Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q8MV48 (GALT7_DROME)

Entry version 134 (18 Sep 2019)
Sequence version 2 (16 Aug 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

N-acetylgalactosaminyltransferase 7

Gene

Pgant7

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

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (PubMed:11925450, PubMed:12829714). In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties (PubMed:11925450). Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the monoglycosylated Muc5AC-3 as substrate (PubMed:11925450). 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).3 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

<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_section">'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.2 Publications
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_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei182SubstrateBy similarity1
Binding sitei212SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi235ManganeseBy similarity1
Metal bindingi237ManganeseBy similarity1
Binding sitei344SubstrateBy similarity1
Metal bindingi372ManganeseBy similarity1
Binding sitei375SubstrateBy similarity1
Binding sitei380SubstrateBy 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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		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_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:
N-acetylgalactosaminyltransferase 7 (EC:2.4.1.412 Publications)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Short name:
pp-GaNTase 7
dGalNAc-T2
<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:Pgant7Imported
Synonyms:GalNAc-T2Imported
ORF Names:CG6394
<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 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_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 X

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0030930 Pgant7

<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_location_section">'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 – 11CytoplasmicSequence analysisAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei12 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST18
Topological domaini30 – 591LumenalSequence analysisAdd BLAST562

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

RNAi-mediated knockdown in the whole body or respiratory system during development is lethal (PubMed:22157008). RNAi-mediated knockdown in hemocytes, amnioserosa, mesoderm or digestive system and reproductive tract causes no defect (PubMed:22157008).1 Publication

<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_00000591611 – 591N-acetylgalactosaminyltransferase 7Add BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi30N-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 bondi132 ↔ 367PROSITE-ProRule annotation
Disulfide bondi358 ↔ 441PROSITE-ProRule annotation
Disulfide bondi479 ↔ 496PROSITE-ProRule annotation
Disulfide bondi519 ↔ 532PROSITE-ProRule annotation
Disulfide bondi558 ↔ 573PROSITE-ProRule annotation
Glycosylationi576N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...PaxDbi		Q8MV48

PRoteomics IDEntifications database

More...PRIDEi		Q8MV48

PTM databases

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q8MV48

<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 primordium of the foregut, midgut and hindgut. Expressed in the salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. During embryonic stages 16-17, expressed in the antennomaxillary complex. In third instar larvae, ubiquitously expressed in wing, with increased expression in the notum and ventral wing pouch, 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, with increasing levels during larval development.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0030930 Expressed in 47 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila)

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8MV48 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8MV48 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		59149, 4 interactors

Protein interaction database and analysis system

More...IntActi		Q8MV48, 4 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0074396

<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

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

More...SMRi		Q8MV48

Database of comparative protein structure models

More...ModBasei		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

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>Domaini466 – 585Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST120

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>Regioni141 – 251Catalytic subdomain AAdd BLAST111
Regioni313 – 375Catalytic 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
ENOG410XPMK LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8MV48

KEGG Orthology (KO)

More...KOi		K00710

Identification of Orthologs from Complete Genome Data

More...OMAi		NFEYRPV

Database of Orthologous Groups

More...OrthoDBi		606683at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8MV48

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

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

Q8MV48-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVSTIRSGR ICRLALCLLV LLPLLYLLAN WSDHHKRVQE AYHTRFGGPK 
        60         70         80         90        100
FAHQRLEGRP REVPKLVDGL GNFEPKDVKP RSGPGENGEA HSLSPDKKHM 
       110        120        130        140        150
SDASEMEYGM NIACSDEISM HRSVRDTRLE ECRHWDYPFD LPRTSVIIVF 
       160        170        180        190        200
HNEGFSVLMR TVHSVIDRSP THMLHEIILV DDFSDKENLR SQLDEYVLQF 
       210        220        230        240        250
KGLVKVIRNK EREGLIRTRS RGAMEATGEV IVFLDAHCEV NTNWLPPLLA 
       260        270        280        290        300
PIYRDRTVMT VPIIDGIDHK NFEYRPVYGT DNHFRGIFEW GMLYKENEVP 
       310        320        330        340        350
RREQRRRAHN SEPYRSPTHA GGLFAINREY FLELGAYDPG LLVWGGENFE 
       360        370        380        390        400
LSFKIWQCGG SIEWVPCSRV GHVYRGFMPY NFGKLASKKK GPLITINYKR 
       410        420        430        440        450
VIETWFDDTH KEYFYTREPL ARYLDMGDIS EQLALKKRLN CKSFQWFMDH 
       460        470        480        490        500
IAYDVYDKFP GLPANLHWGE LRSVASDGCL DSMGHQPPAI MGLTYCHGGG 
       510        520        530        540        550
NNQLVRLNAA GQLGVGERCV EADRQGIKLA VCRLGTVDGP WQYNEHTKHL 
       560        570        580        590 
MHRVHKKCMA LHPATQQLSL GHCDVNDSYQ QWWFKEIRPR W
Length:591
Mass (Da):68,333
Last modified:August 16, 2004 - v2
<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:i6CC2F7DC38E4CF17
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X2JEA3X2JEA3_DROME
Polypeptide N-acetylgalactosaminylt...
Pgant7 anon-WO02059370.15, dGalNAc-T2, Dmel\CG6394, GalNAc-T2, PGANT7
591Annotation score:

Annotation score:3 out of 5

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

<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 AAL13889 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL28887 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti84P → S in AAM62412 (PubMed:11925450).Curated1

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
AF493067 mRNA Translation: AAM62412.1
AY268068 mRNA Translation: AAQ56704.1
AE014298 Genomic DNA Translation: AAF48851.1
AE014298 Genomic DNA Translation: AAN09470.1
BT016123 mRNA Translation: AAV37008.1
AY058660 mRNA Translation: AAL13889.1 Different initiation.
AY061339 mRNA Translation: AAL28887.1 Different initiation.

NCBI Reference Sequences

More...RefSeqi		NP_001285406.1, NM_001298477.1
NP_573301.2, NM_133073.3
NP_728178.1, NM_167623.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0074624; FBpp0074395; FBgn0030930
FBtr0074625; FBpp0074396; FBgn0030930
FBtr0346082; FBpp0311917; FBgn0030930

Database of genes from NCBI RefSeq genomes

More...GeneIDi		32836

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG6394

UCSC genome browser

More...UCSCi		CG6394-RB 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
AF493067 mRNA Translation: AAM62412.1
AY268068 mRNA Translation: AAQ56704.1
AE014298 Genomic DNA Translation: AAF48851.1
AE014298 Genomic DNA Translation: AAN09470.1
BT016123 mRNA Translation: AAV37008.1
AY058660 mRNA Translation: AAL13889.1 Different initiation.
AY061339 mRNA Translation: AAL28887.1 Different initiation.
RefSeqiNP_001285406.1, NM_001298477.1
NP_573301.2, NM_133073.3
NP_728178.1, NM_167623.2

3D structure databases

SMRiQ8MV48
ModBaseiSearch...

Protein-protein interaction databases

BioGridi59149, 4 interactors
IntActiQ8MV48, 4 interactors
STRINGi7227.FBpp0074396

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
GT27 Glycosyltransferase Family 27

PTM databases

SwissPalmiQ8MV48

Proteomic databases

PaxDbiQ8MV48
PRIDEiQ8MV48

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074624; FBpp0074395; FBgn0030930
FBtr0074625; FBpp0074396; FBgn0030930
FBtr0346082; FBpp0311917; FBgn0030930
GeneIDi32836
KEGGidme:Dmel_CG6394
UCSCiCG6394-RB d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		32836
FlyBaseiFBgn0030930 Pgant7

Phylogenomic databases

eggNOGiKOG3736 Eukaryota
ENOG410XPMK LUCA
InParanoidiQ8MV48
KOiK00710
OMAiNFEYRPV
OrthoDBi606683at2759
PhylomeDBiQ8MV48

Enzyme and pathway databases

UniPathwayiUPA00378
ReactomeiR-DME-913709 O-linked glycosylation of mucins

Miscellaneous databases

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

More...GenomeRNAii		32836

Protein Ontology

More...PROi		PR:Q8MV48

Gene expression databases

BgeeiFBgn0030930 Expressed in 47 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila)
ExpressionAtlasiQ8MV48 baseline and differential
GenevisibleiQ8MV48 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 nameiGALT7_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: Q8MV48
Secondary accession number(s): A4V4R2
, Q5U0W9, Q95RJ3, Q95TN2, Q9VWT6
<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: August 16, 2004
Last sequence update: August 16, 2004
Last modified: September 18, 2019
This is version 134 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again