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Protein

Guanyl-specific ribonuclease pgl-3

Gene

pgl-3

Organism
Caenorhabditis elegans
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

Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). P-granule component involved in germline development (PubMed:15238518, PubMed:19372764, PubMed:24746798). Together with the P-granule component pgl-1, is involved in the formation of P-granules (PubMed:21402787, PubMed:24746798, PubMed:27594427). Together with pgl-1, probably recruits other granule components such as pos-1, mex-3 and glh-1, and RNA to P-granules (PubMed:21402787, PubMed:27594427). In vitro, binds mRNA; this interaction is required for the formation of liquid-like droplets that resemble P-granules (PubMed:27594427). Most likely recruits pgl-1 into P-granules during autophagy (PubMed:19167332). Associates with adapters such as sepa-1 and is required for the accumulation and degradation of P-granules by autophagy in somatic cells (PubMed:19167332, PubMed:24140420, PubMed:28806108). This ensures exclusive localization of the P-granules in germ cells (PubMed:19167332, PubMed:28806108). In addition, may act redundantly with pgl-1 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (PubMed:26598553). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (PubMed:26598553). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246).11 Publications

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei437Proton acceptorBy similarity1

<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

  • endonuclease activity Source: UniProtKB-KW
  • ribonuclease T1 activity Source: UniProtKB-EC
  • RNA binding Source: WormBase

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 functionDevelopmental protein, Endonuclease, Hydrolase, Nuclease, RNA-binding

<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:
Guanyl-specific ribonuclease pgl-3Curated (EC:3.1.27.31 Publication)
Alternative name(s):
P granule abnormality protein 3Imported
<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:pgl-3Imported
ORF Names:C18G1.4Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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: Chromosome V

Organism-specific databases

WormBase

More...
WormBasei
C18G1.4a ; CE17420 ; WBGene00003994 ; pgl-3
C18G1.4b ; CE27717 ; WBGene00003994 ; pgl-3

<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

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Viable, and not temperature sensitive (PubMed:15238518). Failed degradation and diffuse cytoplasmic localization of the P-granule component pgl-1 in the somatic cells of embryos (PubMed:19167332). Increased germ cell apoptosis in gonadal arms, and this is further increased following UV irradiation (PubMed:26598553). Double knockout with pgl-1 results in 37% of progeny arresting as late embryos and 9% as larvae at 26 degrees Celsius (PubMed:15238518). Double knockout with pgl-1 enhances the temperature-sensitive sterility phenotype and germline defects of the pgl-1 single knockout (PubMed:15238518, PubMed:26598553). Germline defects include increased apoptosis in the gonad, fewer germ nuclei, no sperm and no oocytes in the gonad arms (PubMed:15238518, PubMed:26598553). The gonads of the double knockout with pgl-1 degenerate as the adults age (PubMed:15238518). Conversely, double knockout with ced-1 results in reduced somatic cell apoptosis (PubMed:27650246). Triple knockout with pgl-1 and pgl-2 results in 58% of progeny arresting as late embryos and 5% as larvae at 26 degrees Celsius (PubMed:15238518). Triple knockout with pgl-1 and him-3 further reduces the number of self-cross progeny as compared to the pgl-1 and him-3 double mutant and him-3 single mutant (PubMed:15238518). Double RNAi-mediated knockdown with pgl-1 results in a reduced number of pos-1, mex-1 and glh-1 positive granules in embryos (PubMed:21402787). Quadruple RNAi-mediated knockdown with glh-1, glh-4 and pgl-1 results in offspring that display 27-89% sterility, abnormal oocytes and do not have embryos in the uterus (PubMed:24746798). These sterile offspring still produce sperm (PubMed:24746798). Furthermore, these offspring may have compromised P-granule integrity as there is diffuse cytoplasmic localization of the P-granule component deps-1, which may cause germ cells to initiate somatic reprogramming (PubMed:24746798). RNAi-mediated knockdown in a double ced-1 and hpl-2 mutant background rescues the reduced somatic cell apoptotic cell defect in the ced-1 and hpl-2 double knockout at 25 degrees Celsius (PubMed:27650246).6 Publications

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>Mutagenesisi627R → A: No effect on methylation of the RNA-binding RGG-box. 1 Publication1
Mutagenesisi633 – 692Missing : Globular cytoplasmic granules form, but do not contain the P-granule components such as pos-1. 1 PublicationAdd BLAST60
Mutagenesisi634R → A: No effect on methylation of the RNA-binding RGG-box. 1 Publication1
Mutagenesisi634R → L: Abolishes RNA-binding; when associated with G-638; L-650; G-661; G-665 and G-690. 1 Publication1
Mutagenesisi638R → A: No effect on methylation of the RNA-binding RGG-box. 1 Publication1
Mutagenesisi638R → G: Abolishes RNA-binding; when associated with L-634; L-650; G-661; G-665 and G-690. 1 Publication1
Mutagenesisi641R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-650; A-658; A-661; A-665; A-668; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi648R → A: No effect on methylation of the RNA-binding RGG-box. 1 Publication1
Mutagenesisi650R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-658; A-661; A-665; A-668; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi650R → L: Abolishes RNA-binding; when associated with L-634; G-638; G-661; G-665 and G-690. 1 Publication1
Mutagenesisi658R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-661; A-665; A-668; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi661R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-665; A-668; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi661R → G: Abolishes RNA-binding; when associated with L-634; G-638; L-650; G-665 and G-690. 1 Publication1
Mutagenesisi665R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-661; A-668; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi665R → G: Abolishes RNA-binding; when associated with L-634; G-638; L-650; G-661 and G-690. 1 Publication1
Mutagenesisi668R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-661; A-665; A-676; A-682 and A-690. 1 Publication1
Mutagenesisi676R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-661; A-665; A-668; A-682 and A-690. 1 Publication1
Mutagenesisi682R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-661; A-665; A-668; A-676 and A-690. 1 Publication1
Mutagenesisi690R → A: Reduces methylation of the RNA-binding RGG-box. Abolishes methylation of the RNA-binding RGG-box; when associated with A-641; A-650; A-658; A-661; A-665; A-668; A-676 and A-682. 1 Publication1
Mutagenesisi690R → G: Abolishes RNA-binding; when associated with L-634; G-638; L-650; G-661 and G-665. 1 Publication1

<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_00004430171 – 693Guanyl-specific ribonuclease pgl-3CuratedAdd BLAST693

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Methylated at arginine residues in the RNA-binding RGG-box by prmt-1. Methylation promotes P-granule degradation by autophagy.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
G5EBV6

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

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PaxDbi
G5EBV6

PeptideAtlas

More...
PeptideAtlasi
G5EBV6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in the germline (PubMed:15238518). Expressed in most somatic cells (PubMed:27650246).2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed throughout development from embryos to adults (PubMed:15238518, PubMed:27650246). Not expressed in somatic cells of embryos (PubMed:28806108). First expressed in 1-cell embryos, and expression continues until the 24-cell stage (PubMed:15238518). Highly expressed in early stage embryos (PubMed:19167332). Expression decreases after the 24-cell stage and is negligible throughout the rest of embryogenesis and early stages of larval development (PubMed:15238518, PubMed:19167332). During larval development, first expressed in the germline of L3 stage larvae (PubMed:15238518).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
WBGene00003994 Expressed in 4 organ(s), highest expression level in germ line (C elegans)

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

May form a homodimer (PubMed:21402787, PubMed:26787882). Interacts with pgl-1 and pgl-2; this association is not required for P-granule localization of either pgl-1 or pgl-2 (PubMed:15238518). Interacts with sepa-1; the interaction is enhanced in the presence of RNA (PubMed:19167332, PubMed:24140420). Interacts with prmt-1; the interaction is direct (PubMed:24140420).1 Publication4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
sepa-1G5EC375EBI-328338,EBI-2256317

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
G5EBV6, 1 interactor

STRING: functional protein association networks

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STRINGi
6239.C18G1.4a

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
G5EBV6

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

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SMRi
G5EBV6

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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

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>Regioni205 – 447Involved in dimerization1 PublicationAdd BLAST243
Regioni581 – 614Required for interaction with sepa-11 PublicationAdd BLAST34
Regioni633 – 693RNA-binding RGG-box1 Publication1 PublicationAdd BLAST61

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The dimerization domain also acts as a hinge; changes in its structure probably impact oligomerization and RNA-binding.1 Publication
The RNA-binding RGG-box is required for the recruitment of some P-granule components such as pos-1 and probably mRNA, but is dispensable for granule formation.2 Publications1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410KABH Eukaryota
ENOG4110IF4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008064

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000017375

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
G5EBV6

Identification of Orthologs from Complete Genome Data

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OMAi
LEHYENE

Database of Orthologous Groups

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OrthoDBi
EOG091G0CPD

Database for complete collections of gene phylogenies

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PhylomeDBi
G5EBV6

<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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform aImported (identifier: G5EBV6-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MEANKRQIVE VDGIKSYFFP HLAHYLASND ELLVNNIAQA NKLAAFVLGA
60 70 80 90 100
TDKRPSNEEI AEMILPNDSS AYVLAAGMDV CLILGDDFRP KFDSGAEKLS
110 120 130 140 150
QLGQAHDLAP IIDDEKKISM LARKTKLKKS NDAKILQVLL KVLGAEEAEE
160 170 180 190 200
KFVELSELSS ALDLDFDVYV LAKLLGFASE ELQEEIEIIR DNVTDAFEAC
210 220 230 240 250
KPLLKKLMIE GPKIDSVDPF TQLLLTPQEE SIEKAVSHIV ARFEEASAVE
260 270 280 290 300
DDESLVLKSQ LGYQLIFLVV RSLADGKRDA SRTIQSLMPS SVRAEVFPGL
310 320 330 340 350
QRSVFKSAVF LASHIIQVFL GSMKSFEDWA FVGLAEDLES TWRRRAIAEL
360 370 380 390 400
LKKFRISVLE QCFSQPIPLL PQSELNNETV IENVNNALQF ALWITEFYGS
410 420 430 440 450
ESEKKSLNQL QFLSPKSKNL LVDSFKKFAQ GLDSKDHVNR IIESLEKSSS
460 470 480 490 500
SEPSATAKQT TTSNGPTTVS TAAQVVTVEK MPFSRQTIPC EGTDLANVLN
510 520 530 540 550
SAKIIGESVT VAAHDVIPEK LNAEKNDNTP STASPVQFSS DGWDSPTKSV
560 570 580 590 600
ALPPKISTLE EEQEEDTTIT KVSPQPQERT GTAWGSGDAT PVPLATPVNE
610 620 630 640 650
YKVSGFGAAP VASGFGQFAS SNGTSGRGSY GGGRGGDRGG RGAYGGDRGR
660 670 680 690
GGSGDGSRGY RGGDRGGRGS YGEGSRGYQG GRAGFFGGSR GGS
Length:693
Mass (Da):74,845
Last modified:December 14, 2011 - 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:i16DA54282F3D8CB0
GO
Isoform bImported (identifier: G5EBV6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: MEANKRQIVE...DVCLILGDDF → MTPVPTCLLLAWTFALFSGMTSL

Show »
Length:628
Mass (Da):67,704
Checksum:i2B58489D4531108A
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0593081 – 88MEANK…LGDDF → MTPVPTCLLLAWTFALFSGM TSL in isoform b. CuratedAdd BLAST88

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB120729 mRNA Translation: BAC87886.1
BX284605 Genomic DNA Translation: CCD65226.1
BX284605 Genomic DNA Translation: CCD65227.1

Protein sequence database of the Protein Information Resource

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PIRi
T33251

NCBI Reference Sequences

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RefSeqi
NP_504278.1, NM_071877.4 [G5EBV6-1]
NP_504279.1, NM_071878.3 [G5EBV6-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Cel.7203

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C18G1.4a; C18G1.4a; WBGene00003994 [G5EBV6-1]
C18G1.4b; C18G1.4b; WBGene00003994 [G5EBV6-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
178867

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C18G1.4

Keywords - Coding sequence diversityi

Alternative splicing

<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
AB120729 mRNA Translation: BAC87886.1
BX284605 Genomic DNA Translation: CCD65226.1
BX284605 Genomic DNA Translation: CCD65227.1
PIRiT33251
RefSeqiNP_504278.1, NM_071877.4 [G5EBV6-1]
NP_504279.1, NM_071878.3 [G5EBV6-2]
UniGeneiCel.7203

3D structure databases

ProteinModelPortaliG5EBV6
SMRiG5EBV6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiG5EBV6, 1 interactor
STRINGi6239.C18G1.4a

Proteomic databases

EPDiG5EBV6
PaxDbiG5EBV6
PeptideAtlasiG5EBV6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC18G1.4a; C18G1.4a; WBGene00003994 [G5EBV6-1]
C18G1.4b; C18G1.4b; WBGene00003994 [G5EBV6-2]
GeneIDi178867
KEGGicel:CELE_C18G1.4

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
178867
WormBaseiC18G1.4a ; CE17420 ; WBGene00003994 ; pgl-3
C18G1.4b ; CE27717 ; WBGene00003994 ; pgl-3

Phylogenomic databases

eggNOGiENOG410KABH Eukaryota
ENOG4110IF4 LUCA
GeneTreeiENSGT00390000008064
HOGENOMiHOG000017375
InParanoidiG5EBV6
OMAiLEHYENE
OrthoDBiEOG091G0CPD
PhylomeDBiG5EBV6

Miscellaneous databases

Protein Ontology

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PROi
PR:G5EBV6

Gene expression databases

BgeeiWBGene00003994 Expressed in 4 organ(s), highest expression level in germ line (C elegans)

Family and domain databases

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<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 nameiPGL3_CAEEL
<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: G5EBV6
Secondary accession number(s): Q965J2
<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: January 31, 2018
Last sequence update: December 14, 2011
Last modified: December 5, 2018
This is version 67 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 programCaenorhabditis annotation project

<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

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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