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Q6GQ23

- EOGT_XENLA

UniProt

Q6GQ23 - EOGT_XENLA

Protein

EGF domain-specific O-linked N-acetylglucosamine transferase

Gene

eogt

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains By similarity.By similarity

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine.
    UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.

    GO - Molecular functioni

    1. protein N-acetylglucosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. protein O-linked glycosylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Protein family/group databases

    CAZyiGT61. Glycosyltransferase Family 61.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EGF domain-specific O-linked N-acetylglucosamine transferase (EC:2.4.1.255)
    Alternative name(s):
    Extracellular O-linked N-acetylglucosamine transferase
    Gene namesi
    Name:eogt
    Synonyms:aer61
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-994622. eogt.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 525501EGF domain-specific O-linked N-acetylglucosamine transferasePRO_0000301976Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi293 – 2953Required for optimal activityBy similarity
    Motifi522 – 5254Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyltransferase 61 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG056678.
    KOiK18134.

    Family and domain databases

    InterProiIPR007657. Glycosyltransferase_AER61.
    [Graphical view]
    PfamiPF04577. DUF563. 1 hit.
    [Graphical view]
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6GQ23-1 [UniParc]FASTAAdd to Basket

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    MVPLRLVLLL HIIHFSCENE VGSAANNGSA QLYNYRKIHL PDDHIPYYLH    50
    SNRHVAALCL QDLHCPYKQH LQNLNSCWGY EKTCAEGHRF GYPVCDQVDF 100
    GWAKTIEESQ QVFWRQADFG YVKERLAETQ ILCRPQEQGD SMLACSQNLQ 150
    HCRATNLYLD LRHPRRGQEN FKEDFLQEGE IGGHCDLDKQ ALLSQGAWKS 200
    PLQSWFAELQ SYSSFKFKPI EDAHCDIIIE KPTYFMKLDA GVNMYHHFCD 250
    FVNLYITQHV NNSFSTDINI VMWTTSVYGY GDLFSDTWKA FTDYEITHLK 300
    AYDNKRVCFK DAVFALLPRM RYGLFYNTPL ISHCHGSGLF RAFSQHVLHR 350
    LNITQHPATE AKIRVTILVR STEFRKILNL DELVQALEAV PTFQVKVVDY 400
    KYRVLGFLEQ LSITHNSDIF IGMHGAGLTH LLFLPDWAVV FELYNCEDAR 450
    CYLDLARLRG IQYMTWEKGD KVFPQDKGHH PNLGEHPKFT NYAFDVEEFL 500
    RLVQQGATYV SRHSKWPLRR TRDEL 525
    Length:525
    Mass (Da):61,182
    Last modified:July 19, 2004 - v1
    Checksum:i71165EA2755AA496
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072925 mRNA. Translation: AAH72925.1.
    RefSeqiNP_001085557.1. NM_001092088.1.
    UniGeneiXl.7160.

    Genome annotation databases

    GeneIDi443983.
    KEGGixla:443983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC072925 mRNA. Translation: AAH72925.1 .
    RefSeqi NP_001085557.1. NM_001092088.1.
    UniGenei Xl.7160.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT61. Glycosyltransferase Family 61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 443983.
    KEGGi xla:443983.

    Organism-specific databases

    CTDi 285203.
    Xenbasei XB-GENE-994622. eogt.

    Phylogenomic databases

    HOVERGENi HBG056678.
    KOi K18134.

    Family and domain databases

    InterProi IPR007657. Glycosyltransferase_AER61.
    [Graphical view ]
    Pfami PF04577. DUF563. 1 hit.
    [Graphical view ]
    PROSITEi PS00014. ER_TARGET. 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: Gastrula.

    Entry informationi

    Entry nameiEOGT_XENLA
    AccessioniPrimary (citable) accession number: Q6GQ23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 44 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3