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Q8K3R3

- PLCD4_MOUSE

UniProt

Q8K3R3 - PLCD4_MOUSE

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Protein

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

Gene

Plcd4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.3 Publications

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 sitei305 – 3051PROSITE-ProRule annotation
Metal bindingi306 – 3061Calcium 1; catalyticBy similarity
Metal bindingi335 – 3351Calcium 1; catalyticBy similarity
Metal bindingi337 – 3371Calcium 1; catalyticBy similarity
Active sitei350 – 3501PROSITE-ProRule annotation
Metal bindingi384 – 3841Calcium 1; catalyticBy similarity
Binding sitei433 – 4331SubstrateBy similarity
Binding sitei435 – 4351SubstrateBy similarity
Binding sitei567 – 5671SubstrateBy similarity
Binding sitei594 – 5941SubstrateBy similarity
Metal bindingi697 – 6971Calcium 2By similarity
Metal bindingi721 – 7211Calcium 2By similarity
Metal bindingi750 – 7501Calcium 3By similarity
Metal bindingi751 – 7511Calcium 3; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi147 – 158121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi183 – 194122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. acrosome reaction Source: MGI
  2. intracellular signal transduction Source: InterPro
  3. lipid catabolic process Source: UniProtKB-KW
  4. phosphatidylinositol metabolic process Source: MGI
  5. signal transduction Source: MGI
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
Synonyms:Plcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107469. Plcd4.

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. intracellular Source: MGI
  3. membrane Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are either sterile or produce few small litters. In these mice, fewer eggs become activated and the Ca2+ transients associated with fertilization are absent or delayed. Sperm are unable to initiate the acrosome reaction.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8078071-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4PRO_0000306826Add
BLAST

Proteomic databases

MaxQBiQ8K3R3.
PaxDbiQ8K3R3.
PRIDEiQ8K3R3.

PTM databases

PhosphoSiteiQ8K3R3.

Expressioni

Inductioni

By treatment with growth factors such as bradykinin, lysophosphatidic acid, and Ca2+ ionophore in addition to serum.1 Publication

Gene expression databases

BgeeiQ8K3R3.
CleanExiMM_PLCD4.
ExpressionAtlasiQ8K3R3. baseline and differential.
GenevestigatoriQ8K3R3.

Interactioni

Subunit structurei

Interacts with GRIP1.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8K3R3.
SMRiQ8K3R3. Positions 9-453, 536-800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 124109PHPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 16936EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini170 – 20536EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 23735EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini290 – 435146PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini538 – 654117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini659 – 764106C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 5328Substrate bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi776 – 7794PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi445 – 45612Poly-GluAdd
BLAST

Domaini

The PDZ-binding motif mediates the interaction with GRIP1.
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.
InParanoidiQ8K3R3.
KOiK05857.
OMAiRDYAFSS.
OrthoDBiEOG7V49XT.
PhylomeDBiQ8K3R3.
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.
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. 2 hits.
PROSITEiPS50004. C2. 1 hit.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K3R3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG
60 70 80 90 100
SQPESMPKPT FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP
110 120 130 140 150
NLDLVANSVE EAQIWMRGLQ LLVDLVASMD HQEQMDQMLN EWFQQADRNQ
160 170 180 190 200
DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ EADVTQSDDL GSEEFVQFYK
210 220 230 240 250
ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH APDLALELID
260 270 280 290 300
RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY
310 320 330 340 350
INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH
360 370 380 390 400
GHTLTSRILF KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT
410 420 430 440 450
EILGEQLLRN TLEGLLVDSM PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE
460 470 480 490 500
EEEELEKDEG PDLDPASPEL DTQPQPETQG QAAGNKKERK KKVMKCPMSC
510 520 530 540 550
LLICGHVMAQ APSSIPESIL LSKQFLLLSS TTIMCPDLSA LVVYLRTVPF
560 570 580 590 600
CSFTHSKENY HIYDISSFSE SKAKNLIKEA GNEFVQHNAR QLCRVYPSGL
610 620 630 640 650
RTDSSNFNPQ EHWNVGCQMV AMNMQTAGSA MDICDGLFRQ NGGSGYVLKP
660 670 680 690 700
EFLRDTQSSF NPERPISLYK AQILVVQVIS GQQLPKVDKT KETTVVDPLV
710 720 730 740 750
KVELYGVPED TKEQETSHVE NNGINPYWGE TFYFRLQVPE LAMLRFVVKD
760 770 780 790 800
YSRKSRNNFI GQYTLPWTCM KQGYRHVSLL SRDGTSLNPA SIFVYTCMQE

DLDMDEP
Length:807
Mass (Da):92,694
Last modified:October 2, 2007 - v2
Checksum:iC109F6255CED45F7
GO
Isoform 2 (identifier: Q8K3R3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     493-524: Missing.

Note: No experimental confirmation available.

Show »
Length:775
Mass (Da):89,296
Checksum:iEFA6651F8635BBF7
GO
Isoform 3 (identifier: Q8K3R3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     493-524: Missing.
     773-807: GYRHVSLLSRDGTSLNPASIFVYTCMQEDLDMDEP → EMALASIQLP...LKIQSQPKDQ

Note: No experimental confirmation available.

Show »
Length:798
Mass (Da):92,091
Checksum:i5D5EEC1B9028824D
GO
Isoform 4 (identifier: Q8K3R3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     494-496: MKC → SQD
     497-807: Missing.

Note: No experimental confirmation available.

Show »
Length:496
Mass (Da):57,480
Checksum:i85050CCD6471FB72
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801Q → R in BAE24292. (PubMed:16141072)Curated
Sequence conflicti310 – 3101V → A in AAH66156. (PubMed:15489334)Curated
Sequence conflicti372 – 3721F → L in AAH66156. (PubMed:15489334)Curated
Sequence conflicti445 – 4451Missing in BAE24292. (PubMed:16141072)Curated
Sequence conflicti470 – 4701L → F in AAK61537. 1 PublicationCurated
Sequence conflicti594 – 5941R → C in AAH66156. (PubMed:15489334)Curated
Sequence conflicti653 – 6531L → V in AAK61537. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei493 – 52432Missing in isoform 2 and isoform 3. 2 PublicationsVSP_028503Add
BLAST
Alternative sequencei494 – 4963MKC → SQD in isoform 4. 1 PublicationVSP_028504
Alternative sequencei497 – 807311Missing in isoform 4. 1 PublicationVSP_028505Add
BLAST
Alternative sequencei773 – 80735GYRHV…DMDEP → EMALASIQLPSLYTPACRKT WIWMSPEKHREGLEEQSTDA QSFPTYNFLKIQSQPKDQ in isoform 3. 1 PublicationVSP_028506Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033991 mRNA. Translation: AAK61537.1.
AK016945 mRNA. Translation: BAB30513.1.
AK039149 mRNA. Translation: BAC30256.1.
AK140231 mRNA. Translation: BAE24292.1.
BC066156 mRNA. Translation: AAH66156.1.
CCDSiCCDS35616.1. [Q8K3R3-1]
CCDS35617.1. [Q8K3R3-2]
RefSeqiNP_001074925.1. NM_001081456.1. [Q8K3R3-2]
NP_683739.2. NM_148937.2. [Q8K3R3-1]
XP_006495851.1. XM_006495788.1. [Q8K3R3-1]
UniGeneiMm.290731.

Genome annotation databases

EnsembliENSMUST00000027362; ENSMUSP00000027362; ENSMUSG00000026173. [Q8K3R3-1]
ENSMUST00000067916; ENSMUSP00000064413; ENSMUSG00000026173. [Q8K3R3-2]
ENSMUST00000113747; ENSMUSP00000109376; ENSMUSG00000026173. [Q8K3R3-2]
ENSMUST00000113749; ENSMUSP00000109378; ENSMUSG00000026173. [Q8K3R3-1]
ENSMUST00000113750; ENSMUSP00000109379; ENSMUSG00000026173. [Q8K3R3-3]
GeneIDi18802.
KEGGimmu:18802.
UCSCiuc007bmg.1. mouse. [Q8K3R3-2]
uc007bmh.1. mouse. [Q8K3R3-1]
uc007bmi.1. mouse. [Q8K3R3-4]
uc011wnb.1. mouse. [Q8K3R3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033991 mRNA. Translation: AAK61537.1 .
AK016945 mRNA. Translation: BAB30513.1 .
AK039149 mRNA. Translation: BAC30256.1 .
AK140231 mRNA. Translation: BAE24292.1 .
BC066156 mRNA. Translation: AAH66156.1 .
CCDSi CCDS35616.1. [Q8K3R3-1 ]
CCDS35617.1. [Q8K3R3-2 ]
RefSeqi NP_001074925.1. NM_001081456.1. [Q8K3R3-2 ]
NP_683739.2. NM_148937.2. [Q8K3R3-1 ]
XP_006495851.1. XM_006495788.1. [Q8K3R3-1 ]
UniGenei Mm.290731.

3D structure databases

ProteinModelPortali Q8K3R3.
SMRi Q8K3R3. Positions 9-453, 536-800.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8K3R3.

Proteomic databases

MaxQBi Q8K3R3.
PaxDbi Q8K3R3.
PRIDEi Q8K3R3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027362 ; ENSMUSP00000027362 ; ENSMUSG00000026173 . [Q8K3R3-1 ]
ENSMUST00000067916 ; ENSMUSP00000064413 ; ENSMUSG00000026173 . [Q8K3R3-2 ]
ENSMUST00000113747 ; ENSMUSP00000109376 ; ENSMUSG00000026173 . [Q8K3R3-2 ]
ENSMUST00000113749 ; ENSMUSP00000109378 ; ENSMUSG00000026173 . [Q8K3R3-1 ]
ENSMUST00000113750 ; ENSMUSP00000109379 ; ENSMUSG00000026173 . [Q8K3R3-3 ]
GeneIDi 18802.
KEGGi mmu:18802.
UCSCi uc007bmg.1. mouse. [Q8K3R3-2 ]
uc007bmh.1. mouse. [Q8K3R3-1 ]
uc007bmi.1. mouse. [Q8K3R3-4 ]
uc011wnb.1. mouse. [Q8K3R3-3 ]

Organism-specific databases

CTDi 84812.
MGIi MGI:107469. Plcd4.

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00760000118936.
HOGENOMi HOG000006871.
HOVERGENi HBG053610.
InParanoidi Q8K3R3.
KOi K05857.
OMAi RDYAFSS.
OrthoDBi EOG7V49XT.
PhylomeDBi Q8K3R3.
TreeFami TF313216.

Miscellaneous databases

ChiTaRSi Plcd4. mouse.
NextBioi 295100.
PROi Q8K3R3.
SOURCEi Search...

Gene expression databases

Bgeei Q8K3R3.
CleanExi MM_PLCD4.
ExpressionAtlasi Q8K3R3. baseline and differential.
Genevestigatori Q8K3R3.

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.
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. 2 hits.
PROSITEi PS50004. C2. 1 hit.
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

« Hide 'large scale' publications
  1. "Molecular cloning of PLC delta4."
    Kim J., Kim H., Lee K.-H.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Hypothalamus and Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: CD-1.
    Tissue: Neural stem cell.
  4. "Growth factor-induced promoter activation of murine phospholipase C delta4 gene."
    Fukami K., Takenaka K., Nagano K., Takenawa T.
    Eur. J. Biochem. 267:28-36(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Requirement of phospholipase Cdelta4 for the zona pellucida-induced acrosome reaction."
    Fukami K., Nakao K., Inoue T., Kataoka Y., Kurokawa M., Fissore R.A., Nakamura K., Katsuki M., Mikoshiba K., Yoshida N., Takenawa T.
    Science 292:920-923(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Phospholipase Cdelta4 is required for Ca2+ mobilization essential for acrosome reaction in sperm."
    Fukami K., Yoshida M., Inoue T., Kurokawa M., Fissore R.A., Yoshida N., Mikoshiba K., Takenawa T.
    J. Cell Biol. 161:79-88(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Phospholipase Cdelta4 associates with glutamate receptor interacting protein 1 in testis."
    Irino Y., Ichinohe M., Nakamura Y., Nakahara M., Fukami K.
    J. Biochem. 138:451-456(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRIP1.
  8. "Disruption of phospholipase Cdelta4 gene modulates the liver regeneration in cooperation with nuclear protein kinase C."
    Akutagawa A., Fukami K., Banno Y., Takenawa T., Kannagi R., Yokoyama Y., Oda K., Nagino M., Nimura Y., Yoshida S., Tamiya-Koizumi K.
    J. Biochem. 140:619-625(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPLCD4_MOUSE
AccessioniPrimary (citable) accession number: Q8K3R3
Secondary accession number(s): Q3USN9
, Q6NZF7, Q8CAB1, Q9CUC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: November 26, 2014
This is version 110 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3