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Entry version 154 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Protein lgg-1

Gene

lgg-1

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

Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes) (PubMed:26687600).

When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy (PubMed:26687600, PubMed:21802374).

Recruits lipidated-lgg-2 to maturing autophagosomes (PubMed:12958363, PubMed:20523114, PubMed:26687600).

Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation (PubMed:26687600).

In particular, binds to components of the unc-51-atg-13 complex to regulate autophagosome formation and cargo sequestration (PubMed:26687600).

Required for the degradation of specific sepa-1- and sqst-1-containing protein aggregates during embryogenesis (PubMed:26687600).

Involved in allophagy, which is an autophagic process in which paternal mitochondria and organelles are degraded during fertilization, and moreover is required for the formation of lgg-2-positive allophagic autophagosomes in embryos (PubMed:24374177).

Involved in the clearance of apoptotic cells by promoting the delivery of engulfed apoptotic cells to the lysosome (PubMed:22451698).

Plays a role in the distribution and clearance of germ cell specific P-granules from somatic cells (PubMed:19167332).

Also plays a role in the autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes (PubMed:30102152).

Involved in xenophagy, the autophagy-mediated degradation of pathogens and pathogen products, such as toxins (PubMed:27875098).

Required for normal survival when exposed to pathogenic bacteria S.typhimurium probably by promoting autophagic degradation of intracellular S.typhimurium (PubMed:19667176).

Also plays a role in membrane-pore repair (PubMed:27875098).

Plays a role in mitophagy (PubMed:25896323).

Essential for dauer development and longevity, including longevity in response to moderate, short-term heat shock, also known as a hormetic heat shock (PubMed:12958363, PubMed:20523114, PubMed:28198373).

11 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei25Required for the interaction with unc-511 Publication1
Sitei28Required for interaction with sqst-11 Publication1
Sitei50Required for the interaction with unc-511 Publication1
Sitei104Required for the interaction with unc-511 Publication1

<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

Biological processAutophagy

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-1632852, Macroautophagy

<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:
Protein lgg-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:lgg-1Imported
Synonyms:atg-8.1Imported
ORF Names:C32D5.9Imported
<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 elegans
<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 II

Organism-specific databases

WormBase

More...
WormBasei
C32D5.9 ; CE01849 ; WBGene00002980 ; lgg-1

<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

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Lysosome, Membrane, Mitochondrion

<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

RNAi-mediated knockdown prevents mitophagy (PubMed:25896323). Accumulation of germ cell specific P-granules in somatic cells as indicated by increased numbers of pgl-1 and pgl-3 positive granules in embryos and L1 stage larva (PubMed:19167332). RNAi-mediated knockdown results in increased numbers of sepa-1- and lgg-2-expressing protein aggregates in embryos (PubMed:26687600). RNAi-mediated knockdown reduces autophagic degradation of membrane pore-forming toxin Cry5B (PubMed:27875098). Impaired survival when exposed to pathogenic bacteria S.typhimurium (PubMed:19667176). Reduces the number of vacuolated (dying) touch receptor neurons in a mec-4 u231, deg-1 u506 or deg-3 u662 mutants (PubMed:17327275). The extended lifespan of animals exposed to hormetic heat shock early in life is signficantly reduced by RNAi-mediated knockdown.7 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>Mutagenesisi2K → A: Mildly impaired membrane tethering activity and fusion in vitro. 1 Publication1
Mutagenesisi3 – 4WA → GG: Impaired membrane tethering activity and fusion in vitro. 1 Publication2
Mutagenesisi3W → G: Does not rescue the protein aggregate degradation defect in the lgg-1 bp500 mutant. 1 Publication1
Mutagenesisi7E → A: Mildly impaired membrane tethering activity and fusion in vitro. 1 Publication1
Mutagenesisi14 – 15RR → AA: Severely impaired membrane tethering activity and fusion in vitro. Does not rescue the degradation defect in the lgg-1 bp500 mutant. 1 Publication2
Mutagenesisi28R → C in bp523; abolishes interaction with sqst-1 and impairs the interaction with epg-7, sepa-1 and unc-51. Defective degradation of sepa-1- and sqst-1-containing aggregates in embryos. No defects in lipidation or puncta formation. 1 Publication1
Mutagenesisi94 – 123Missing in bp500; defective degradation of sepa-1-containing protein aggregates in comma stage embryos. Suppresses the lysosomal accumulation of ribosomal RNA and ribosomal proteins in the rnst-2 qx245 mutant. 2 PublicationsAdd BLAST30
Mutagenesisi102D → A: Defective degradation of sepa-1-containing protein aggregates in embryos. 1 Publication1
Mutagenesisi108A → V: Does not rescue the degradation defect in the lgg-1 bp500 mutant. 1 Publication1
Mutagenesisi116 – 123Missing : Impairs interaction with atg-3. Rescues the protein degradation defect in the atg-4.1 bp501 and atg-4.2 tm3948 single mutants. Does not rescue the lethal phenotype of the atg-4.1 bp501 and atg-4.2 tm3948 double mutant, but partially rescues the protein degradation defect. 2 Publications8
Mutagenesisi116G → A: Diffuse cytosolic localization in 500-cell embryos with no punctate pattern of distribution which is in contrast to wild-type. Not cleaved by atg-4.1 and atg-4.2. Does not rescue the protein degradation defect in the atg-4.1 bp501 mutant. Reduces lgg-2 lipidation and the accumulation of sqst-1-containing aggregates. Abolishes the interaction with atg-3. 3 Publications1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004382821 – 116Protein lgg-1Add BLAST116
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000212377117 – 123Removed in mature form2 Publications7

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(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi116Phosphatidylethanolamine amidated glycine2 Publications1 Publication1

<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

Cleaved by atg-4.1 and/or atg-4.2, after Gly-116 to form a thioester bond with 'Cys-523' of atg-7 (E1-like activating enzyme) before being transferred to 'Cys-255' of atg-3 (E2 conjugating enzyme), in order to be amidated with phosphatidylethanolamine (Probable) (PubMed:26687600, PubMed:22767594). This lipid modification anchors lgg-1 to membranes and can be reversed by atg-4.2, releasing soluble lgg-1 (PubMed:30880001). Lipidation regulates lgg-2-positive autophagosome formation (PubMed:26687600).5 Publications3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei116 – 117Cleavage2 Publications1 Publication2

Keywords - PTMi

Lipoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q09490

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

More...
PaxDbi
Q09490

PeptideAtlas

More...
PeptideAtlasi
Q09490

PRoteomics IDEntifications database

More...
PRIDEi
Q09490

<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

Expressed in PLML touch receptor neuron and in the ventral nerve cord (PubMed:17327275). Expressed in AIY interneurons (PubMed:30880001).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 during embryogenesis (PubMed:19167332, PubMed:24374177, PubMed:28806108, PubMed:20550938, PubMed:24185444, PubMed:26687600). First expressed at the 20 cell stage with expression peaking at the 80-100 cell stage, and decreasing as development continues (PubMed:20550938, PubMed:24185444, PubMed:28806108, PubMed:22767594). Undetectable at the comma stage (PubMed:28806108).7 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced in response to a moderate, short-term heat stess, also known as a hormetic heat stess.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00002980, Expressed in multi-cellular organism and 5 other tissues

<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

Interacts with sepa-1 (via the LIR motifs); the interaction is direct (PubMed:19167332, PubMed:26687600).

Interacts with allo-1 (via the LIR motif) (PubMed:29255173).

Interacts with sqst-1 (via the LIR motifs); the interaction is direct (PubMed:26687600). Both lipidated and unlipidated forms interact with epg-7 (via the LIR motif); the interaction is direct (PubMed:26687600).

Interacts with epg-2 (via the LIR motifs); the interaction is direct (PubMed:26687600).

Interacts with atg-13; the interaction is direct (PubMed:26687600).

Interacts with unc-51 (via the LIR motif); the interaction is direct (PubMed:26687600).

Interacts with atg-7; the interaction is direct (PubMed:26687600).

Interacts with atg-3 (PubMed:26687600). The interaction with atg-7 and atg-3 may be required for the lipidation of lgg-1 (PubMed:26687600).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
39390, 77 interactors

Database of interacting proteins

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DIPi
DIP-27176N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q09490

Protein interaction database and analysis system

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IntActi
Q09490, 9 interactors

Molecular INTeraction database

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MINTi
Q09490

STRING: functional protein association networks

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STRINGi
6239.C32D5.9

<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

1123
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

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SMRi
Q09490

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ATG8 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1654, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000168096

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_119276_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q09490

Identification of Orthologs from Complete Genome Data

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OMAi
MTTMGQL

Database of Orthologous Groups

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OrthoDBi
1508198at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q09490

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004241, Atg8-like
IPR029071, Ubiquitin-like_domsf

The PANTHER Classification System

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PANTHERi
PTHR10969, PTHR10969, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02991, Atg8, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54236, SSF54236, 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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q09490-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKWAYKEENN FEKRRAEGDK IRRKYPDRIP VIVEKAPKSK LHDLDKKKYL
60 70 80 90 100
VPSDLTVGQF YFLIRKRIQL RPEDALFFFV NNVIPQTMTT MGQLYQDHHE
110 120
EDLFLYIAYS DESVYGGEVE KKE
Length:123
Mass (Da):14,764
Last modified:November 1, 1996 - 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:iBC08727A3101875A
GO

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
BX284602 Genomic DNA Translation: CCD66037.1
AF326943 mRNA Translation: AAG49393.1

Protein sequence database of the Protein Information Resource

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PIRi
T15740

NCBI Reference Sequences

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RefSeqi
NP_495277.1, NM_062876.5

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C32D5.9.1; C32D5.9.1; WBGene00002980

Database of genes from NCBI RefSeq genomes

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GeneIDi
174050

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C32D5.9

UCSC genome browser

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UCSCi
C32D5.9.1, c. elegans

<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
BX284602 Genomic DNA Translation: CCD66037.1
AF326943 mRNA Translation: AAG49393.1
PIRiT15740
RefSeqiNP_495277.1, NM_062876.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AZFX-ray1.60A/B1-116[»]
5AZGX-ray1.81A/B1-116[»]
SMRiQ09490
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi39390, 77 interactors
DIPiDIP-27176N
ELMiQ09490
IntActiQ09490, 9 interactors
MINTiQ09490
STRINGi6239.C32D5.9

Proteomic databases

EPDiQ09490
PaxDbiQ09490
PeptideAtlasiQ09490
PRIDEiQ09490

Genome annotation databases

EnsemblMetazoaiC32D5.9.1; C32D5.9.1; WBGene00002980
GeneIDi174050
KEGGicel:CELE_C32D5.9
UCSCiC32D5.9.1, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
174050
WormBaseiC32D5.9 ; CE01849 ; WBGene00002980 ; lgg-1

Phylogenomic databases

eggNOGiKOG1654, Eukaryota
GeneTreeiENSGT00940000168096
HOGENOMiCLU_119276_0_0_1
InParanoidiQ09490
OMAiMTTMGQL
OrthoDBi1508198at2759
PhylomeDBiQ09490

Enzyme and pathway databases

ReactomeiR-CEL-1632852, Macroautophagy

Miscellaneous databases

Protein Ontology

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PROi
PR:Q09490

Gene expression databases

BgeeiWBGene00002980, Expressed in multi-cellular organism and 5 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR004241, Atg8-like
IPR029071, Ubiquitin-like_domsf
PANTHERiPTHR10969, PTHR10969, 1 hit
PfamiView protein in Pfam
PF02991, Atg8, 1 hit
SUPFAMiSSF54236, SSF54236, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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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 nameiLGG1_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: Q09490
<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 15, 1998
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 154 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

3D-structure, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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