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UniProtKB - Q9Y117 (GALT3_DROME)

Entry version 148 (02 Dec 2020)
Sequence version 1 (01 Nov 1999)
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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

Pgant3

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

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:12829714). It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers EA2 as substrate. Has weak activity toward Muc5AC-3, -13 and -3/13 substrates (PubMed:12829714). Plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface (PubMed:18835818, PubMed:20371600, PubMed:20807760, PubMed:22157008). Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure (PubMed:20807760). Together with Pgant35A, regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles (PubMed:25253852).6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mn2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei190SubstrateBy similarity1
Binding sitei220SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi243ManganeseBy similarity1
Metal bindingi245ManganeseBy similarity1
Binding sitei352SubstrateBy similarity1
Metal bindingi380ManganeseBy similarity1
Binding sitei383SubstrateBy similarity1
Binding sitei388SubstrateBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.41, 1994

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-DME-190372, FGFR3c ligand binding and activation
R-DME-913709, O-linked glycosylation of mucins

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM13, Carbohydrate-Binding Module Family 13
GT27, Glycosyltransferase Family 27

<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%5Fand%5Ftaxonomy%5Fsection">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:
Polypeptide N-acetylgalactosaminyltransferase 3 (EC:2.4.1.411 Publication)
Short name:
pp-GaNTase 3
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Pgant3Imported
ORF Names:CG4445Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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		FBgn0027558, Pgant3

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei13 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini36 – 667LumenalSequence analysisAdd BLAST632

Keywords - Cellular componenti

Golgi apparatus, Membrane

<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

Mutant larval wing disks show a decrease in thickness and in the content of O-glycoproteins specifically along the basal surface of the columnar epithelial cells (PubMed:18835818, PubMed:20371600). Adult mutants display blistered wings (PubMed:18835818, PubMed:20371600). Mutant larval shows down-regulation of synaptic O-linked glycosylation, integrin level and signaling via Ten-m and if. Synapses show smaller synaptic boutons, expanded activity-dependent postsynaptic pockets which affect synaptic plasticity and synaptic strength in both the pre-synaptic and post-synaptic assembly, no differences in neuromuscular junction morphology (PubMed:25253852). Simultaneous knockout of Pgant35A, restores normal synaptic strength (PubMed:25253852). RNAi-mediated knockdown in the developing wing results in a blistered phenotype (PubMed:22157008).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi130R → C: Does not affect subcellular location. Loss of catalytic activity. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000591571 – 667Polypeptide N-acetylgalactosaminyltransferase 3Add BLAST667

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi75N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi129N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi140 ↔ 375PROSITE-ProRule annotation
Glycosylationi279N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi313N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi366 ↔ 446PROSITE-ProRule annotation
Glycosylationi433N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi526 ↔ 547PROSITE-ProRule annotation
Disulfide bondi572 ↔ 601PROSITE-ProRule annotation
Glycosylationi590N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi626 ↔ 649PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...PaxDbi		Q9Y117

PRoteomics IDEntifications database

More...PRIDEi		Q9Y117

<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 developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordiums of the foregut, midgut and hindgut. During embryonic stages 12-13, expression is found uniquely in the posterior spiracle. During embryonic stages 14-17, expressed in the pharynx, esophagus and posterior spiracles. Expression observed in the epidermis during embryonic stages 16-17. In third instar larvae, expressed ubiquitously in wing, with increased expression in pleura and notum, eye-antennal, leg and haltere imaginal disks.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 both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0027558, Expressed in embryo and 50 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Y117, DM

<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		61516, 6 interactors

Protein interaction database and analysis system

More...IntActi		Q9Y117, 2 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0088130

<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%5Fand%5Fdomains%5Fsection">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>Domaini513 – 661Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST149

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>Regioni149 – 259Catalytic subdomain AAdd BLAST111
Regioni321 – 383Catalytic subdomain BAdd BLAST63

<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

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

<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 glycosyltransferase 2 family. GalNAc-T subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3736, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013477_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9Y117

Identification of Orthologs from Complete Genome Data

More...OMAi		FAFFMFA

Database of Orthologous Groups

More...OrthoDBi		606683at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Y117

Family and domain databases

Conserved Domains Database

More...CDDi		cd00161, RICIN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans
IPR035992, Ricin_B-like_lectins
IPR000772, Ricin_B_lectin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00535, Glycos_transf_2, 1 hit
PF00652, Ricin_B_lectin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00458, RICIN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50370, SSF50370, 1 hit
SSF53448, SSF53448, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50231, RICIN_B_LECTIN, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9Y117-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP 
        60         70         80         90        100
PKRRSLWPHK NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV 
       110        120        130        140        150
VPPRDRFRMQ RFFRLNSFNL LASDRIPLNR TLKDYRTPEC RDKKYASGLP 
       160        170        180        190        200
STSVIIVFHN EAWSVLLRTI TSVINRSPRH LLKEIILVDD ASDRSYLKRQ 
       210        220        230        240        250
LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT FLDAHCECSR 
       260        270        280        290        300
GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR 
       310        320        330        340        350
WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR 
       360        370        380        390        400
VWGGENVEMS FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD 
       410        420        430        440        450
NLARAATVWM DDWQYFIMLY TSGLTLGAKD KVNVTERVAL RERLQCKPFS 
       460        470        480        490        500
WYLENIWPEH FFPAPDRFFG KIIWLDGETE CAQAYSKHMK NLPGRALSRE 
       510        520        530        540        550
WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS AVTVGDCTSH 
       560        570        580        590        600
AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ 
       610        620        630        640        650
CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD 
       660 
FKDITQKWGF IPLPWRM
Length:667
Mass (Da):76,807
Last modified:November 1, 1999 - 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:iB8C6924AA8E19805
GO

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
AE013599 Genomic DNA Translation: AAF59298.1
AF145655 mRNA Translation: AAD38630.1

NCBI Reference Sequences

More...RefSeqi		NP_610256.1, NM_136412.4

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0089061; FBpp0088130; FBgn0027558

Database of genes from NCBI RefSeq genomes

More...GeneIDi		35627

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG4445

<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
AE013599 Genomic DNA Translation: AAF59298.1
AF145655 mRNA Translation: AAD38630.1
RefSeqiNP_610256.1, NM_136412.4

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

BioGRIDi61516, 6 interactors
IntActiQ9Y117, 2 interactors
STRINGi7227.FBpp0088130

Protein family/group databases

CAZyiCBM13, Carbohydrate-Binding Module Family 13
GT27, Glycosyltransferase Family 27

Proteomic databases

PaxDbiQ9Y117
PRIDEiQ9Y117

Genome annotation databases

EnsemblMetazoaiFBtr0089061; FBpp0088130; FBgn0027558
GeneIDi35627
KEGGidme:Dmel_CG4445

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		35627
FlyBaseiFBgn0027558, Pgant3

Phylogenomic databases

eggNOGiKOG3736, Eukaryota
HOGENOMiCLU_013477_0_1_1
InParanoidiQ9Y117
OMAiFAFFMFA
OrthoDBi606683at2759
PhylomeDBiQ9Y117

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.41, 1994
ReactomeiR-DME-190372, FGFR3c ligand binding and activation
R-DME-913709, O-linked glycosylation of mucins

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		35627, 0 hits in 1 CRISPR screen

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

More...ChiTaRSi		pgant3, fly

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

More...GenomeRNAii		35627

Protein Ontology

More...PROi		PR:Q9Y117

Gene expression databases

BgeeiFBgn0027558, Expressed in embryo and 50 other tissues
GenevisibleiQ9Y117, DM

Family and domain databases

CDDicd00161, RICIN, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173, Glyco_trans_2-like
IPR029044, Nucleotide-diphossugar_trans
IPR035992, Ricin_B-like_lectins
IPR000772, Ricin_B_lectin
PfamiView protein in Pfam
PF00535, Glycos_transf_2, 1 hit
PF00652, Ricin_B_lectin, 1 hit
SMARTiView protein in SMART
SM00458, RICIN, 1 hit
SUPFAMiSSF50370, SSF50370, 1 hit
SSF53448, SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231, RICIN_B_LECTIN, 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 nameiGALT3_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: Q9Y117
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: December 2, 2020
This is version 148 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

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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