Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

Plcd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Ca2+Note: Binds 3 Ca(2+) ions per subunit. Two of the Ca2+ 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

  • calcium ion binding Source: RGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: RGD
  • phosphatidylinositol phospholipase C activity Source: RGD
  • phospholipid binding Source: RGD
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • cytosolic calcium ion homeostasis Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • intracellular signal transduction Source: InterPro
  • lipid catabolic process Source: UniProtKB-KW
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: RGD
  • positive regulation of inositol trisphosphate biosynthetic process Source: RGD
  • positive regulation of norepinephrine secretion Source: RGD
  • regulation of phospholipase C activity Source: RGD
  • response to aluminum ion Source: RGD
  • response to calcium ion Source: RGD
  • response to hyperoxia Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to prostaglandin F Source: RGD
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

RGDi3346. Plcd1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • membrane Source: RGD
  • membrane raft Source: RGD
  • mitochondrial membrane Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

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
Modified residuei460 – 4601PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10688.
PRIDEiP10688.

PTM databases

PhosphoSiteiP10688.

Expressioni

Gene expression databases

GenevisibleiP10688. RN.

Interactioni

Protein-protein interaction databases

BioGridi246790. 1 interaction.
MINTiMINT-245440.
STRINGi10116.ENSRNOP00000042824.

Structurei

Secondary structure

1
756
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 248Combined sources
Beta strandi26 – 3510Combined sources
Beta strandi37 – 448Combined sources
Beta strandi48 – 536Combined sources
Turni62 – 654Combined sources
Beta strandi66 – 683Combined sources
Helixi69 – 713Combined sources
Beta strandi72 – 798Combined sources
Helixi82 – 876Combined sources
Helixi93 – 953Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi108 – 1114Combined sources
Helixi115 – 12915Combined sources
Beta strandi159 – 1613Combined sources
Helixi162 – 1709Combined sources
Turni171 – 1733Combined sources
Helixi178 – 1803Combined sources
Helixi181 – 1888Combined sources
Beta strandi190 – 1978Combined sources
Helixi203 – 2086Combined sources
Helixi212 – 22211Combined sources
Beta strandi225 – 2295Combined sources
Helixi230 – 23910Combined sources
Helixi248 – 25811Combined sources
Helixi262 – 2665Combined sources
Helixi272 – 2809Combined sources
Turni282 – 2843Combined sources
Beta strandi285 – 2873Combined sources
Helixi289 – 2924Combined sources
Helixi302 – 3043Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi319 – 3213Combined sources
Helixi326 – 3349Combined sources
Beta strandi339 – 3457Combined sources
Helixi348 – 3503Combined sources
Beta strandi353 – 3553Combined sources
Turni357 – 3604Combined sources
Helixi366 – 37611Combined sources
Turni377 – 3793Combined sources
Beta strandi385 – 3928Combined sources
Helixi395 – 40915Combined sources
Helixi410 – 4123Combined sources
Turni428 – 4336Combined sources
Beta strandi435 – 4395Combined sources
Helixi490 – 4934Combined sources
Beta strandi496 – 5027Combined sources
Beta strandi509 – 5146Combined sources
Beta strandi519 – 5246Combined sources
Helixi525 – 54521Combined sources
Beta strandi548 – 5514Combined sources
Helixi565 – 5684Combined sources
Turni569 – 5713Combined sources
Beta strandi574 – 5774Combined sources
Helixi584 – 59411Combined sources
Helixi596 – 5983Combined sources
Beta strandi600 – 6034Combined sources
Helixi606 – 6094Combined sources
Beta strandi629 – 64012Combined sources
Helixi644 – 6463Combined sources
Beta strandi648 – 6503Combined sources
Beta strandi654 – 66310Combined sources
Helixi664 – 6663Combined sources
Beta strandi668 – 6714Combined sources
Beta strandi679 – 6813Combined sources
Beta strandi683 – 69311Combined sources
Helixi695 – 6973Combined sources
Beta strandi699 – 7068Combined sources
Beta strandi709 – 7113Combined sources
Beta strandi714 – 7229Combined sources
Helixi723 – 7253Combined sources
Beta strandi729 – 7368Combined sources
Beta strandi742 – 75514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
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

        10         20         30         40         50
MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT
60 70 80 90 100
IWQESRKVMR SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV
110 120 130 140 150
FKDQRNTLDL IAPSPADAQH WVQGLRKIIH HSGSMDQRQK LQHWIHSCLR
160 170 180 190 200
KADKNKDNKM NFKELKDFLK ELNIQVDDGY ARKIFRECDH SQTDSLEDEE
210 220 230 240 250
IETFYKMLTQ RAEIDRAFEE AAGSAETLSV ERLVTFLQHQ QREEEAGPAL
260 270 280 290 300
ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMDQ
310 320 330 340 350
PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ
360 370 380 390 400
EPIIYHGYTF TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV
410 420 430 440 450
MARHLRAILG PILLDQPLDG VTTSLPSPEQ LKGKILLKGK KLGGLLPAGG
460 470 480 490 500
ENGSEATDVS DEVEAAEMED EAVRSQVQHK PKEDKLKLVP ELSDMIIYCK
510 520 530 540 550
SVHFGGFSSP GTSGQAFYEM ASFSESRALR LLQESGNGFV RHNVSCLSRI
560 570 580 590 600
YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG
610 620 630 640 650
YVLKPAFLRD PNTTFNSRAL TQGPWWRPER LRVRIISGQQ LPKVNKNKNS
660 670 680 690 700
IVDPKVIVEI HGVGRDTGSR QTAVITNNGF NPRWDMEFEF EVTVPDLALV
710 720 730 740 750
RFMVEDYDSS SKNDFIGQST IPWNSLKQGY RHVHLLSKNG DQHPSATLFV

KISIQD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M20637 mRNA. Translation: AAA41886.1.
S74591 mRNA. Translation: AAP31521.1.
PIRiB28821.
RefSeqiNP_058731.1. NM_017035.1.
UniGeneiRn.12324.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi246790. 1 interaction.
MINTiMINT-245440.
STRINGi10116.ENSRNOP00000042824.

Chemistry

BindingDBiP10688.
ChEMBLiCHEMBL1914273.

PTM databases

PhosphoSiteiP10688.

Proteomic databases

PaxDbiP10688.
PRIDEiP10688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5333.
RGDi3346. Plcd1.

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiP10688.
KOiK05857.
PhylomeDBiP10688.

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.
SABIO-RKP10688.

Miscellaneous databases

EvolutionaryTraceiP10688.
NextBioi603990.
PROiP10688.

Gene expression databases

GenevisibleiP10688. RN.

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.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
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]
ProtoNetiSearch...

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: July 22, 2015
This is version 163 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.