SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5RET0

- PLCD4_PONAB

UniProt

Q5RET0 - PLCD4_PONAB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
Gene
PLCD4
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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. Required for acrosome reaction in sperm during fertilization, probably by acting as an important enzyme for intracellular Ca2+ mobilization in the zona pellucida-induced acrosome reaction. May play a role in cell growth. Modulates the liver regeneration in cooperation with nuclear PKC. Overexpression up-regulates the Erk signaling pathway and proliferation By similarity.

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 sitei305 – 3051 By similarity
Metal bindingi306 – 3061Calcium 1; catalytic By similarity
Metal bindingi335 – 3351Calcium 1; catalytic By similarity
Metal bindingi337 – 3371Calcium 1; catalytic By similarity
Active sitei350 – 3501 By similarity
Metal bindingi384 – 3841Calcium 1; catalytic By similarity
Binding sitei433 – 4331Substrate By similarity
Binding sitei435 – 4351Substrate By similarity
Binding sitei522 – 5221Substrate By similarity
Binding sitei549 – 5491Substrate By similarity
Metal bindingi650 – 6501Calcium 2; via carbonyl oxygen By similarity
Metal bindingi652 – 6521Calcium 2 By similarity
Metal bindingi676 – 6761Calcium 2 By similarity
Metal bindingi705 – 7051Calcium 3 By similarity
Metal bindingi706 – 7061Calcium 3; via carbonyl oxygen By similarity
Metal bindingi707 – 7071Calcium 3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi147 – 158121 Reviewed prediction
Add
BLAST
Calcium bindingi183 – 194122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. acrosome reaction Source: InterPro
  2. intracellular signal transduction Source: InterPro
  3. lipid catabolic process Source: UniProtKB-KW
  4. phosphatidylinositol metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-delta-4
Phospholipase C-delta-4
Short name:
PLC-delta-4
Gene namesi
Name:PLCD4
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Cytoplasm By similarity. Endoplasmic reticulum By similarity
Note: Localizes primarily to intracellular membranes mostly to the endoplasmic reticulum By similarity.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7627621-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
PRO_0000306828Add
BLAST

Interactioni

Subunit structurei

Interacts with GRIP1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RET0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 124109PH
Add
BLAST
Domaini134 – 16936EF-hand 1
Add
BLAST
Domaini170 – 20536EF-hand 2
Add
BLAST
Domaini203 – 23735EF-hand 3
Add
BLAST
Domaini290 – 435146PI-PLC X-box
Add
BLAST
Domaini493 – 609117PI-PLC Y-box
Add
BLAST
Domaini614 – 719106C2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 5328Substrate binding By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi731 – 7344PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi440 – 47334Glu-rich
Add
BLAST
Compositional biasi479 – 4868Poly-Lys

Domaini

The PDZ-binding motif mediates the interaction with GRIP1 By similarity.
The C2 domain mediates pre-localization to the membrane prior to Ca2+ import and non-selective Ca2+-mediated targeting to various cellular membranes By similarity.
The PH domain is not a critical determinant of the membrane localization By similarity.

Sequence similaritiesi

Contains 1 C2 domain.
Contains 3 EF-hand domains.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG053610.
KOiK05857.

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.
IPR028387. PLC-delta4.
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:SF31. PTHR10336:SF31. 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. 3 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. 3 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5RET0-1 [UniParc]FASTAAdd to Basket

« Hide

MASLLQDQLT TDQDLLLMQE GMPMRKVRSK SWKKLRYFRL QNDGMTVWHA    50
RQARGSAKPS FSISDVDTIR NGHDSELLRS LAEELPLEQG FTVVFHGRRS 100
NLDLVANSVE EAQMWMRGLQ LLVDLVTSMD HQERLDQWLS DWFQRGDKNQ 150
DGKMSFQEVQ RLLHLMNVEM DQEYAFSLFQ AADTSQSGTL EGEEFVQFYK 200
ALTKRAEVQE LFESFSADGQ KLTLLEFLDF LREEQKERDC TSELALELID 250
HYEPSDSGKL RHVLSMDGFL SYLCSKDGDI FNPACLPIYQ DMTQPLNHYF 300
ICSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDVWD GPSGEPVVYH 350
GHTLTSRILF KDVVATVAQY AFQTSDYPVI LSLETHCSWE QQQTMARHLT 400
EILGEQLLST TLDGVLPTQL PSPEELRRRI LVKGKKLTLE EDLEYEEEEA 450
EPELEESELA LESQFETEPE PQEQNLQSKD KKKKSKPILC PALSSLVIYL 500
KSVSFRSFTH SKEHYHFYEI SSFSETKAER LIKEAGNEFV QHNTWQLSRV 550
YPSGLRTDSS NYNPQELWNA GCQMVAMNMQ TAGLEMDICD GHFRQNGGCG 600
YVLKPDFLRD IQSSFHPERP ISPFKAQTLL IQVISGQQLP KVDKTKEGSI 650
VDPLVKVQIF GVRLDTARQE TNYVENNGFN PYWGETLCFR VLVPELAMLR 700
FVVMDYDWKS RNDFIGQYTL PWTCMQQGYR HIHLLSKVGI SLRPASIFVY 750
ICIQEDLEGD ES 762
Length:762
Mass (Da):87,625
Last modified:December 21, 2004 - v1
Checksum:i89B03949861987C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857436 mRNA. Translation: CAH89727.1.
RefSeqiNP_001124787.1. NM_001131315.1.
UniGeneiPab.12236.

Genome annotation databases

GeneIDi100171640.
KEGGipon:100171640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857436 mRNA. Translation: CAH89727.1 .
RefSeqi NP_001124787.1. NM_001131315.1.
UniGenei Pab.12236.

3D structure databases

ProteinModelPortali Q5RET0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171640.
KEGGi pon:100171640.

Organism-specific databases

CTDi 84812.

Phylogenomic databases

HOVERGENi HBG053610.
KOi K05857.

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.
IPR028387. PLC-delta4.
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:SF31. PTHR10336:SF31. 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. 3 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. 3 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiPLCD4_PONAB
AccessioniPrimary (citable) accession number: Q5RET0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 74 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi