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Q8SPR7

- PLCD4_PIG

UniProt

Q8SPR7 - PLCD4_PIG

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Protein

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

Gene

PLCD4

Organism
Sus scrofa (Pig)
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).By similarity

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Ca2+By similarityNote: Binds 3 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound to the C2 domain.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei312 – 3121PROSITE-ProRule annotation
Metal bindingi313 – 3131Calcium 1; catalyticBy similarity
Metal bindingi342 – 3421Calcium 1; catalyticBy similarity
Metal bindingi344 – 3441Calcium 1; catalyticBy similarity
Active sitei357 – 3571PROSITE-ProRule annotation
Metal bindingi391 – 3911Calcium 1; catalyticBy similarity
Binding sitei440 – 4401SubstrateBy similarity
Binding sitei442 – 4421SubstrateBy similarity
Binding sitei532 – 5321SubstrateBy similarity
Binding sitei559 – 5591SubstrateBy similarity
Metal bindingi660 – 6601Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi662 – 6621Calcium 2By similarity
Metal bindingi686 – 6861Calcium 2By similarity
Metal bindingi715 – 7151Calcium 3By similarity
Metal bindingi716 – 7161Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi717 – 7171Calcium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi154 – 165121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi190 – 201122PROSITE-ProRule annotationAdd
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 15

Subcellular locationi

Membrane By similarity; 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-KW
  2. membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7727721-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4PRO_0000306827Add
BLAST

Proteomic databases

PaxDbiQ8SPR7.

Interactioni

Subunit structurei

Interacts with GRIP1.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017155.

Structurei

3D structure databases

ProteinModelPortaliQ8SPR7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 131109PHPROSITE-ProRule annotationAdd
BLAST
Domaini141 – 17636EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini177 – 21236EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini210 – 24435EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini297 – 442146PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini503 – 619117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini624 – 729106C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6028Substrate bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi741 – 7444PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi448 – 48336Glu-richAdd
BLAST
Compositional biasi489 – 4968Poly-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.PROSITE-ProRule annotation
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8SPR7.
KOiK05857.
OMAiRDYAFSS.
OrthoDBiEOG7V49XT.
TreeFamiTF313216.

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.
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.

Q8SPR7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLLQGLSA SPGSGLPINQ DLLLMQKGML MRKVRSKSWK KLRYYRLQDD
60 70 80 90 100
GMTVWHARQA GGRAKPSFSI SDVETVRGGH ESELLRNLAE EFPLEQGFTI
110 120 130 140 150
VFHGRRSNLD LVANSVEEAQ VWMQGLQLLV DFVTNMDQQE RLDQWLSDWF
160 170 180 190 200
QRGDKNQDGR MSFGEVQRLL HLMNVEMDQE HAFQLFQTAD TSQSGTLEGE
210 220 230 240 250
EFVEFYKSLT KRAEVQELFE NFSSDGQKLT LLEFVDFLQE EQKEGERASD
260 270 280 290 300
LALELIDRHE PSDSGKLRHV LSLDGFLSYL CSKDGDIFNP TCLPIYQDMT
310 320 330 340 350
QPLNHYFINS SHNTYLVGDQ LCGQSSVEGY IRALKRGCRC VEVDIWDGPN
360 370 380 390 400
GEPVVYHGHT LTSRIPFKDV VAAIAQYAFQ TSDYPVILSL ENHCSWEQQE
410 420 430 440 450
MIAHHLTEIL GEQLLSTTLD GQLPTQLPSP EELRRKILVK GKKLRTLEED
460 470 480 490 500
LEEEEEEPEE SELEGEQEAE LELEAQFESE PQELSPRSKD KKKKVKAILC
510 520 530 540 550
PALSALVVYL KAVSFYSFAH SREHYRFYEI SSFSEAKAKS LIKESGNEFV
560 570 580 590 600
QHNTWQLSRV YPGGLRTDSS NYNPQEFWNA GCQMVAMNMQ TAGLEMDLCD
610 620 630 640 650
GLFRQNAGCG YVLKPDFLRD AQSSFHPERP ISPSKAQTLL IQVISGQQLP
660 670 680 690 700
KVDDSKEGSI VDPLVRVEIF GVRPDTARQE TSYVENNGFN PYWGQTLCFR
710 720 730 740 750
VLVPELALLR FVVKDYDWKS RNDFVGQYTL PWNCMQQGYR HIHLLSKDGI
760 770
SLHPASIFVH ICIREGIEGV ES
Length:772
Mass (Da):88,075
Last modified:June 1, 2002 - v1
Checksum:i86E5706A74247548
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF498759 mRNA. Translation: AAM18122.1.
RefSeqiNP_999217.1. NM_214052.1.
UniGeneiSsc.191.

Genome annotation databases

EnsembliENSSSCT00000017632; ENSSSCP00000017154; ENSSSCG00000016192.
GeneIDi397119.
KEGGissc:397119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF498759 mRNA. Translation: AAM18122.1 .
RefSeqi NP_999217.1. NM_214052.1.
UniGenei Ssc.191.

3D structure databases

ProteinModelPortali Q8SPR7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000017155.

Proteomic databases

PaxDbi Q8SPR7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000017632 ; ENSSSCP00000017154 ; ENSSSCG00000016192 .
GeneIDi 397119.
KEGGi ssc:397119.

Organism-specific databases

CTDi 84812.

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00760000118936.
HOGENOMi HOG000006871.
HOVERGENi HBG053610.
InParanoidi Q8SPR7.
KOi K05857.
OMAi RDYAFSS.
OrthoDBi EOG7V49XT.
TreeFami TF313216.

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.
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. Smith T.P.L.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPLCD4_PIG
AccessioniPrimary (citable) accession number: Q8SPR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 99 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