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

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Reviewed, UniProtKB/Swiss-Prot P10895 (PLCD1_BOVIN)

Last modified September 22, 2009. Version 99. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Phospholipase C-delta-1
      Short name=PLC-delta-1
    PLC-III

Gene names

Name:

PLCD1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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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.

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Ontologies

Keywords
Biological process	Lipid degradation
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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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_0000088503

Regions

Domain

21 – 130

110

Domain

140 – 175

EF-hand 1

Domain

176 – 211

EF-hand 2

Domain

296 – 440

145

PI-PLC X-box

Domain

492 – 609

118

PI-PLC Y-box

Domain

628 – 720

Calcium binding

153 – 164

1 Potential

Calcium binding

189 – 200

2 Potential

Sites

Active site

311

By similarity

Active site

356

By similarity

Metal binding

312

Calcium 1; catalytic By similarity

Metal binding

341

Calcium 1; catalytic By similarity

Metal binding

343

Calcium 1; catalytic By similarity

Metal binding

390

Calcium 1; catalytic By similarity

Metal binding

651

Calcium 2; via carbonyl oxygen By similarity

Metal binding

653

Calcium 2 By similarity

Metal binding

677

Calcium 2 By similarity

Metal binding

706

Calcium 3 By similarity

Metal binding

707

Calcium 3; via carbonyl oxygen By similarity

Metal binding

708

Calcium 3 By similarity

Binding site

438

Substrate By similarity

Binding site

440

Substrate By similarity

Binding site

522

Substrate By similarity

Binding site

549

Substrate By similarity

Experimental info

Sequence conflict

291

H → D in AAA30710. Ref.2

Sequence conflict

664 – 665

SR → TG in AAA30710. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P10895-1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: EBA47E8BAEE2D398
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FASTA

756

86,073

        10         20         30         40         50         60 
MDSGRDFLTL HGLQDDKDLQ ALLKGGQLLK VKSNSWRRER FYKLQEDCKT IWQESRKVMR 

        70         80         90        100        110        120 
TPESQLFSIE DIQEVRMGHR TEGLEKFARD VPENRCFSIV FKDQRNTLDL IAPSPADAQH 

       130        140        150        160        170        180 
WVQGLGKIIH HSGSMDQQQK LRHWIHSCLR KADKNKDNKM SFKELQNFLK ELNIQVDDSY 

       190        200        210        220        230        240 
ARKIFKECDH SQTDSLEDEE IETFYKILTQ RKEIDRTFEE ATGSKETLSV DQLVTFLQHQ 

       250        260        270        280        290        300 
QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGSAFDLA HRRVYQDMDQ 

       310        320        330        340        350        360 
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF 

       370        380        390        400        410        420 
TSKILFCDVV RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MARHLRTLLG PMLLDRPLDG 

       430        440        450        460        470        480 
VVTSLPSPEQ LRGKILLKGK KLGGLFPPGG EGGPEATVVS DEDEAAEMED EAVRSQVQHK 

       490        500        510        520        530        540 
SKEDKLRLAK ELSDMVIYCK SVHFRGFPSS GTSGQAFYEM SSFSENRALR LLQESGNSFV 

       550        560        570        580        590        600 
RHNVNHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGSEMDVYQ GRFLDNGACG 

       610        620        630        640        650        660 
YVLKPAFLRD PNSTFNSRAL AHGPWWTPKR LNVRVISGQQ LPKVNKNKNS IVDPKVTVEI 

       670        680        690        700        710        720 
HGVSRDVASR QTAVVTNNGF NPWWDTELEF EVAVPELALV RFVVEDYDAS SKNDFIGQST 

       730        740        750 
IPLKSLKQGY RHIHLLSKNG DQHPSATLFV KVALQD

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal skin.
[2]	"Cloning and sequence of multiple forms of phospholipase C." Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G. Cell 54:161-169(1988) [PubMed: 3390863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-756.

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Cross-references

Sequence databases
	BC133304 mRNA. Translation: AAI33305.1. M20638 mRNA. Translation: AAA30710.1.
IPI	IPI00839940.
PIR	C28821.
RefSeq	NP_001075045.1. XP_001256610.2.
UniGene	Bt.4877 Bt.90659
3D structure databases
HSSP	HSSP built from PDB template 1MAI based on UniProtKB P10688.
SMR	P10895. Positions 1-69, 97-695.
ModBase	Search...
Protein-protein interaction databases
STRING	P10895.
Genome annotation databases
Ensembl	ENSBTAT00000052073; ENSBTAP00000049395; ENSBTAG00000037726; Bos taurus. [Genome view] ENSBTAT00000054727; ENSBTAP00000050229; ENSBTAG00000038587; Bos taurus. [Genome view]
GeneID	281986. 790012.
KEGG	bta:281986. bta:790012.
Organism-specific databases
CTD	281986.
Phylogenomic databases
HOVERGEN	P10895.
Enzyme and pathway databases
BRENDA	3.1.4.11. 251.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR011992. EF-Hand_type. IPR018247. EF_HAND_1_Ca_BS. IPR018249. EF_HAND_2. IPR011993. PH_type. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR000909. Phospholipase_C_Pinositol-sp_X. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR001849. Pleckstrin_homology. [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. PF00169. PH. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
ProDom	PD001202. PI_PLC_Y. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00239. C2. 1 hit. 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...

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Entry information

Entry name

PLCD1_BOVIN

Accession

Primary (citable) accession number: P10895
Secondary accession number(s): A2VDM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 13, 2007
Last modified:	September 22, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents