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Q5NDL9

- EOGT_CANFA

UniProt

Q5NDL9 - EOGT_CANFA

Protein

EGF domain-specific O-linked N-acetylglucosamine transferase

Gene

EOGT

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      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
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 527510EGF domain-specific O-linked N-acetylglucosamine transferasePRO_0000301971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000009819.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi295 – 2973Required for optimal activityBy similarity
    Motifi524 – 5274Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyltransferase 61 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG320328.
    HOGENOMiHOG000033829.
    HOVERGENiHBG056678.
    InParanoidiQ5NDL9.
    KOiK18134.
    OrthoDBiEOG7D2FDQ.

    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.

    Q5NDL9-1 [UniParc]FASTAAdd to Basket

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    MLKLLVLGVL LHDVSLSGQD EAPPKADGIP GEPLFNYASI RLPEEHIPFF    50
    LHNNRHIATV CKKDSHCPYK KHLENLKYCW GYEKSCKPEF RFGYPVCTYI 100
    DMGWTDTLES AQDIFWKQAD FGYAGERLEE LHVLCQPEEP HDSSLLCSRY 150
    LQYCRAANLY LDLRNIKRNH DRFKEDFFQS GEIGGHCTLD TQTLLSEGQR 200
    KSPLQSWFAE LQSYTELNFR PIEDAKCDVV IEKPTYFMKL DAGVNMYHHF 250
    CDFVNLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW KAFTDYDVIH 300
    LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFSQHVL 350
    HRLNITQEGP KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTLEVQIV 400
    DYKYKELGFL DQLRITHNTD IFIGMHGAGL THLLFLPDWA AVFELYNCED 450
    ERCYLDLARL RGVHYITWRR QNKVFPQDKG HHPTLGEHPK FTNYSFDVEE 500
    FMYLVLQAAD HVLQHPKWPF KKKRDEL 527
    Length:527
    Mass (Da):61,670
    Last modified:February 1, 2005 - v1
    Checksum:iDA5DE507862BB6AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ868227 mRNA. Translation: CAI30562.1.
    RefSeqiNP_001009187.1. NM_001009187.1.
    XP_005632096.1. XM_005632039.1.
    XP_005632097.1. XM_005632040.1.
    XP_005632098.1. XM_005632041.1.
    UniGeneiCfa.16220.

    Genome annotation databases

    GeneIDi494221.
    KEGGicfa:494221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ868227 mRNA. Translation: CAI30562.1 .
    RefSeqi NP_001009187.1. NM_001009187.1.
    XP_005632096.1. XM_005632039.1.
    XP_005632097.1. XM_005632040.1.
    XP_005632098.1. XM_005632041.1.
    UniGenei Cfa.16220.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000009819.

    Protein family/group databases

    CAZyi GT61. Glycosyltransferase Family 61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 494221.
    KEGGi cfa:494221.

    Organism-specific databases

    CTDi 285203.

    Phylogenomic databases

    eggNOGi NOG320328.
    HOGENOMi HOG000033829.
    HOVERGENi HBG056678.
    InParanoidi Q5NDL9.
    KOi K18134.
    OrthoDBi EOG7D2FDQ.

    Miscellaneous databases

    NextBioi 20865674.

    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. "Phylogeny of xylosyltransferases."
      Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V., Mollicone R., Oriol R.
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiEOGT_CANFA
    AccessioniPrimary (citable) accession number: Q5NDL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3