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Entry version 125 (08 May 2019)
Sequence version 1 (03 Oct 2006)
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Protein

Protein immune deficiency

Gene

imd

Organism
Drosophila melanogaster (Fruit fly)
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

Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria (PubMed:7568155, PubMed:8808632, PubMed:11266367, PubMed:12433364). Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway (PubMed:7568155, PubMed:11269502, PubMed:11703941, PubMed:12433364, PubMed:20122400). Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex (PubMed:11269502, PubMed:12433364, PubMed:20122400). Once in proximity, Dredd cleaves imd in a Fadd-dependent manner to enable its association and activation by the ubiquitin E3-ligase DIAP2 (PubMed:20122400). The activated form of imd recruits and activates the Tab2/Tak1 complex thus acting upstream of the IKK complex (ird5 and key) to activate Rel and induce the expression of antimicrobial peptides such as Def, Dpt and Cecropin (PubMed:7568155, PubMed:8808632, PubMed:11703941, PubMed:12433364, PubMed:19837371, PubMed:20122400, PubMed:11266367). Also able to inhibit the viral replication of the Sindbis virus (PubMed:19763182). Involved in promoting the polyubiquitination and stability of faf which in turn, regulates the Imd pathway by controlling imd polyubiquitination and/or stability; they may therefore form a regulatory feedback mechanism within the Imd pathway (PubMed:23919485). Not required for the cuticle melanization immune response to bacterial challenge (PubMed:11266367).10 Publications

<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 processImmunity, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-214397 Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214399 Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214411 REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214416 Phosphorylated REL is cleaved by and dissociates from DREDD

<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 immune deficiency1 Publication
<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:imd1 PublicationImported
ORF Names:CG5576Imported
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 2R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0013983 imd

<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

<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 in the fat body results in reduced expression of the antimicrobial peptide gene Dpt following infection with E.coli.1 Publication

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>Mutagenesisi30D → A: Loss of function. Abolishes caspase-mediated cleavage and ubiquitination. Blocks expression of Dpt in response to E.coli peptidoglycans (PGN). 1 Publication1
Mutagenesisi31A → V in imd-1; immune response defective. Reduced survival and decreased induction of various antibacterial peptides after bacterial challenge. Abolishes ubiquitination and reduces binding to Diap2 but has no effect on caspase-mediated cleavage. Increased resistance to UV radiation. No effect on survival after infection with the fungus A.fumigatus. No effect on up-regulation of Drs after bacterial challenge. 4 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004454811 – 273Protein immune deficiencyAdd BLAST273

<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

Phosphorylated.1 Publication
Caspase-mediated cleavage is required for activation and function; upon immune stimulation, peptidoglycans (PGN) induce proteolytic cleavage by caspases such as Dredd leading to its ubiquitination.1 Publication
Ubiquitination is essential for function; after PGN-induced caspase-mediated cleavage the N-terminally cleaved imd interacts with the E3 ligase Diap2 leading to polyubiquitination of 'Lys-63'-linked chains involving the E2 complex members Uev1A, ben and Ubc5 (PubMed:20122400). These 'Lys-63' chains stabilize imd and may serve as scaffolds to recruit and activate the key kinases TAK1 and IKK (PubMed:20122400). Under normal unchallenged conditions, scny deubiquitinates the activating 'Lys-63'-linked chains to prevent signal transduction and this is also likely to promote the polyubiquitination of 'Lys-48'-linked chains which act as 'tags' for proteosomal degradation (PubMed:19837371). Usp2 then deubiquitinates the 'Lys-48'-linked chains and this promotes degradation of imd probably by allowing interaction between imd and the proteasome (PubMed:25027767).3 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>Sitei30 – 31Cleavage; by Dredd1 Publication2

Keywords - PTMi

Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q7K4Z4

PRoteomics IDEntifications database

More...
PRIDEi
Q7K4Z4

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0013983 Expressed in 27 organ(s), highest expression level in head

<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 Fadd (PubMed:12433364).

Interacts with faf (PubMed:23919485).

Interacts with Rpt6 (PubMed:25027767).

Interacts (via N-terminus) with Usp2 (via N-terminus) (PubMed:25027767).

Interacts (via N-terminus) with scny (via C-terminus) (PubMed:19837371). The N-terminally cleaved form interacts (via IAP-Binding motif) with Diap2 (via the BIR2 and BIR3 domains); the interaction promotes ubiquitination by Diap2 and the E2 ligases Uev1A, ben and Ubc5 (PubMed:20122400).

5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q7K4Z4

Protein interaction database and analysis system

More...
IntActi
Q7K4Z4, 4 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0085904

<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>Domaini176 – 260DeathPROSITE-ProRule annotationAdd BLAST85

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>Regioni132 – 178May be required for interaction with Fadd1 PublicationAdd BLAST47
Regioni143 – 177Essential for ubiquitination and the induction of Dpt1 PublicationAdd BLAST35

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi31 – 34IAP-binding motif1 Publication4

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410J38S Eukaryota
ENOG4112D3I LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q7K4Z4

KEGG Orthology (KO)

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KOi
K20699

Identification of Orthologs from Complete Genome Data

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OMAi
AIIDHQM

Database of Orthologous Groups

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OrthoDBi
1460301at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q7K4Z4

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00531 Death, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986 SSF47986, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50017 DEATH_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>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.

Q7K4Z4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKLRNLLPT IFGGKEAQNP TPVEGRLEKD AAPVDDNEPD NNNSGALALP
60 70 80 90 100
STAGTPTASS DLTESVLREL SDPNYNSMDV VHSANIPGTL SNVQTNNTMN
110 120 130 140 150
VHSAQQQVVM NFSNANNLHF GSVYNFNQNL SACSSRKGST STAEESVASP
160 170 180 190 200
DGKPRASATR KTVSIVAMMQ SQEEPDVRLL DVVSTHLGEG WKQVMRDLGM
210 220 230 240 250
SEGQIDQAII DHQMHGNIRE VIYQLLLQWI RSSADGVATV GRLTTLLWES
260 270
QHRDCVQRMK LVWKALEKRK TNS
Length:273
Mass (Da):29,899
Last modified:October 3, 2006 - 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:i7247CA4B46F5545B
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAF44326 differs from that shown. Reason: Frameshift at position 254.Curated
The sequence AAF44326 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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

More...
DDBJi
Links Updated
AF222006 mRNA Translation: AAF44326.1 Sequence problems.
AE013599 Genomic DNA Translation: AAF57692.1
AE013599 Genomic DNA Translation: AHN56367.1
AY051558 mRNA Translation: AAK92982.1

NCBI Reference Sequences

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RefSeqi
NP_001286572.1, NM_001299643.1
NP_573394.1, NM_133166.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0086725; FBpp0085904; FBgn0013983
FBtr0345891; FBpp0311815; FBgn0013983

Database of genes from NCBI RefSeq genomes

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GeneIDi
44339

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG5576

UCSC genome browser

More...
UCSCi
CG5576-RA d. melanogaster

<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
AF222006 mRNA Translation: AAF44326.1 Sequence problems.
AE013599 Genomic DNA Translation: AAF57692.1
AE013599 Genomic DNA Translation: AHN56367.1
AY051558 mRNA Translation: AAK92982.1
RefSeqiNP_001286572.1, NM_001299643.1
NP_573394.1, NM_133166.4

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

ELMiQ7K4Z4
IntActiQ7K4Z4, 4 interactors
STRINGi7227.FBpp0085904

Proteomic databases

PaxDbiQ7K4Z4
PRIDEiQ7K4Z4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086725; FBpp0085904; FBgn0013983
FBtr0345891; FBpp0311815; FBgn0013983
GeneIDi44339
KEGGidme:Dmel_CG5576
UCSCiCG5576-RA d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
44339
FlyBaseiFBgn0013983 imd

Phylogenomic databases

eggNOGiENOG410J38S Eukaryota
ENOG4112D3I LUCA
InParanoidiQ7K4Z4
KOiK20699
OMAiAIIDHQM
OrthoDBi1460301at2759
PhylomeDBiQ7K4Z4

Enzyme and pathway databases

ReactomeiR-DME-214397 Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214399 Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214411 REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'
R-DME-214416 Phosphorylated REL is cleaved by and dissociates from DREDD

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
imd fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
44339

Gene expression databases

BgeeiFBgn0013983 Expressed in 27 organ(s), highest expression level in head

Family and domain databases

InterProiView protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
PfamiView protein in Pfam
PF00531 Death, 1 hit
SUPFAMiSSF47986 SSF47986, 1 hit
PROSITEiView protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiIMD_DROME
<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: Q7K4Z4
Secondary accession number(s): Q9NHG0
<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: October 10, 2018
Last sequence update: October 3, 2006
Last modified: May 8, 2019
This is version 125 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 programDrosophila 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. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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