Q86YW0 (PLCZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-zeta-1
Phospholipase C-zeta-1
Short name=PLC-zeta-1
Testis-development protein NYD-SP27

Gene names

Name:

PLCZ1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca2+-dependent manner. Triggers intracellular Ca2+ oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. Ref.1 Ref.2 Ref.5 UniProtKB Q8K4D7
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. UniProtKB P10688
Cofactor	Calcium By similarity. UniProtKB Q8K4D7
Subunit structure	Interacts via its C2 domain with PtdIns3P and, to a lesser extent, PtdIns5P in vitro By similarity. UniProtKB Q8K4D7
Subcellular location	Nucleus By similarity. Cytoplasm › perinuclear region By similarity. Note: Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronucleus at interphase following meiosis and mitosis By similarity. UniProtKB Q8K4D7
Tissue specificity	Expressed specifically in testis. Weakly expressed in pancreatic-duct cells. Up-regulated in pancreatic-duct cells from patients with cystic fibrosis. Ref.1 Ref.2
Domain	The EF-hand and C2 domains are essential for triggering Ca2+ oscillating activity and the regulation of PLCZ1 enzyme activity By similarity. UniProtKB Q8K4D7 The X-Y linker region between PI-PLC X-box and Y-box domains may be a target for proteolysis and may play an important regulatory role during fertilization By similarity. UniProtKB Q8K4D7
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
Biological process	Fertilization Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Calcium
Molecular function	Developmental protein Hydrolase Transducer
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion transport Inferred from electronic annotation. Source: Compara egg activation Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm 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 signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.2 Ref.3 (identifier: Q86YW0-1)

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 Ref.4 (identifier: Q86YW0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     46-238: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q86YW0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 608	608	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1		PRO_0000347244
Regions
	Domain	35 – 70	36	EF-hand
	Domain	155 – 299	145	PI-PLC X-box
	Domain	349 – 465	117	PI-PLC Y-box
	Domain	469 – 572	104	C2
Sites
	Active site	170	1	By similarity UniProtKB P10688
	Active site	215	1	By similarity UniProtKB P10688
Natural variations
	Alternative sequence	1 – 104	104	Missing in isoform 3.		VSP_035076
	Alternative sequence	46 – 238	193	Missing in isoform 2. Ref.4		VSP_052862
	Natural variant	500	1	S → L. Corresponds to variant rs10505830 [ dbSNP | Ensembl ].		VAR_050542
Experimental info
	Sequence conflict	294	1	I → V in AAK61372. Ref.2
	Sequence conflict	489	1	I → T in AAK61372. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 540A81A2DDB9537B	FASTA	608	70,411
	10 20 30 40 50 60 MEMRWFLSKI QDDFRGGKIN LEKTQRLLEK LDIRCSYIHV KQIFKDNDRL KQGRITIEEF 70 80 90 100 110 120 RAIYRIITHR EEIIEIFNTY SENRKILLAS NLAQFLTQEQ YAAEMSKAIA FEIIQKYEPI 130 140 150 160 170 180 EEVRKAHQMS LEGFTRYMDS RECLLFKNEC RKVYQDMTHP LNDYFISSSH NTYLVSDQLL 190 200 210 220 230 240 GPSDLWGYVS ALVKGCRCLE IDCWDGAQNE PVVYHGYTLT SKLLFKTVIQ AIHKYAFMTS 250 260 270 280 290 300 DYPVVLSLEN HCSTAQQEVM ADNLQATFGE SLLSDMLDDF PDTLPSPEAL KFKILVKNKK 310 320 330 340 350 360 IGTLKETHER KGSDKRGDNQ DKETGVKKLP GVMLFKKKKT RKLKIALALS DLVIYTKAEK 370 380 390 400 410 420 FKSFQHSRLY QQFNENNSIG ETQARKLSKL RVHEFIFHTR KFITRIYPKA TRADSSNFNP 430 440 450 460 470 480 QEFWNIGCQM VALNFQTPGL PMDLQNGKFL DNGGSGYILK PHFLRESKSY FNPSNIKEGM 490 500 510 520 530 540 PITLTIRLIS GIQLPLTHSS SNKGDSLVII EVFGVPNDQM KQQTRVIKKN AFSPRWNETF 550 560 570 580 590 600 TFIIHVPELA LIRFVVEGQG LIAGNEFLGQ YTLPLLCMNK GYRRIPLFSR MGESLEPASL FVYVWYVR
	Isoform 2 [UniParc]. Checksum: 68B6337B885663DE	FASTA	415	47,758
	10 20 30 40 50 60 MEMRWFLSKI QDDFRGGKIN LEKTQRLLEK LDIRCSYIHV KQIFKTSDYP VVLSLENHCS 70 80 90 100 110 120 TAQQEVMADN LQATFGESLL SDMLDDFPDT LPSPEALKFK ILVKNKKIGT LKETHERKGS 130 140 150 160 170 180 DKRGDNQDKE TGVKKLPGVM LFKKKKTRKL KIALALSDLV IYTKAEKFKS FQHSRLYQQF 190 200 210 220 230 240 NENNSIGETQ ARKLSKLRVH EFIFHTRKFI TRIYPKATRA DSSNFNPQEF WNIGCQMVAL 250 260 270 280 290 300 NFQTPGLPMD LQNGKFLDNG GSGYILKPHF LRESKSYFNP SNIKEGMPIT LTIRLISGIQ 310 320 330 340 350 360 LPLTHSSSNK GDSLVIIEVF GVPNDQMKQQ TRVIKKNAFS PRWNETFTFI IHVPELALIR 370 380 390 400 410 FVVEGQGLIA GNEFLGQYTL PLLCMNKGYR RIPLFSRMGE SLEPASLFVY VWYVR
	Isoform 3 [UniParc]. Checksum: 671C2692852FED44	FASTA	504	57,804
	10 20 30 40 50 60 MSKAIAFEII QKYEPIEEVR KAHQMSLEGF TRYMDSRECL LFKNECRKVY QDMTHPLNDY 70 80 90 100 110 120 FISSSHNTYL VSDQLLGPSD LWGYVSALVK GCRCLEIDCW DGAQNEPVVY HGYTLTSKLL 130 140 150 160 170 180 FKTVIQAIHK YAFMTSDYPV VLSLENHCST AQQEVMADNL QATFGESLLS DMLDDFPDTL 190 200 210 220 230 240 PSPEALKFKI LVKNKKIGTL KETHERKGSD KRGDNQDKET GVKKLPGVML FKKKKTRKLK 250 260 270 280 290 300 IALALSDLVI YTKAEKFKSF QHSRLYQQFN ENNSIGETQA RKLSKLRVHE FIFHTRKFIT 310 320 330 340 350 360 RIYPKATRAD SSNFNPQEFW NIGCQMVALN FQTPGLPMDL QNGKFLDNGG SGYILKPHFL 370 380 390 400 410 420 RESKSYFNPS NIKEGMPITL TIRLISGIQL PLTHSSSNKG DSLVIIEVFG VPNDQMKQQT 430 440 450 460 470 480 RVIKKNAFSP RWNETFTFII HVPELALIRF VVEGQGLIAG NEFLGQYTLP LLCMNKGYRR 490 500 IPLFSRMGES LEPASLFVYV WYVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sperm phospholipase Czeta from humans and cynomolgus monkeys triggers Ca2+ oscillations, activation and development of mouse oocytes." Cox L.J., Larman M.G., Saunders C.M., Hashimoto K., Swann K., Lai F.A. Reproduction 124:611-623(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Testis.
[2]	"Rescue of defective pancreatic secretion in cystic-fibrosis cells by suppression of a novel isoform of phospholipase C." Zhu H., Zhu J.X., Lo P.S., Li J., Leung K.M., Rowlands D.K., Tsang L.L., Yu M.K., Jiang J.L., Lam S.Y., Chung Y.W., Zhou Z., Sha J., Chang Chan H. Lancet 362:2059-2065(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY. Tissue: Testis.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[4]	"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).
[5]	"Phospholipase Czeta causes Ca2+ oscillations and parthenogenetic activation of human oocytes." Rogers N.T., Hobson E., Pickering S., Lai F.A., Braude P., Swann K. Reproduction 128:697-702(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF532185 mRNA. Translation: AAN71895.1. AY035866 mRNA. Translation: AAK61372.1. AK292279 mRNA. Translation: BAF84968.1. BC125067 mRNA. Translation: AAI25068.1.
IPI	IPI00172666. IPI00384651. IPI00792324.
RefSeq	NP_149114.2. NM_033123.3.
UniGene	Hs.97542.
3D structure databases
HSSP	HSSP built from PDB template 1QAS based on UniProtKB P10688.
ProteinModelPortal	Q86YW0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000266505.
Polymorphism databases
DMDM	74714209.
Proteomic databases
PaxDb	Q86YW0.
PRIDE	Q86YW0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266505; ENSP00000266505; ENSG00000139151. ENST00000539875; ENSP00000445026; ENSG00000139151.
GeneID	89869.
KEGG	hsa:89869.
UCSC	uc001rdv.4. human.
Organism-specific databases
CTD	89869.
GeneCards	GC12M018736.
H-InvDB	HIX0010470.
HGNC	HGNC:19218. PLCZ1.
HPA	HPA040732.
MIM	608075. gene.
neXtProt	NX_Q86YW0.
PharmGKB	PA134875646.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG149692.
HOGENOM	HOG000006871.
HOVERGEN	HBG053610.
InParanoid	Q86YW0.
KO	K05861.
OMA	THREEII.
OrthoDB	EOG4X0MSB.
PhylomeDB	Q86YW0.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q86YW0.
Bgee	Q86YW0.
CleanEx	HS_PLCZ1.
Genevestigator	Q86YW0.
Family and domain databases
Gene3D	1.10.238.10. 2 hits. 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. IPR002048. EF_hand_dom. IPR001192. Pinositol_PLipase_C. 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]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 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. False negative. PS50222. EF_HAND_2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PLCZ1. human.
GenomeRNAi	89869.
NextBio	76366.
SOURCE	Search...

Entry information

Entry name

PLCZ1_HUMAN

Accession

Primary (citable) accession number: Q86YW0
Secondary accession number(s): Q08AQ7, Q96J70

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.