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P10688

- PLCD1_RAT

UniProt

P10688 - PLCD1_RAT

Protein

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

Gene

Plcd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    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. Essential for trophoblast and placental development.

    Catalytic activityi

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

    Cofactori

    Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei311 – 3111
    Metal bindingi312 – 3121Calcium 1; catalytic
    Metal bindingi341 – 3411Calcium 1; catalytic
    Metal bindingi343 – 3431Calcium 1; catalytic
    Active sitei356 – 3561
    Metal bindingi390 – 3901Calcium 1; catalytic
    Binding sitei438 – 4381Substrate
    Binding sitei440 – 4401Substrate
    Binding sitei522 – 5221Substrate
    Binding sitei549 – 5491Substrate
    Metal bindingi651 – 6511Calcium 2; via carbonyl oxygen
    Metal bindingi653 – 6531Calcium 2
    Metal bindingi677 – 6771Calcium 2
    Metal bindingi706 – 7061Calcium 3
    Metal bindingi707 – 7071Calcium 3; via carbonyl oxygen
    Metal bindingi708 – 7081Calcium 3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi153 – 164121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi189 – 200122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: RGD
    2. phosphatidylinositol-4,5-bisphosphate binding Source: RGD
    3. phosphatidylinositol phospholipase C activity Source: RGD
    4. phospholipid binding Source: RGD
    5. protein binding Source: RGD
    6. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. cytosolic calcium ion homeostasis Source: RGD
    2. G-protein coupled receptor signaling pathway Source: RGD
    3. intracellular signal transduction Source: InterPro
    4. lipid catabolic process Source: UniProtKB-KW
    5. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: RGD
    6. positive regulation of inositol trisphosphate biosynthetic process Source: RGD
    7. positive regulation of norepinephrine secretion Source: RGD
    8. regulation of phospholipase C activity Source: RGD
    9. response to aluminum ion Source: RGD
    10. response to calcium ion Source: RGD
    11. response to hyperoxia Source: RGD
    12. response to organonitrogen compound Source: RGD
    13. response to peptide hormone Source: RGD
    14. response to prostaglandin F Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.4.11. 5301.
    SABIO-RKP10688.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-delta-1
    Phospholipase C-III
    Short name:
    PLC-III
    Phospholipase C-delta-1
    Short name:
    PLC-delta-1
    Gene namesi
    Name:Plcd1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3346. Plcd1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. membrane Source: RGD
    3. membrane raft Source: RGD
    4. mitochondrial membrane Source: RGD
    5. nucleus Source: RGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi311 – 3111H → A: Lowers activity 10000-fold. 1 Publication
    Mutagenesisi312 – 3121N → A: Lowers activity 10000-fold. 1 Publication
    Mutagenesisi320 – 3201L → A: Lowers activity 3-fold. 1 Publication
    Mutagenesisi341 – 3411E → A, H or Q: Lowers activity 200000-fold. 1 Publication
    Mutagenesisi343 – 3431D → A: Lowers activity 1000-fold. 1 Publication
    Mutagenesisi343 – 3431D → R: Lowers activity 100000-fold. 1 Publication
    Mutagenesisi356 – 3561H → A: Lowers activity 1000-fold. 1 Publication
    Mutagenesisi360 – 3601F → A: Lowers activity 4-fold. 1 Publication
    Mutagenesisi390 – 3901E → A, H or K: Lowers activity 1000-fold. 1 Publication
    Mutagenesisi390 – 3901E → Q: Lowers activity 200-fold. 1 Publication
    Mutagenesisi438 – 4381K → A: Lowers activity very slightly. 1 Publication
    Mutagenesisi440 – 4401K → A: No effect on activity towards phosphatidylinositol 4-monophosphate. Lowers activity 5-fold towards phosphatidylinositol 4,5-bisphosphate. 1 Publication
    Mutagenesisi522 – 5221S → A: Lowers activity 10000-fold. 1 Publication
    Mutagenesisi549 – 5491R → A: Lowers activity 600-fold. 1 Publication
    Mutagenesisi551 – 5511Y → A: Lowers activity 600-fold. 1 Publication
    Mutagenesisi555 – 5551W → A: Lowers activity very slightly. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7567561-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1PRO_0000088506Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi191 – 1911O-linked (GlcNAc)1 Publication
    Glycosylationi193 – 1931O-linked (GlcNAc)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP10688.
    PRIDEiP10688.

    PTM databases

    PhosphoSiteiP10688.

    Expressioni

    Gene expression databases

    GenevestigatoriP10688.

    Interactioni

    Protein-protein interaction databases

    BioGridi246790. 1 interaction.
    MINTiMINT-245440.

    Structurei

    Secondary structure

    1
    756
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 248
    Beta strandi26 – 3510
    Beta strandi37 – 448
    Beta strandi48 – 536
    Turni62 – 654
    Beta strandi66 – 683
    Helixi69 – 713
    Beta strandi72 – 798
    Helixi82 – 876
    Helixi93 – 953
    Beta strandi96 – 1049
    Beta strandi108 – 1114
    Helixi115 – 12915
    Helixi203 – 2086
    Helixi212 – 22211
    Beta strandi225 – 2295
    Helixi230 – 23910
    Helixi248 – 25811
    Helixi262 – 2665
    Helixi272 – 2809
    Turni282 – 2843
    Beta strandi285 – 2873
    Helixi289 – 2924
    Helixi302 – 3043
    Beta strandi305 – 3073
    Beta strandi309 – 3124
    Beta strandi315 – 3173
    Beta strandi319 – 3213
    Helixi326 – 3349
    Beta strandi339 – 3457
    Helixi348 – 3503
    Beta strandi353 – 3553
    Turni357 – 3604
    Helixi366 – 37611
    Turni377 – 3793
    Beta strandi385 – 3928
    Helixi395 – 40915
    Helixi410 – 4123
    Turni428 – 4336
    Beta strandi435 – 4395
    Helixi490 – 4934
    Beta strandi496 – 5027
    Beta strandi509 – 5146
    Beta strandi519 – 5246
    Helixi525 – 54521
    Beta strandi548 – 5514
    Helixi565 – 5684
    Turni569 – 5713
    Beta strandi574 – 5774
    Helixi584 – 59411
    Helixi596 – 5983
    Beta strandi600 – 6034
    Helixi606 – 6094
    Beta strandi629 – 64012
    Helixi644 – 6463
    Beta strandi648 – 6503
    Beta strandi654 – 66310
    Helixi664 – 6663
    Beta strandi668 – 6714
    Beta strandi679 – 6813
    Beta strandi683 – 69311
    Helixi695 – 6973
    Beta strandi699 – 7068
    Beta strandi709 – 7113
    Beta strandi714 – 7229
    Helixi723 – 7253
    Beta strandi729 – 7368
    Beta strandi742 – 75514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DJGX-ray2.60A/B133-756[»]
    1DJHX-ray2.50A/B133-756[»]
    1DJIX-ray2.50A/B133-756[»]
    1DJWX-ray2.45A/B133-756[»]
    1DJXX-ray2.30A/B133-756[»]
    1DJYX-ray2.80A/B133-756[»]
    1DJZX-ray2.95A/B133-756[»]
    1MAIX-ray1.90A11-140[»]
    1QASX-ray2.40A/B135-756[»]
    1QATX-ray3.00A/B135-756[»]
    2ISDX-ray2.50A/B133-756[»]
    DisProtiDP00055.
    ProteinModelPortaliP10688.
    SMRiP10688. Positions 12-130, 158-756.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10688.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 130110PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 17536EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini176 – 21136EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini296 – 440145PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini492 – 609118PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini630 – 72091C2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 5728Substrate bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 2 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.
    HOGENOMiHOG000006871.
    HOVERGENiHBG053610.
    InParanoidiP10688.
    KOiK05857.
    PhylomeDBiP10688.

    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.
    IPR028391. PLC-delta1.
    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:SF80. PTHR10336:SF80. 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. 2 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. 2 hits.
    PS50003. PH_DOMAIN. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10688-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT    50
    IWQESRKVMR SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV 100
    FKDQRNTLDL IAPSPADAQH WVQGLRKIIH HSGSMDQRQK LQHWIHSCLR 150
    KADKNKDNKM NFKELKDFLK ELNIQVDDGY ARKIFRECDH SQTDSLEDEE 200
    IETFYKMLTQ RAEIDRAFEE AAGSAETLSV ERLVTFLQHQ QREEEAGPAL 250
    ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMDQ 300
    PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ 350
    EPIIYHGYTF TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV 400
    MARHLRAILG PILLDQPLDG VTTSLPSPEQ LKGKILLKGK KLGGLLPAGG 450
    ENGSEATDVS DEVEAAEMED EAVRSQVQHK PKEDKLKLVP ELSDMIIYCK 500
    SVHFGGFSSP GTSGQAFYEM ASFSESRALR LLQESGNGFV RHNVSCLSRI 550
    YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG 600
    YVLKPAFLRD PNTTFNSRAL TQGPWWRPER LRVRIISGQQ LPKVNKNKNS 650
    IVDPKVIVEI HGVGRDTGSR QTAVITNNGF NPRWDMEFEF EVTVPDLALV 700
    RFMVEDYDSS SKNDFIGQST IPWNSLKQGY RHVHLLSKNG DQHPSATLFV 750
    KISIQD 756
    Length:756
    Mass (Da):85,962
    Last modified:July 1, 1989 - v1
    Checksum:iE33F2313AC81E9F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti627 – 6293RPE → APK in AAP31521. (PubMed:1684614)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti412 – 4121I → M in SHR. 1 Publication
    Natural varianti423 – 4231T → S in SHR. 1 Publication
    Natural varianti463 – 4631V → D in SHR. 1 Publication
    Natural varianti668 – 6681G → A in SHR. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20637 mRNA. Translation: AAA41886.1.
    S74591 mRNA. Translation: AAP31521.1.
    PIRiB28821.
    RefSeqiNP_058731.1. NM_017035.1.
    UniGeneiRn.12324.

    Genome annotation databases

    GeneIDi24655.
    KEGGirno:24655.
    UCSCiRGD:3346. rat.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20637 mRNA. Translation: AAA41886.1 .
    S74591 mRNA. Translation: AAP31521.1 .
    PIRi B28821.
    RefSeqi NP_058731.1. NM_017035.1.
    UniGenei Rn.12324.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DJG X-ray 2.60 A/B 133-756 [» ]
    1DJH X-ray 2.50 A/B 133-756 [» ]
    1DJI X-ray 2.50 A/B 133-756 [» ]
    1DJW X-ray 2.45 A/B 133-756 [» ]
    1DJX X-ray 2.30 A/B 133-756 [» ]
    1DJY X-ray 2.80 A/B 133-756 [» ]
    1DJZ X-ray 2.95 A/B 133-756 [» ]
    1MAI X-ray 1.90 A 11-140 [» ]
    1QAS X-ray 2.40 A/B 135-756 [» ]
    1QAT X-ray 3.00 A/B 135-756 [» ]
    2ISD X-ray 2.50 A/B 133-756 [» ]
    DisProti DP00055.
    ProteinModelPortali P10688.
    SMRi P10688. Positions 12-130, 158-756.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246790. 1 interaction.
    MINTi MINT-245440.

    Chemistry

    BindingDBi P10688.
    ChEMBLi CHEMBL1914273.

    PTM databases

    PhosphoSitei P10688.

    Proteomic databases

    PaxDbi P10688.
    PRIDEi P10688.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24655.
    KEGGi rno:24655.
    UCSCi RGD:3346. rat.

    Organism-specific databases

    CTDi 5333.
    RGDi 3346. Plcd1.

    Phylogenomic databases

    eggNOGi NOG149692.
    HOGENOMi HOG000006871.
    HOVERGENi HBG053610.
    InParanoidi P10688.
    KOi K05857.
    PhylomeDBi P10688.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 5301.
    SABIO-RK P10688.

    Miscellaneous databases

    EvolutionaryTracei P10688.
    NextBioi 603990.
    PROi P10688.

    Gene expression databases

    Genevestigatori P10688.

    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.
    IPR028391. PLC-delta1.
    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:SF80. PTHR10336:SF80. 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. 2 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. 2 hits.
    PS50003. PH_DOMAIN. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence of multiple forms of phospholipase C."
      Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.
      Cell 54:161-169(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Phospholipase C-delta gene of the spontaneously hypertensive rat harbors point mutations causing amino acid substitutions in a catalytic domain."
      Yagisawa H., Tanase H., Nojima H.
      J. Hypertens. 9:997-1004(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SHR MET-412; SER-423; ASP-463 AND ALA-668.
      Tissue: Aorta.
    3. "Putative inositol 1,4,5-trisphosphate binding proteins in rat brain cytosol."
      Kanematsu T., Takeya H., Watanabe Y., Ozaki S., Yoshida M., Koga T., Iwanaga S., Hirata M.
      J. Biol. Chem. 267:6518-6525(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 50-57; 128-140 AND 728-738.
      Tissue: Brain.
    4. Lubec G., Diao W.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 61-76, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus.
    5. "Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1."
      Ellis M.V., James S.R., Perisic O., Downes C.P., Williams R.L., Katan M.
      J. Biol. Chem. 273:11650-11659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-311; ASN-312; LEU-320; GLU-341; ASP-343; HIS-356; PHE-360; GLU-390; LYS-438; LYS-440; SER-522; ARG-549; TYR-551 AND TRP-555.
    6. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
      Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
      PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-191 AND THR-193.
    7. "Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain."
      Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.
      Cell 83:1037-1046(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-130.
    8. "C2 domain conformational changes in phospholipase C-delta 1."
      Grobler J.A., Essen L.-O., Williams R.L., Hurley J.H.
      Nat. Struct. Biol. 3:788-795(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 205-756.
    9. "Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta."
      Essen L.-O., Perisic O., Cheung R., Katan M., Williams R.L.
      Nature 380:595-602(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 133-756.
    10. "A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1."
      Essen L.-O., Perisic O., Lynch D.E., Katan M., Williams R.L.
      Biochemistry 36:2753-2762(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-756, CALCIUM-BINDING.

    Entry informationi

    Entry nameiPLCD1_RAT
    AccessioniPrimary (citable) accession number: P10688
    Secondary accession number(s): Q80WI4
    , Q9QVD3, Q9QVD4, Q9QVD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 155 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3