Reviewed, UniProtKB/Swiss-Prot Q8K3R3 (PLCD4_MOUSE)

Names and origin

Protein names

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 names

Name:	Plcd4
Synonyms:	Plcd

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. 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 upregulates the Erk signaling pathway and proliferation. Ref.5 Ref.6 Ref.8
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.
Subunit structure	Interacts with GRIP1. Ref.7
Subcellular location	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.
Induction	By treatment with growth factors such as bradykinin, lysophosphatidic acid, and Ca2+ ionophore in addition to serum. Ref.4
Domain	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.
Disruption phenotype	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. Ref.5
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
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Gene Ontology (GO)
Biological process	acrosome reaction Ref.5 Inferred from mutant phenotype. Source: MGI intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide metabolic process Ref.5 Traceable author statement. Source: MGI
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8K3R3-1)

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.

Isoform 2 (identifier: Q8K3R3-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8K3R3-3)

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.

Isoform 4 (identifier: Q8K3R3-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 807	807	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4		PRO_0000306826
Regions
	Domain	16 – 124	109	PH
	Domain	134 – 169	36	EF-hand 1
	Domain	170 – 205	36	EF-hand 2
	Domain	203 – 237	35	EF-hand 3
	Domain	290 – 435	146	PI-PLC X-box
	Domain	538 – 654	117	PI-PLC Y-box
	Domain	659 – 764	106	C2
	Calcium binding	147 – 158	12	1 Potential
	Calcium binding	183 – 194	12	2 Potential
	Region	26 – 53	28	Substrate binding By similarity
	Motif	776 – 779	4	PDZ-binding
	Compositional bias	445 – 456	12	Poly-Glu
Sites
	Active site	305	1	By similarity
	Active site	350	1	By similarity
	Metal binding	306	1	Calcium 1; catalytic By similarity
	Metal binding	335	1	Calcium 1; catalytic By similarity
	Metal binding	337	1	Calcium 1; catalytic By similarity
	Metal binding	384	1	Calcium 1; catalytic By similarity
	Metal binding	697	1	Calcium 2 By similarity
	Metal binding	721	1	Calcium 2 By similarity
	Metal binding	750	1	Calcium 3 By similarity
	Metal binding	751	1	Calcium 3; via carbonyl oxygen By similarity
	Binding site	433	1	Substrate By similarity
	Binding site	435	1	Substrate By similarity
	Binding site	567	1	Substrate By similarity
	Binding site	594	1	Substrate By similarity
Natural variations
	Alternative sequence	493 – 524	32	Missing in isoform 2 and isoform 3.		VSP_028503
	Alternative sequence	494 – 496	3	MKC → SQD in isoform 4.		VSP_028504
	Alternative sequence	497 – 807	311	Missing in isoform 4.		VSP_028505
	Alternative sequence	773 – 807	35	GYRHV…DMDEP → EMALASIQLPSLYTPACRKT WIWMSPEKHREGLEEQSTDA QSFPTYNFLKIQSQPKDQ in isoform 3.		VSP_028506
Experimental info
	Sequence conflict	180	1	Q → R in BAE24292. Ref.2
	Sequence conflict	310	1	V → A in AAH66156. Ref.3
	Sequence conflict	372	1	F → L in AAH66156. Ref.3
	Sequence conflict	445	1	Missing in BAE24292. Ref.2
	Sequence conflict	470	1	L → F in AAK61537. Ref.1
	Sequence conflict	594	1	R → C in AAH66156. Ref.3
	Sequence conflict	653	1	L → V in AAK61537. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 2, 2007. Version 2. Checksum: C109F6255CED45F7	FASTA	807	92,694
	10 20 30 40 50 60 MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG SQPESMPKPT 70 80 90 100 110 120 FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP NLDLVANSVE EAQIWMRGLQ 130 140 150 160 170 180 LLVDLVASMD HQEQMDQMLN EWFQQADRNQ DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ 190 200 210 220 230 240 EADVTQSDDL GSEEFVQFYK ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH 250 260 270 280 290 300 APDLALELID RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY 310 320 330 340 350 360 INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GHTLTSRILF 370 380 390 400 410 420 KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT EILGEQLLRN TLEGLLVDSM 430 440 450 460 470 480 PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE EEEELEKDEG PDLDPASPEL DTQPQPETQG 490 500 510 520 530 540 QAAGNKKERK KKVMKCPMSC LLICGHVMAQ APSSIPESIL LSKQFLLLSS TTIMCPDLSA 550 560 570 580 590 600 LVVYLRTVPF CSFTHSKENY HIYDISSFSE SKAKNLIKEA GNEFVQHNAR QLCRVYPSGL 610 620 630 640 650 660 RTDSSNFNPQ EHWNVGCQMV AMNMQTAGSA MDICDGLFRQ NGGSGYVLKP EFLRDTQSSF 670 680 690 700 710 720 NPERPISLYK AQILVVQVIS GQQLPKVDKT KETTVVDPLV KVELYGVPED TKEQETSHVE 730 740 750 760 770 780 NNGINPYWGE TFYFRLQVPE LAMLRFVVKD YSRKSRNNFI GQYTLPWTCM KQGYRHVSLL 790 800 SRDGTSLNPA SIFVYTCMQE DLDMDEP
	Isoform 2. Checksum: EFA6651F8635BBF7	FASTA	775	89,296
	10 20 30 40 50 60 MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG SQPESMPKPT 70 80 90 100 110 120 FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP NLDLVANSVE EAQIWMRGLQ 130 140 150 160 170 180 LLVDLVASMD HQEQMDQMLN EWFQQADRNQ DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ 190 200 210 220 230 240 EADVTQSDDL GSEEFVQFYK ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH 250 260 270 280 290 300 APDLALELID RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY 310 320 330 340 350 360 INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GHTLTSRILF 370 380 390 400 410 420 KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT EILGEQLLRN TLEGLLVDSM 430 440 450 460 470 480 PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE EEEELEKDEG PDLDPASPEL DTQPQPETQG 490 500 510 520 530 540 QAAGNKKERK KKFLLLSSTT IMCPDLSALV VYLRTVPFCS FTHSKENYHI YDISSFSESK 550 560 570 580 590 600 AKNLIKEAGN EFVQHNARQL CRVYPSGLRT DSSNFNPQEH WNVGCQMVAM NMQTAGSAMD 610 620 630 640 650 660 ICDGLFRQNG GSGYVLKPEF LRDTQSSFNP ERPISLYKAQ ILVVQVISGQ QLPKVDKTKE 670 680 690 700 710 720 TTVVDPLVKV ELYGVPEDTK EQETSHVENN GINPYWGETF YFRLQVPELA MLRFVVKDYS 730 740 750 760 770 RKSRNNFIGQ YTLPWTCMKQ GYRHVSLLSR DGTSLNPASI FVYTCMQEDL DMDEP
	Isoform 3. Checksum: 5D5EEC1B9028824D	FASTA	798	92,091
	10 20 30 40 50 60 MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG SQPESMPKPT 70 80 90 100 110 120 FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP NLDLVANSVE EAQIWMRGLQ 130 140 150 160 170 180 LLVDLVASMD HQEQMDQMLN EWFQQADRNQ DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ 190 200 210 220 230 240 EADVTQSDDL GSEEFVQFYK ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH 250 260 270 280 290 300 APDLALELID RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY 310 320 330 340 350 360 INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GHTLTSRILF 370 380 390 400 410 420 KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT EILGEQLLRN TLEGLLVDSM 430 440 450 460 470 480 PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE EEEELEKDEG PDLDPASPEL DTQPQPETQG 490 500 510 520 530 540 QAAGNKKERK KKFLLLSSTT IMCPDLSALV VYLRTVPFCS FTHSKENYHI YDISSFSESK 550 560 570 580 590 600 AKNLIKEAGN EFVQHNARQL CRVYPSGLRT DSSNFNPQEH WNVGCQMVAM NMQTAGSAMD 610 620 630 640 650 660 ICDGLFRQNG GSGYVLKPEF LRDTQSSFNP ERPISLYKAQ ILVVQVISGQ QLPKVDKTKE 670 680 690 700 710 720 TTVVDPLVKV ELYGVPEDTK EQETSHVENN GINPYWGETF YFRLQVPELA MLRFVVKDYS 730 740 750 760 770 780 RKSRNNFIGQ YTLPWTCMKQ EMALASIQLP SLYTPACRKT WIWMSPEKHR EGLEEQSTDA 790 QSFPTYNFLK IQSQPKDQ
	Isoform 4. Checksum: 85050CCD6471FB72	FASTA	496	57,480
	10 20 30 40 50 60 MTSQIQDLLA TDQDLLLMQE GTMMRKVRTK SWKKLRYFRL QNDGMTVWHG SQPESMPKPT 70 80 90 100 110 120 FSISDVERIR KGQDSELLRY LVEEFPLEQG FTVVFHGRRP NLDLVANSVE EAQIWMRGLQ 130 140 150 160 170 180 LLVDLVASMD HQEQMDQMLN EWFQQADRNQ DGRMSFREAQ RLLLLMNVEM DEEYAFSLFQ 190 200 210 220 230 240 EADVTQSDDL GSEEFVQFYK ALTKRTEIEE IFEDFSSDKQ KLTLLEFVDF LRKEQKEKDH 250 260 270 280 290 300 APDLALELID RYEPSENGRL LHVLSKDGFL KYLCSKDGNI FNSDCLPIYQ DMTQPLSHYY 310 320 330 340 350 360 INSSHNTYLV GDQLCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GHTLTSRILF 370 380 390 400 410 420 KDVLATLAQY AFQSSDYPLI LSLENHCTWE QQRTMAHHLT EILGEQLLRN TLEGLLVDSM 430 440 450 460 470 480 PSPEQLRGKI LVKGKKLRTI EVDKEEEEEE EEEELEKDEG PDLDPASPEL DTQPQPETQG 490 QAAGNKKERK KKVSQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [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: 15489334] [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: 10601847] [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: 11340203] [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: 12695499] [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: 16272139] [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: 16998201] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00322551. IPI00652756. IPI00831343. IPI00831599.
RefSeq	NP_001074925.1. NP_683739.2.
UniGene	Mm.290731
3D structure databases
HSSP	HSSP built from PDB template 1QAS based on UniProtKB P10688.
SMR	Q8K3R3. Positions 194-800.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8K3R3.
Proteomic databases
PRIDE	Q8K3R3.
Genome annotation databases
Ensembl	ENSMUST00000027362; ENSMUSP00000027362; ENSMUSG00000026173; Mus musculus. [Genome view] ENSMUST00000067916; ENSMUSP00000064413; ENSMUSG00000026173; Mus musculus. [Genome view] ENSMUST00000113748; ENSMUSP00000109377; ENSMUSG00000026173; Mus musculus. [Genome view] ENSMUST00000113749; ENSMUSP00000109378; ENSMUSG00000026173; Mus musculus. [Genome view]
GeneID	18802.
KEGG	mmu:18802.
UCSC	uc007bmh.1. mouse.
Organism-specific databases
CTD	18802.
MGI	MGI:107469. Plcd4.
Phylogenomic databases
eggNOG	roNOG13444.
HOGENOM	HBG527074.
HOVERGEN	Q8K3R3.
InParanoid	Q8K3R3.
OMA	IHSSHNT.
OrthoDB	EOG9HB152.
PhylomeDB	Q8K3R3.
Enzyme and pathway databases
BRENDA	3.1.4.11. 244.
Gene expression databases
ArrayExpress	Q8K3R3.
Bgee	Q8K3R3.
CleanEx	MM_PLCD4.
Genevestigator	Q8K3R3.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR011993. PH_type. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR001849. Pleckstrin_homology. IPR000909. PLipase_C_PInositol-sp_X_dom. [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.
SMART	SM00239. C2. 1 hit. SM00054. EFh. 3 hits. SM00233. PH. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
PROSITE	PS50004. C2. 1 hit. PS00018. EF_HAND_1. False negative. 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]
ProtoNet	Search...
Other Resources
NextBio	295100.
SOURCE	Search...

Entry information

Entry name

PLCD4_MOUSE

Accession

Primary (citable) accession number: Q8K3R3
Secondary accession number(s): Q3USN9 , Q6NZF7, Q8CAB1, Q9CUC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 2, 2007
Last modified:	February 9, 2010
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)