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Q6DJR8

- GLT11_XENTR

UniProt

Q6DJR8 - GLT11_XENTR

Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

galnt11

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 2 (22 Jan 2014)
      Previous versions | rss
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    Functioni

    Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.1 Publication

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

    Cofactori

    Manganese.By similarity
    Calcium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. Notch binding Source: UniProtKB
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. determination of left/right symmetry Source: UniProtKB
    3. Notch receptor processing Source: UniProtKB
    4. Notch signaling involved in heart development Source: UniProtKB
    5. protein O-linked glycosylation via threonine Source: UniProtKB
    6. regulation of Notch signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Notch signaling pathway

    Keywords - Ligandi

    Calcium, Lectin, Manganese

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 11 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 11
    Short name:
    GalNAc-T11
    Short name:
    pp-GaNTase 11
    Protein-UDP acetylgalactosaminyltransferase 11
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
    Gene namesi
    Name:galnt11
    OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
    Taxonomic identifieri8364 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
    ProteomesiUP000008143: Unplaced

    Organism-specific databases

    XenbaseiXB-GENE-981830. galnt11.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Aberrant left-right patterning resulting in abnormal cardiac loops, including leftward and symmetric/midline loops.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601Polypeptide N-acetylgalactosaminyltransferase 11PRO_0000425208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi486 ↔ 505PROSITE-ProRule annotation
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi529 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi571 ↔ 589PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Interacts with notch1.1 Publication

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Topological domaini29 – 601573LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini469 – 600132Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni143 – 254112Catalytic subdomain ABy similarityAdd
    BLAST
    Regioni312 – 37463Catalytic subdomain BBy similarityAdd
    BLAST

    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

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG051699.
    KOiK00710.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6DJR8-1 [UniParc]FASTAAdd to Basket

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    MGSAALRCFC YGCLFTSVTW TLLLFIYFNF SEESQGFRHV PVKGLEPYKP    50
    LPKKIYPRFS RDSMGQHSDP RKGHNGNQLE TEANADLSPE LGMIFNEQDQ 100
    DVRDVGYQKH AFNLLISNRL GYHRDVPDTR DSKCAKKTYP PDLPMASIVI 150
    CFYNEAFSAL LRTVHSVLDR TPAQLLHEII LVDDNSELDD LKKDLDGYMQ 200
    ENLSKKVKLV RNKQREGLIR GRMVGASHAT GDVLVFLDSH CEVNEMWLQP 250
    LLAPIKENPR TVVCPVIDII SADTLIYSSS PVVRGGFNWG LHFKWDPVPL 300
    AELGGPEGFS APFRSPTMAG GLFAMDREYF NMLGQYDSGM DIWGGENLEI 350
    SFRIWMCGGS LLIVPCSRVG HIFRKRRPYG SPGGHDTMAH NSLRLAHVWM 400
    DEYKDQYFAL RPELRNRDFG DIRERLALRR RLNCKSFKWY LDNIYPEMQV 450
    SGPNAKPQPP VFMNKGQKRP KILQRGRLIN MQTNRCLVAQ GHPSQKGGLV 500
    VAKECDYNDS EQVWSYNEEH ELILSNLLCL DMSETRSSDP PRLMKCHGSG 550
    GSQQWVFGKS NRLYQVSVGQ CLKLVDPMSR KGYVSMAICD GSPSQQWHLE 600
    N 601
    Length:601
    Mass (Da):68,383
    Last modified:January 22, 2014 - v2
    Checksum:i1FA0294A3CEEA236
    GO

    Sequence cautioni

    The sequence AAH75106.1 differs from that shown. Reason: Frameshift at position 39.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC075106 mRNA. Translation: AAH75106.1. Frameshift.
    RefSeqiNP_001006904.1. NM_001006903.1.
    UniGeneiStr.1760.

    Genome annotation databases

    GeneIDi448751.
    KEGGixtr:448751.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC075106 mRNA. Translation: AAH75106.1 . Frameshift.
    RefSeqi NP_001006904.1. NM_001006903.1.
    UniGenei Str.1760.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 448751.
    KEGGi xtr:448751.

    Organism-specific databases

    CTDi 63917.
    Xenbasei XB-GENE-981830. galnt11.

    Phylogenomic databases

    HOVERGENi HBG051699.
    KOi K00710.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    2. "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
      Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
      Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH NOTCH1.

    Entry informationi

    Entry nameiGLT11_XENTR
    AccessioniPrimary (citable) accession number: Q6DJR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 22, 2014
    Last sequence update: January 22, 2014
    Last modified: October 1, 2014
    This is version 67 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3