1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A

Contribute

Send feedback

Read comments (?) or add your own

A5D6R3 (PLD3A_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. History...

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

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-delta-3-A
Phospholipase C-delta-3-A
Short name=PLC-delta-3-A

Gene names

Name:	plcd3a
ORF Names:	zgc:158396

Organism

Danio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 By similarity.
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.
Subcellular location	Membrane; Peripheral membrane protein By similarity. Cytoplasm By similarity.
Domain	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 similarities	Contains 1 C2 domain. Contains 3 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
Cellular component	Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 784

784

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A

PRO_0000306823

Regions

Domain

38 – 149

112

Domain

159 – 194

EF-hand 1

Domain

195 – 230

EF-hand 2

Domain

227 – 262

EF-hand 3

Domain

313 – 458

146

PI-PLC X-box

Domain

506 – 621

116

PI-PLC Y-box

Domain

628 – 733

106

Calcium binding

172 – 183

1 Potential

Calcium binding

208 – 219

2 Potential

Region

48 – 78

Substrate binding By similarity

Sites

Active site

328

By similarity

Active site

373

By similarity

Metal binding

329

Calcium 1; catalytic By similarity

Metal binding

358

Calcium 1; catalytic By similarity

Metal binding

360

Calcium 1; catalytic By similarity

Metal binding

407

Calcium 1; catalytic By similarity

Metal binding

664

Calcium 2; via carbonyl oxygen By similarity

Metal binding

666

Calcium 2 By similarity

Metal binding

690

Calcium 2 By similarity

Metal binding

719

Calcium 3 By similarity

Metal binding

721

Calcium 3 By similarity

Binding site

456

Substrate By similarity

Binding site

458

Substrate By similarity

Binding site

534

Substrate By similarity

Binding site

561

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5D6R3 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 4078823F379343C6
Show »

FASTA

784

89,381

        10         20         30         40         50         60 
MLGRKKNPET VQTESKSVES KTHDPLRRLG VLDDEDVLLM LQGSKMMKVR SQRWRKDRRL 

        70         80         90        100        110        120 
KLLEDCVTVW CESSKTSRKS NRQQTFSVTE VECVREGCQS ECLRRMTDLV PEKNCFTVVF 

       130        140        150        160        170        180 
RGGRKSLDLC CHTQEEAERW VRGIRTLKDR VSNMSQKEKL DHWIRGYLRR ADQNQDGKMS 

       190        200        210        220        230        240 
YDEVKHLLQL INIDLNEQYA RTLFKKCDRS CDGRLDHVEI EEFCREMMRR PELDAVFRHY 

       250        260        270        280        290        300 
SGNGCVLTTL ELRDFLGDQG EDASLVHAKS LIQTFELNDW AQKNLFMTQN GFTMYMLSKE 

       310        320        330        340        350        360 
NDVFNPDHTH VYQDMSKPLA HYYISSSHNT YLTKDQVTSA SSTEPYIRAL NQGCRCVELD 

       370        380        390        400        410        420 
CWDGDKGEPI IYHGHTLTSK VLFKEVIETI AQYAFKASPY PLILSLENHC SVEQQAIMAQ 

       430        440        450        460        470        480 
QLQSILGKKL LAKPLSDLPL KQLPSPEELK GRILLKGKKL NGLLGKTESW TSFTNSSDEE 

       490        500        510        520        530        540 
SVAGGNKKES KKDLARSAST KLSPELSDLV VYCQSVPFSG FETANQRPPS VITSFSENEA 

       550        560        570        580        590        600 
LKLIKDSGKL FVRNNSRQLS RIYPSAQRLQ SSNFDPQDMW NAGCQMVALN FQTPGEQMDL 

       610        620        630        640        650        660 
NQGRFLPNGR CGYVLKPEFL CDPKSDFDPE NTGGGPGHIP TQLTIRVISA QQLPKINTDK 

       670        680        690        700        710        720 
PNSIVDPQVW VEIHGVSIDK ARAKTQRIDN NGFNPRWDCT VSFQLQLPEL ALVRFMVEDH 

       730        740        750        760        770        780 
DHKSKNDFIG QFTLPFTSLR TGYRHVHLLK ADGSTLSPAT LFIHVKVVRR GVHIKTVSER 


IGKA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[2]	"Duplication of phospholipase C-delta gene family in fish genomes." Kim M.S., Seo J.S., Ahn S.J., Kim N.Y., Je J.E., Sung J.H., Lee H.H., Chung J.K. Genomics 92:366-371(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENE DUPLICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC139849 mRNA. Translation: AAI39850.1.
IPI	IPI00483414.
RefSeq	NP_001092893.1. NM_001099423.1.
UniGene	Dr.50929.
3D structure databases
ProteinModelPortal	A5D6R3.
SMR	A5D6R3. Positions 219-768.
ModBase	Search...
Protein-protein interaction databases
STRING	7955.ENSDARP00000093449.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSDART00000102674; ENSDARP00000093449; ENSDARG00000052957.
GeneID	569040.
KEGG	dre:569040.
Organism-specific databases
CTD	569040.
ZFIN	ZDB-GENE-070620-1. plcd3a.
Phylogenomic databases
eggNOG	NOG149692.
GeneTree	ENSGT00700000104181.
HOGENOM	HOG000006871.
KO	K05857.
OMA	KEELEWA.
OrthoDB	EOG45QHCM.
Gene expression databases
Bgee	A5D6R3.
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	20889471.

Entry information

Entry name

PLD3A_DANRE

Accession

Primary (citable) accession number: A5D6R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents