Q8R3B1 (PLCD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Plcd1
Synonyms:	Plcd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. Ref.6
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.
Tissue specificity	Highly expressed in brain, heart, lung, epididymis and testis. Detected at lower levels in kidney and skeletal muscle. Ref.1
Disruption phenotype	Mice lacking Plcd1 and Plcd3 die at embryonic day 11.5 (E11.5) to E13.5 and 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 E14.5, clearly indicating that the embryonic lethality is caused by a defect in trophoblasts. Ref.6
Sequence similarities	Contains 1 C2 domain. Contains 2 EF-hand domains. Contains 1 PH domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from genetic interaction Ref.6. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro labyrinthine layer blood vessel development Inferred from genetic interaction Ref.6. Source: MGI lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell proliferation Inferred from genetic interaction Ref.6. Source: MGI
Cellular_component	cytosol Inferred from direct assay PubMed 15899900. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 756	756	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1		PRO_0000088505
Regions
	Domain	21 – 130	110	PH
	Domain	140 – 175	36	EF-hand 1
	Domain	176 – 211	36	EF-hand 2
	Domain	296 – 440	145	PI-PLC X-box
	Domain	492 – 609	118	PI-PLC Y-box
	Domain	630 – 720	91	C2
	Calcium binding	153 – 164	12	1 Potential
	Calcium binding	189 – 200	12	2 Potential
	Region	30 – 57	28	Substrate binding By similarity
Sites
	Active site	311	1	By similarity
	Active site	356	1	By similarity
	Metal binding	312	1	Calcium 1; catalytic By similarity
	Metal binding	341	1	Calcium 1; catalytic By similarity
	Metal binding	343	1	Calcium 1; catalytic By similarity
	Metal binding	390	1	Calcium 1; catalytic By similarity
	Metal binding	651	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	653	1	Calcium 2 By similarity
	Metal binding	677	1	Calcium 2 By similarity
	Metal binding	706	1	Calcium 3 By similarity
	Metal binding	707	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	708	1	Calcium 3 By similarity
	Binding site	438	1	Substrate By similarity
	Binding site	440	1	Substrate By similarity
	Binding site	522	1	Substrate By similarity
	Binding site	549	1	Substrate By similarity
Experimental info
	Sequence conflict	212	1	A → V in AAH25798. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8R3B1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 71F17810F9B0B938	FASTA	756	85,873
	10 20 30 40 50 60 MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR 70 80 90 100 110 120 SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADVQH 130 140 150 160 170 180 WVQGLRKIID RSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKEVKDFLK ELNVQVDDSY 190 200 210 220 230 240 ARKIFRECDH SQTDSLEDEE IETFYRMLTQ RAEIDRAFAE AAGSAETLSV EKLVTFLQHQ 250 260 270 280 290 300 QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMNQ 310 320 330 340 350 360 PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF 370 380 390 400 410 420 TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MAHHLRAILG PMLLDQPLDG 430 440 450 460 470 480 VTTSLPSPEQ LKEKILLKGK KLGGLLPAGG ENGPEATDVS DEDEAAEMED EAVRSQVQHK 490 500 510 520 530 540 PKEDKLKLVP ELSDMVIYCK SVHFGGFSSP STSGQAFYEM ASFSESRALR LLQESGNSFV 550 560 570 580 590 600 RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG 610 620 630 640 650 660 YVLKPAFLRD PDTTFNSRAL TQGPWWAPKK LRVWIISGQQ LPKVNKNKNS IVDPKVIVEI 670 680 690 700 710 720 HGVGQDVASR QTAVITNNGF NPRWDTEFEF VVAVPDLALV RFMVEDYDSS SKNDFIGQST 730 740 750 IPWNSLKQGY RHVHLLSKNG DLHPSATLFV KISIQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00321515.
RefSeq	NP_062650.1. NM_019676.2.
UniGene	Mm.23963.
3D structure databases
ProteinModelPortal	Q8R3B1.
SMR	Q8R3B1. Positions 12-129, 158-756.
ModBase	Search...
PTM databases
PhosphoSite	Q8R3B1.
Proteomic databases
PaxDb	Q8R3B1.
PRIDE	Q8R3B1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000010804; ENSMUSP00000010804; ENSMUSG00000010660.
GeneID	18799.
KEGG	mmu:18799.
Organism-specific databases
CTD	5333.
MGI	MGI:97614. Plcd1.
Phylogenomic databases
eggNOG	NOG149692.
GeneTree	ENSGT00700000104181.
HOGENOM	HOG000006871.
HOVERGEN	HBG053610.
InParanoid	Q9Z1B4.
KO	K05857.
OMA	MGHRTEG.
OrthoDB	EOG4H19V6.
Enzyme and pathway databases
BRENDA	3.1.4.11. 3474.
Gene expression databases
Bgee	Q8R3B1.
CleanEx	MM_PLCD1.
Genevestigator	Q8R3B1.
GermOnline	ENSMUSG00000010660. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 2 hits. 2.30.29.30. 1 hit. 3.20.20.190. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR011993. PH_like_dom. IPR001192. Pinositol_PLipase_C. 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]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00169. PH. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00054. EFh. 2 hits. SM00233. PH. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	295096.
SOURCE	Search...

Entry information

Entry name

PLCD1_MOUSE

Accession

Primary (citable) accession number: Q8R3B1
Secondary accession number(s): Q9Z1B4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program