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Entry version 190 (16 Oct 2019)
Sequence version 1 (01 Jul 1989)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Note: Binds 3 Ca2+ ions per subunit. Two of the Ca2+ ions are bound to the C2 domain.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3111
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi312Calcium 1; catalytic1
Metal bindingi341Calcium 1; catalytic1
Metal bindingi343Calcium 1; catalytic1
Active sitei3561
Metal bindingi390Calcium 1; catalytic1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei438Substrate1
Binding sitei440Substrate1
Binding sitei522Substrate1
Binding sitei549Substrate1
Metal bindingi651Calcium 2; via carbonyl oxygen1
Metal bindingi653Calcium 21
Metal bindingi677Calcium 21
Metal bindingi706Calcium 31
Metal bindingi707Calcium 3; via carbonyl oxygen1
Metal bindingi708Calcium 31

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi153 – 1641PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi189 – 2002PROSITE-ProRule annotationAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Transducer
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.11 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P10688

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001066

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Plcd1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3346 Plcd1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi311H → A: Lowers activity 10000-fold. 1 Publication1
Mutagenesisi312N → A: Lowers activity 10000-fold. 1 Publication1
Mutagenesisi320L → A: Lowers activity 3-fold. 1 Publication1
Mutagenesisi341E → A, H or Q: Lowers activity 200000-fold. 1 Publication1
Mutagenesisi343D → A: Lowers activity 1000-fold. 1 Publication1
Mutagenesisi343D → R: Lowers activity 100000-fold. 1 Publication1
Mutagenesisi356H → A: Lowers activity 1000-fold. 1 Publication1
Mutagenesisi360F → A: Lowers activity 4-fold. 1 Publication1
Mutagenesisi390E → A, H or K: Lowers activity 1000-fold. 1 Publication1
Mutagenesisi390E → Q: Lowers activity 200-fold. 1 Publication1
Mutagenesisi438K → A: Lowers activity very slightly. 1 Publication1
Mutagenesisi440K → A: No effect on activity towards phosphatidylinositol 4-monophosphate. Lowers activity 5-fold towards phosphatidylinositol 4,5-bisphosphate. 1 Publication1
Mutagenesisi522S → A: Lowers activity 10000-fold. 1 Publication1
Mutagenesisi549R → A: Lowers activity 600-fold. 1 Publication1
Mutagenesisi551Y → A: Lowers activity 600-fold. 1 Publication1
Mutagenesisi555W → A: Lowers activity very slightly. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1914273

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000885061 – 7561-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1Add BLAST756

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi191O-linked (GlcNAc) serine1 Publication1
Glycosylationi193O-linked (GlcNAc) threonine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei457PhosphothreonineBy similarity1
Modified residuei460PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P10688

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P10688

PRoteomics IDEntifications database

More...
PRIDEi
P10688

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10688

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P10688

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246790, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000042824

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P10688

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1756
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P10688

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10688

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini21 – 130PHPROSITE-ProRule annotationAdd BLAST110
Domaini140 – 175EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini176 – 211EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini296 – 440PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini492 – 609PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST118
Domaini630 – 720C2PROSITE-ProRule annotationAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 57Substrate bindingAdd BLAST28

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0169 Eukaryota
ENOG410XPSW LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000006871

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10688

KEGG Orthology (KO)

More...
KOi
K05857

Database of Orthologous Groups

More...
OrthoDBi
368239at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10688

Family and domain databases

Database of protein disorder

More...
DisProti
DP00055

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 1 hit
2.60.40.150, 1 hit
3.20.20.190, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR001192 PI-PLC_fam
IPR028391 PLC-delta1
IPR017946 PLC-like_Pdiesterase_TIM-brl
IPR015359 PLC_EF-hand-like
IPR000909 PLipase_C_PInositol-sp_X_dom
IPR001711 PLipase_C_Pinositol-sp_Y

The PANTHER Classification System

More...
PANTHERi
PTHR10336 PTHR10336, 1 hit
PTHR10336:SF80 PTHR10336:SF80, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00168 C2, 1 hit
PF09279 EF-hand_like, 1 hit
PF16457 PH_12, 1 hit
PF00388 PI-PLC-X, 1 hit
PF00387 PI-PLC-Y, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00390 PHPHLIPASEC

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00239 C2, 1 hit
SM00054 EFh, 2 hits
SM00233 PH, 1 hit
SM00148 PLCXc, 1 hit
SM00149 PLCYc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 1 hit
SSF51695 SSF51695, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE33F2313AC81E9F9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V9D1G3V9D1_RAT
Phosphoinositide phospholipase C
Plcd1 rCG_25198
756Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti627 – 629RPE → APK in AAP31521 (PubMed:1684614).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti412I → M in SHR. 1 Publication1
Natural varianti423T → S in SHR. 1 Publication1
Natural varianti463V → D in SHR. 1 Publication1
Natural varianti668G → A in SHR. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M20637 mRNA Translation: AAA41886.1
S74591 mRNA Translation: AAP31521.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B28821

NCBI Reference Sequences

More...
RefSeqi
NP_058731.1, NM_017035.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24655

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24655

UCSC genome browser

More...
UCSCi
RGD:3346 rat

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
SMRiP10688
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi246790, 1 interactor
STRINGi10116.ENSRNOP00000042824

Chemistry databases

BindingDBiP10688
ChEMBLiCHEMBL1914273
SwissLipidsiSLP:000001066

PTM databases

iPTMnetiP10688
PhosphoSitePlusiP10688

Proteomic databases

jPOSTiP10688
PaxDbiP10688
PRIDEiP10688

Genome annotation databases

GeneIDi24655
KEGGirno:24655
UCSCiRGD:3346 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5333
RGDi3346 Plcd1

Phylogenomic databases

eggNOGiKOG0169 Eukaryota
ENOG410XPSW LUCA
HOGENOMiHOG000006871
InParanoidiP10688
KOiK05857
OrthoDBi368239at2759
PhylomeDBiP10688

Enzyme and pathway databases

BRENDAi3.1.4.11 5301
ReactomeiR-RNO-1855204 Synthesis of IP3 and IP4 in the cytosol
SABIO-RKiP10688

Miscellaneous databases

EvolutionaryTraceiP10688

Protein Ontology

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PROi
PR:P10688

Family and domain databases

DisProtiDP00055
Gene3Di2.30.29.30, 1 hit
2.60.40.150, 1 hit
3.20.20.190, 1 hit
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR001192 PI-PLC_fam
IPR028391 PLC-delta1
IPR017946 PLC-like_Pdiesterase_TIM-brl
IPR015359 PLC_EF-hand-like
IPR000909 PLipase_C_PInositol-sp_X_dom
IPR001711 PLipase_C_Pinositol-sp_Y
PANTHERiPTHR10336 PTHR10336, 1 hit
PTHR10336:SF80 PTHR10336:SF80, 1 hit
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF09279 EF-hand_like, 1 hit
PF16457 PH_12, 1 hit
PF00388 PI-PLC-X, 1 hit
PF00387 PI-PLC-Y, 1 hit
PRINTSiPR00390 PHPHLIPASEC
SMARTiView protein in SMART
SM00239 C2, 1 hit
SM00054 EFh, 2 hits
SM00233 PH, 1 hit
SM00148 PLCXc, 1 hit
SM00149 PLCYc, 1 hit
SUPFAMiSSF47473 SSF47473, 1 hit
SSF51695 SSF51695, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLCD1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10688
Secondary accession number(s): Q80WI4
, Q9QVD3, Q9QVD4, Q9QVD5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 16, 2019
This is version 190 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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