Reviewed,
UniProtKB/Swiss-Prot A2AP18 (PLCH2_MOUSE)
Last modified
February 9, 2010.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2 EC=3.1.4.11 Alternative name(s): Phosphoinositide phospholipase C-eta-2 Phospholipase C-eta-2 Short name=PLC-eta2 Phosphoinositide phospholipase C-like 4 Short name=Phospholipase C-like protein 4 Short name=PLC-L4 | ||||
| Gene names |
| ||||
| 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 | 1501 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein 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. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain. Ref.1 Ref.4 |
| Catalytic activity | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. |
| Cofactor | Calcium. |
| Subcellular location | Cytoplasm. Cell membrane. Note: Localized predominantly at the plasma membrane. Ref.4 |
| Tissue specificity | Specifically detected in the brain, with higher level in cerebral cortex, olfactory bulb and hippocampus (at protein level). Expressed in the pyramidal cells of the hippocampus, but also in eye and lung. Ref.1 Ref.4 |
| Developmental stage | Expressed at 2 weeks after birth but barely detected 1 week after birth. Increased expression during brain development. Ref.4 |
| Sequence similarities | Contains 1 C2 domain. Contains 2 EF-hand domains. Contains 1 PH domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain. |
| Sequence caution | The sequence BAC32005.1 differs from that shown. Reason: Frameshift at positions 691, 947 and 1260. The sequence BAC37371.1 differs from that shown. Reason: Erroneous termination at position 433. Translated as Tyr. The sequence CAO78007.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAO78129.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Cell membrane Cytoplasm Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase Transducer |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW phosphoinositide metabolic process Ref.4Inferred from direct assay. Source: MGI |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.4Inferred from direct assay. Source: MGI |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activityInferred from electronic annotation. Source: EC signal transducer activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: A2AP18-1) 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: A2AP18-2) The sequence of this isoform differs from the canonical sequence as follows: 1068-1238: DTRLFPLQRP...SSSSSMSSND → GKAPGGEATE...HSPMFSTVRD 1239-1501: Missing. | ||||||
| Isoform 3 (identifier: A2AP18-3) The sequence of this isoform differs from the canonical sequence as follows: 1068-1252: DTRLFPLQRP...LSLPSLGLCR → GKAPGGEATE...ASHALYTWHA 1253-1501: Missing. | ||||||
| Isoform 4 (identifier: A2AP18-4) The sequence of this isoform differs from the canonical sequence as follows: 1-105: Missing. 106-116: VSPRWQLSLVV → MDAGAAPQKHM | ||||||
| Isoform 5 (identifier: A2AP18-5) The sequence of this isoform differs from the canonical sequence as follows: 40-115: Missing. 580-675: ASTNRKRVEN...KKGSKIKKVA → VSGSPGSACR...GKWWFTNVKK 676-1501: Missing. | ||||||
| Isoform 6 (identifier: A2AP18-6) The sequence of this isoform differs from the canonical sequence as follows: 1067-1067: R → RGKAPGGEAT...STVRDDLRVP |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1501 | 1501 | 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2 | PRO_0000308959 | |||||
Regions | |||||||||
| Domain | 121 – 229 | 109 | PH | ||||||
| Domain | 243 – 278 | 36 | EF-hand 1 | ||||||
| Domain | 279 – 315 | 37 | EF-hand 2 | ||||||
| Domain | 400 – 545 | 146 | PI-PLC X-box | ||||||
| Domain | 707 – 821 | 115 | PI-PLC Y-box | ||||||
| Domain | 826 – 933 | 108 | C2 | ||||||
| Calcium binding | 256 – 267 | 12 | Potential | ||||||
| Region | 75 – 229 | 155 | Necessary for plasma membrane localization | ||||||
| Compositional bias | 1227 – 1236 | 10 | Poly-Ser | ||||||
Sites | |||||||||
| Active site | 415 | 1 | By similarity | ||||||
| Active site | 459 | 1 | By similarity | ||||||
| Metal binding | 416 | 1 | Calcium 1; catalytic By similarity | ||||||
| Metal binding | 445 | 1 | Calcium 1; catalytic By similarity | ||||||
| Metal binding | 447 | 1 | Calcium 1; catalytic By similarity | ||||||
| Metal binding | 494 | 1 | Calcium 1; catalytic By similarity | ||||||
| Metal binding | 865 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 867 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 891 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 920 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 921 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 922 | 1 | Calcium 3 By similarity | ||||||
| Binding site | 543 | 1 | Substrate By similarity | ||||||
| Binding site | 545 | 1 | Substrate By similarity | ||||||
| Binding site | 734 | 1 | Substrate By similarity | ||||||
| Binding site | 761 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 676 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 686 | 1 | Phosphoserine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 105 | 105 | Missing in isoform 4. | VSP_029075 | |||||
| Alternative sequence | 40 – 115 | 76 | Missing in isoform 5. | VSP_029076 | |||||
| Alternative sequence | 106 – 116 | 11 | VSPRWQLSLVV → MDAGAAPQKHM in isoform 4. | VSP_029077 | |||||
| Alternative sequence | 580 – 675 | 96 | ASTNR…IKKVA → VSGSPGSACREPGVGPQHPR PILSTKGIYLPQRERGQGVR DKDRRWRVREKGKGTREGAR GICPGGRGDKGLPLDREETD RQTWPIGKWWFTNVKK in isoform 5. | VSP_029078 | |||||
| Alternative sequence | 676 – 1501 | 826 | Missing in isoform 5. | VSP_029079 | |||||
| Alternative sequence | 1067 | 1 | R → RGKAPGGEATEERTLAQVRS PNAPEGPGPAGMAATCMKCV VGSCAGMDVEGLRREQQPSP GPAGSHMAISHQPRARVDSL GGPCCSPSPRATPGRSKEAP KGPRARRQGPGGGSVSSDSS SPDSPGSPKVAPCQPEGAHR QQGALQGEMNALFVQKLEEI RSHSPMFSTVRDDLRVP in isoform 6. | VSP_029080 | |||||
| Alternative sequence | 1068 – 1252 | 185 | DTRLF…LGLCR → GKAPGGEATEERTLAQVRSP NAPEGPGPAGMAATCMKCVV GSCAGMDVEGLQREQQPSPG PAGSHMAISHQPRARVDSLG GPCCSPSPRATPGRSKEAPK GPRARRQGPGGGSVSSDSSS PDSPGSPKVAPCQPEGAHRQ QGALQGEMNALFVQKLEEIR SHSPMFSTGKACRSAASHAL YTWHA in isoform 3. | VSP_029081 | |||||
| Alternative sequence | 1068 – 1238 | 171 | DTRLF…MSSND → GKAPGGEATEERTLAQVRSP NAPEGPGPAGMAATCMKCVV GSCAGMDVEGLRREQQPSPG PAGSHMAISHQPRARVDSLG GPCCSPSPRATPGRSKEAPK GPRARRQGPGGGSVSSDSSS PDSPGSPKVAPCQPEGAHRQ QGALQGEMNALFVQKLEEIR SHSPMFSTVRD in isoform 2. | VSP_029082 | |||||
| Alternative sequence | 1239 – 1501 | 263 | Missing in isoform 2. | VSP_029083 | |||||
| Alternative sequence | 1253 – 1501 | 249 | Missing in isoform 3. | VSP_029084 | |||||
Experimental info | |||||||||
| Mutagenesis | 415 | 1 | H → A: Inhibition of activity. Ref.4 | ||||||
| Sequence conflict | 340 | 1 | F → L in BAC34011. Ref.3 | ||||||
| Sequence conflict | 664 – 665 | 2 | RK → HR in AAH40465. Ref.5 | ||||||
| Sequence conflict | 781 | 1 | N → D in BAC32005. Ref.3 | ||||||
| Sequence conflict | 1258 | 1 | P → A in BAC32005. Ref.3 | ||||||
| Sequence conflict | 1495 | 1 | G → S in BAC32005. Ref.3 | ||||||
Sequences
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References
| [1] | "Molecular cloning and characterization of PLC-eta2." Zhou Y., Wing M.R., Sondek J., Harden T.K. Biochem. J. 391:667-676(2005) [PubMed: 16107206] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY. Strain: C57BL/6J. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [3] | "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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-664 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1501 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1501 (ISOFORM 6). Strain: C57BL/6J. Tissue: Eye, Hippocampus and Retina. |
| [4] | "A novel phospholipase C, PLC(eta)2, is a neuron-specific isozyme." Nakahara M., Shimozawa M., Nakamura Y., Irino Y., Morita M., Kudo Y., Fukami K. J. Biol. Chem. 280:29128-29134(2005) [PubMed: 15899900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-1501 (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, REGION, FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF HIS-415. Strain: C57BL/6J x 129. Tissue: Brain. |
| [5] | "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] OF 624-1501 (ISOFORM 3). Tissue: Eye. |
| [6] | "Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-686, MASS SPECTROMETRY. Tissue: Brain. |
| [7] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ176851 mRNA. Translation: ABA12210.1. AL831788, BX004788 Genomic DNA. Translation: CAM16344.2. BX004788, AL831788 Genomic DNA. Translation: CAM28037.2. AL831788, BX004788 Genomic DNA. Translation: CAO78007.1. Sequence problems. BX004788, AL831788 Genomic DNA. Translation: CAO78129.1. Sequence problems. AK044619 mRNA. Translation: BAC32005.1. Frameshift. AK049970 mRNA. Translation: BAC34011.1. AK078731 mRNA. Translation: BAC37371.1. Sequence problems. AY966876 mRNA. Translation: AAY33831.1. BC040465 mRNA. Translation: AAH40465.1. BC052329 mRNA. Translation: AAH52329.1. |
| IPI | IPI00226764. IPI00649874. IPI00830504. IPI00875018. IPI00875482. IPI00876566. |
| RefSeq | NP_001106831.1. NP_780765.2. |
| UniGene | Mm.379458 |
3D structure databases | |
| SMR | A2AP18. Positions 120-964. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | A2AP18. |
Proteomic databases | |
| PRIDE | A2AP18. |
Genome annotation databases | |
| Ensembl | ENSMUST00000030929; ENSMUSP00000030929; ENSMUSG00000029055; Mus musculus. [Genome view] ENSMUST00000105630; ENSMUSP00000101255; ENSMUSG00000029055; Mus musculus. [Genome view] ENSMUST00000105631; ENSMUSP00000101256; ENSMUSG00000029055; Mus musculus. [Genome view] |
| GeneID | 269615. |
| KEGG | mmu:269615. |
Organism-specific databases | |
| CTD | 269615. |
| MGI | MGI:2443078. Plch2. |
Phylogenomic databases | |
| eggNOG | maNOG16228. |
| HOVERGEN | A2AP18. |
| InParanoid | A2AP18. |
| OrthoDB | EOG9JWZ0J. |
| PhylomeDB | A2AP18. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.11. 244. |
Gene expression databases | |
| Bgee | A2AP18. |
| CleanEx | MM_PLCH2. |
| Genevestigator | A2AP18. |
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. IPR018247. EF_Hand_1_Ca_BS. 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. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits. |
| 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. SM00054. EFh. 2 hits. SM00233. PH. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view] |
| PROSITE | PS50004. C2. 1 hit. PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 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 | 392931. |
| SOURCE | Search... |
Entry information
| Entry name | PLCH2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: A2AP18 Secondary accession number(s): A6PWW5 Q8CFR1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


