substrate By similarity
Metal bindingi651 – 6511Calcium 2; via carbonyl oxygen By similarity
Metal bindingi653 – 6531Calcium 2 By similarity
Metal bindingi677 – 6771Calcium 2 By similarity
Metal bindingi706 – 7061Calcium 3 By similarity
Metal bindingi707 – 7071Calcium 3; via carbonyl oxygen By similarity
Metal bindingi708 – 7081Calcium 3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi153 – 164121 Reviewed predictionAdd
BLAST
Calcium bindingi189 – 200122 Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidic acid binding Source: MGI
  3. phosphatidylinositol phosphate binding Source: MGI
  4. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  5. phosphatidylserine binding Source: MGI
  6. phospholipase C activity Source: MGI
  7. protein binding Source: MGI
  8. 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

BRENDAi3.1.4.11. 3474.
ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-delta-1
Phospholipase C-delta-1
Short name:
PLC-delta-1
Gene namesi
Name:Plcd1
Synonyms:Plcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:97614. Plcd1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
Complete GO annotation...

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 – 7567561-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1PRO_0000088505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi191 – 1911O-linked (GlcNAc) By similarity
Glycosylationi193 – 1931O-linked (GlcNAc) By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8R3B1.
PaxDbiQ8R3B1.
PRIDEiQ8R3B1.

PTM databases

PhosphoSiteiQ8R3B1.

Expressioni

Tissue specificityi

Highly expressed in brain, heart, lung, epididymis and testis. Detected at lower levels in kidney and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ8R3B1.
CleanExiMM_PLCD1.
GenevestigatoriQ8R3B1.

Structurei

3D structure databases

ProteinModelPortaliQ8R3B1.
SMRiQ8R3B1. Positions 12-129, 158-756.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 130110PHAdd
BLAST
Domaini140 – 17536EF-hand 1Add
BLAST
Domaini176 – 21136EF-hand 2Add
BLAST
Domaini296 – 440145PI-PLC X-boxAdd
BLAST
Domaini492 – 609118PI-PLC Y-boxAdd
BLAST
Domaini630 – 72091C2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5728Substrate binding By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.
Contains 2 EF-hand domains.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00740000114979.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ9Z1B4.
KOiK05857.
OMAiTSGQAFY.
OrthoDBiEOG7V49XT.
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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028391. PLC-delta1.
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:SF80. PTHR10336:SF80. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00169. PH. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00054. EFh. 2 hits.
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.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R3B1-1 [UniParc]FASTAAdd to Basket

« Hide

MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT    50
IWQESRKVMR SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV 100
FKDQRNTLDL IAPSPADVQH WVQGLRKIID RSGSMDQRQK LQHWIHSCLR 150
KADKNKDNKM NFKEVKDFLK ELNVQVDDSY ARKIFRECDH SQTDSLEDEE 200
IETFYRMLTQ RAEIDRAFAE AAGSAETLSV EKLVTFLQHQ QREEEAGPAL 250
ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMNQ 300
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ 350
EPIIYHGYTF TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV 400
MAHHLRAILG PMLLDQPLDG VTTSLPSPEQ LKEKILLKGK KLGGLLPAGG 450
ENGPEATDVS DEDEAAEMED EAVRSQVQHK PKEDKLKLVP ELSDMVIYCK 500
SVHFGGFSSP STSGQAFYEM ASFSESRALR LLQESGNSFV RHNVGHLSRI 550
YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG 600
YVLKPAFLRD PDTTFNSRAL TQGPWWAPKK LRVWIISGQQ LPKVNKNKNS 650
IVDPKVIVEI HGVGQDVASR QTAVITNNGF NPRWDTEFEF VVAVPDLALV 700
RFMVEDYDSS SKNDFIGQST IPWNSLKQGY RHVHLLSKNG DLHPSATLFV 750
KISIQD 756
Length:756
Mass (Da):85,873
Last modified:July 27, 2011 - v2
Checksum:i71F17810F9B0B938
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121A → V in AAH25798. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF133125 mRNA. Translation: AAD32616.1.
U85711 mRNA. Translation: AAD00570.1.
AK028749 mRNA. Translation: BAC26096.1.
AK082890 mRNA. Translation: BAC38671.1.
CH466587 Genomic DNA. Translation: EDL09242.1.
BC025798 mRNA. Translation: AAH25798.1.
CCDSiCCDS23607.1.
RefSeqiNP_062650.1. NM_019676.3.
UniGeneiMm.23963.

Genome annotation databases

EnsembliENSMUST00000010804; ENSMUSP00000010804; ENSMUSG00000010660.
GeneIDi18799.
KEGGimmu:18799.
UCSCiuc009saf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF133125 mRNA. Translation: AAD32616.1 .
U85711 mRNA. Translation: AAD00570.1 .
AK028749 mRNA. Translation: BAC26096.1 .
AK082890 mRNA. Translation: BAC38671.1 .
CH466587 Genomic DNA. Translation: EDL09242.1 .
BC025798 mRNA. Translation: AAH25798.1 .
CCDSi CCDS23607.1.
RefSeqi NP_062650.1. NM_019676.3.
UniGenei Mm.23963.

3D structure databases

ProteinModelPortali Q8R3B1.
SMRi Q8R3B1. Positions 12-129, 158-756.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8R3B1.

Proteomic databases

MaxQBi Q8R3B1.
PaxDbi Q8R3B1.
PRIDEi Q8R3B1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000010804 ; ENSMUSP00000010804 ; ENSMUSG00000010660 .
GeneIDi 18799.
KEGGi mmu:18799.
UCSCi uc009saf.1. mouse.

Organism-specific databases

CTDi 5333.
MGIi MGI:97614. Plcd1.

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00740000114979.
HOGENOMi HOG000006871.
HOVERGENi HBG053610.
InParanoidi Q9Z1B4.
KOi K05857.
OMAi TSGQAFY.
OrthoDBi EOG7V49XT.
TreeFami TF313216.

Enzyme and pathway databases

BRENDAi 3.1.4.11. 3474.
Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

NextBioi 295096.
PROi Q8R3B1.
SOURCEi Search...

Gene expression databases

Bgeei Q8R3B1.
CleanExi MM_PLCD1.
Genevestigatori Q8R3B1.

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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR028391. PLC-delta1.
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:SF80. PTHR10336:SF80. 1 hit.
Pfami PF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00169. PH. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view ]
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00054. EFh. 2 hits.
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.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression analysis of a mouse phospholipase C-delta1."
    Lee W.K., Kim J.K., Seo M.S., Cha J.H., Lee K.J., Rha H.K., Min D.S., Jo Y.H., Lee K.H.
    Biochem. Biophys. Res. Commun. 261:393-399(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Brain.
  2. Wu K., Bai J., Marks D.L., Pagano R.E.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss.
  3. "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: Embryo and Skin.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "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.

Entry informationi

Entry nameiPLCD1_MOUSE
AccessioniPrimary (citable) accession number: Q8R3B1
Secondary accession number(s): Q9Z1B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 125 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