Reviewed, UniProtKB/Swiss-Prot P51178 (PLCD1_HUMAN)

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
    Phospholipase C-III
      Short name=PLC-III

Gene names

Name:

PLCD1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
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.
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
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: MGI
Molecular function	GTPase activating protein binding Inferred from physical interaction. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Traceable author statement. Source: ProtInc 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_0000088504
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	616 – 720	105	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
Natural variations
	Natural variant	257	1	R → H: dbSNP rs933135.		VAR_046560
Experimental info
	Sequence conflict	224	1	S → P in AAA73567. Ref.1
	Sequence conflict	264	1	A → T in AAA73567. Ref.1
	Sequence conflict	591	1	G → D in AAA73567. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51178-1 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 6C6FD7F89BA08C83	FASTA	756	85,665
	10 20 30 40 50 60 MDSGRDFLTL HGLQDDEDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR 70 80 90 100 110 120 TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPEDRCFSIV FKDQRNTLDL IAPSPADAQH 130 140 150 160 170 180 WVLGLHKIIH HSGSMDQRQK LQHWIHSCLR KADKNKDNKM SFKELQNFLK ELNIQVDDSY 190 200 210 220 230 240 ARKIFRECDH SQTDSLEDEE IEAFYKMLTQ RVEIDRTFAE AAGSGETLSV DQLVTFLQHQ 250 260 270 280 290 300 QREEAAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFSLA HRRVYQDMGQ 310 320 330 340 350 360 PLSHYLVSSS HNTYLLEDQL AGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF 370 380 390 400 410 420 TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCTLEQQRV MARHLHAILG PMLLNRPLDG 430 440 450 460 470 480 VTNSLPSPEQ LKGKILLKGK KLGGLLPPGG EGGPEATVVS DEDEAAEMED EAVRSRVQHK 490 500 510 520 530 540 PKEDKLRLAQ ELSDMVIYCK SVHFGGFSSP GTPGQAFYEM ASFSENRALR LLQESGNGFV 550 560 570 580 590 600 RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYQ GRFQDNGACG 610 620 630 640 650 660 YVLKPAFLRD PNGTFNPRAL AQGPWWARKR LNIRVISGQQ LPKVNKNKNS IVDPKVTVEI 670 680 690 700 710 720 HGVSRDVASR QTAVITNNGF NPWWDTEFAF EVVVPDLALI RFLVEDYDAS SKNDFIGQST 730 740 750 IPLNSLKQGY RHVHLMSKNG DQHPSATLFV KISLQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis." Cheng H.F., Jiang M.J., Chen C.L., Liu S.M., Wong L.P., Lomasney J.W., King K. J. Biol. Chem. 270:5495-5505(1995) [PubMed: 7890667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Aorta.
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09117 mRNA. Translation: AAA73567.1. CH471055 Genomic DNA. Translation: EAW64507.1. BC050382 mRNA. Translation: AAH50382.2.
IPI	IPI00746030.
PIR	A55943.
RefSeq	NP_001124436.1. NP_006216.2.
UniGene	Hs.80776
3D structure databases
SMR	P51178. Positions 12-130, 158-756.
ModBase	Search...
Protein-protein interaction databases
STRING	P51178.
PTM databases
PhosphoSite	P51178.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00746030.
Proteomic databases
PRIDE	P51178.
Genome annotation databases
Ensembl	ENST00000334661; ENSP00000335600; ENSG00000187091; Homo sapiens. [Genome view]
GeneID	5333.
KEGG	hsa:5333.
Organism-specific databases
CTD	5333.
GeneCards	GC03M038023.
H-InvDB	HIX0003175.
HGNC	HGNC:9060. PLCD1.
HPA	CAB009913. HPA020107. HPA021677.
MIM	602142. gene.
PharmGKB	PA33388.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14621.
HOVERGEN	P51178.
OrthoDB	EOG9HB152.
PhylomeDB	P51178.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000144682-MONOMER.
BRENDA	3.1.4.11. 247.
Gene expression databases
ArrayExpress	P51178.
Bgee	P51178.
CleanEx	HS_PLCD1.
Genevestigator	P51178.
GermOnline	ENSG00000187091. Homo sapiens.
Family and domain databases
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. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR011993. PH_type. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR001849. Pleckstrin_homology. IPR000909. PLipase_C_PInositol-sp_X_dom. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 2 hits. G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 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]
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 Resources
SOURCE	Search...

Entry information

Entry name

PLCD1_HUMAN

Accession

Primary (citable) accession number: P51178
Secondary accession number(s): Q86VN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 23, 2008
Last modified:	February 9, 2010
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.