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Entry version 132 (16 Oct 2019)
Sequence version 2 (16 Aug 2004)
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Protein

Polypeptide N-acetylgalactosaminyltransferase 35A

Gene

Pgant35A

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

Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:11925450, PubMed:12829714). Displays the same enzyme activity toward MUC1, MUC4, and EA2 (PubMed:11925450, PubMed:12829714). Not involved in glycosylation of erythropoietin (EPO) (PubMed:11925450). 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 (PubMed:11925450, PubMed:12829714). Protein modification by this enzyme might be important for cytokinesis and tube formation during embryogenesis (PubMed:16251381, PubMed:20807760). Together with Pgant3, regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles (PubMed:25253852).5 Publications

Miscellaneous

The human ortholog GALNT11 (AC Q8NCW6) is not able to rescue lethality caused by the SF32 mutation.1 Publication

<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 ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=8.5 µM for UDP-GalNAc1 Publication
  2. KM=0.35 mM for EA2 acceptor peptide1 Publication

    <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.3 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 sitei188SubstrateBy similarity1
    Binding sitei220SubstrateBy 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 bindingi243ManganeseBy similarity1
    Binding sitei244SubstrateBy similarity1
    Metal bindingi245ManganeseBy similarity1
    Binding sitei348SubstrateBy similarity1
    Metal bindingi376ManganeseBy similarity1
    Binding sitei379SubstrateBy similarity1
    Binding sitei384SubstrateBy 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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular 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-913709 O-linked glycosylation of mucins

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q8MVS5

    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:
    Polypeptide N-acetylgalactosaminyltransferase 35A (EC:2.4.1.413 Publications)
    Alternative name(s):
    Protein l(2)35Aa
    Protein-UDP acetylgalactosaminyltransferase 35A
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A
    Short name:
    pp-GaNTase 35A
    dGalNAc-T1
    <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:Pgant35AImported
    ORF Names:CG7480Imported
    <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 2L

    Organism-specific databases

    Drosophila genome database

    More...
    FlyBasei
    FBgn0001970 Pgant35A

    <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 – 6CytoplasmicSequence analysis6
    <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>Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
    Topological domaini30 – 632LumenalSequence analysisAdd BLAST603

    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 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 Pgant3, restores normal synaptic strength (PubMed:25253852). RNAi-mediated knockdown is lethal (PubMed:22157008). RNAi-mediated knockdown in the mesoderm, respiratory system, digestive system or reproductive tract results in a reduction in viability (PubMed:22157008).2 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>Mutagenesisi227R → W in SF32; induces lethality. 2 Publications1
    Mutagenesisi243D → N: Abolishes glycosyltransferase activity. Not able to rescue lethality caused by SF32 mutation. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000591681 – 632Polypeptide N-acetylgalactosaminyltransferase 35AAdd BLAST632

    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>Glycosylationi69N-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 bondi136 ↔ 371PROSITE-ProRule annotation
    Glycosylationi264N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi362 ↔ 439PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 516PROSITE-ProRule annotation
    Disulfide bondi539 ↔ 553PROSITE-ProRule annotation
    Disulfide bondi580 ↔ 597PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

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

    More...
    PaxDbi
    Q8MVS5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8MVS5

    <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 at high level in ovaries. Expressed at low level in testis. Expressed at higher level in adult females than males. During oogenesis, it is detected in germ cells and follicle epithelia of all developmental stages. Initially expressed during early stages of oogenesis in region I and reaches high levels in regions IIa and IIb of the germarium. Highly expressed in stage 2 egg chambers. Remains highly expressed during later stages of oogenesis. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. Expressed in 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 dorsal longitudinal trachea and posterior spiracles. In third instar larvae, ubiquitously expressed in wing, 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.4 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    FBgn0001970 Expressed in 20 organ(s), highest expression level in head

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q8MVS5 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q8MVS5 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

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    7227.FBpp0080202

    <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>Domaini526 – 632Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST107

    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>Regioni147 – 259Catalytic subdomain AAdd BLAST113
    Regioni317 – 379Catalytic 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

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3736 Eukaryota
    ENOG410XPMK LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000165841

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8MVS5

    KEGG Orthology (KO)

    More...
    KOi
    K00710

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FCYGCLV

    Database of Orthologous Groups

    More...
    OrthoDBi
    606683at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q8MVS5

    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>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.

    Q8MVS5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA
    60 70 80 90 100
    TPRAELSYQA RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ
    110 120 130 140 150
    DKYIRDIGYK HHAFNALVSN NIGLFRAIPD TRHKVCDRQE TTEAENLPQA
    160 170 180 190 200
    SIVMCFYNEH KMTLMRSIKT VLERTPSYLL REIILVDDHS DLPELEFHLH
    210 220 230 240 250
    GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV FLDSHIEVNQ
    260 270 280 290 300
    QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW
    310 320 330 340 350
    ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG
    360 370 380 390 400
    ENIEISFRAW QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL
    410 420 430 440 450
    AHVWMDQYKD YYLKHEKVPK TYDYGDISDR LKLRERLQCR DFAWYLKNVY
    460 470 480 490 500
    PELHVPGEES KKSAAAPIFQ PWHSRKRNYV DTFQLRLTGT ELCAAVVAPK
    510 520 530 540 550
    VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL EASGDAQVTV
    560 570 580 590 600
    NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS
    610 620 630
    NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL
    Length:632
    Mass (Da):71,828
    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:iE726B9F32481E4E9
    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 AAK66862 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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 conflicti72I → T in AAM62405 (PubMed:11925446).Curated1
    Sequence conflicti628S → T in AAL49213 (PubMed:12537569).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
    AF478697 mRNA Translation: AAM62405.1
    AF478698 Genomic DNA Translation: AAM62406.1
    AF478699 Genomic DNA Translation: AAM62407.1
    AF478700 Genomic DNA Translation: AAM62408.1
    AF158747 mRNA Translation: AAK66862.1 Different initiation.
    AE014134 Genomic DNA Translation: AAF53391.1
    AY071591 mRNA Translation: AAL49213.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_652069.2, NM_143812.4

    Genome annotation databases

    Ensembl metazoan genome annotation project

    More...
    EnsemblMetazoai
    FBtr0080629; FBpp0080202; FBgn0001970

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    48775

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    dme:Dmel_CG7480

    <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
    AF478697 mRNA Translation: AAM62405.1
    AF478698 Genomic DNA Translation: AAM62406.1
    AF478699 Genomic DNA Translation: AAM62407.1
    AF478700 Genomic DNA Translation: AAM62408.1
    AF158747 mRNA Translation: AAK66862.1 Different initiation.
    AE014134 Genomic DNA Translation: AAF53391.1
    AY071591 mRNA Translation: AAL49213.1
    RefSeqiNP_652069.2, NM_143812.4

    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

    STRINGi7227.FBpp0080202

    Protein family/group databases

    CAZyiCBM13 Carbohydrate-Binding Module Family 13
    GT27 Glycosyltransferase Family 27

    Proteomic databases

    PaxDbiQ8MVS5
    PRIDEiQ8MVS5

    Genome annotation databases

    EnsemblMetazoaiFBtr0080629; FBpp0080202; FBgn0001970
    GeneIDi48775
    KEGGidme:Dmel_CG7480

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    48775
    FlyBaseiFBgn0001970 Pgant35A

    Phylogenomic databases

    eggNOGiKOG3736 Eukaryota
    ENOG410XPMK LUCA
    GeneTreeiENSGT00940000165841
    InParanoidiQ8MVS5
    KOiK00710
    OMAiFCYGCLV
    OrthoDBi606683at2759
    PhylomeDBiQ8MVS5

    Enzyme and pathway databases

    UniPathwayiUPA00378
    BRENDAi2.4.1.41 1994
    ReactomeiR-DME-913709 O-linked glycosylation of mucins
    SABIO-RKiQ8MVS5

    Miscellaneous databases

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

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    GenomeRNAii
    48775

    Protein Ontology

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    PROi
    PR:Q8MVS5

    Gene expression databases

    BgeeiFBgn0001970 Expressed in 20 organ(s), highest expression level in head
    ExpressionAtlasiQ8MVS5 baseline and differential
    GenevisibleiQ8MVS5 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 nameiGLT35_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: Q8MVS5
    Secondary accession number(s): Q8MVS2
    , Q8MVS3, Q8MVS4, Q8SYF1, Q965E4, Q9V3C9
    <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: October 16, 2019
    This is version 132 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
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