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Protein

Glucoside xylosyltransferase 1

Gene

gxylt1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.By similarity

Catalytic activityi

UDP-alpha-D-xylose + beta-D-glucosyl-R = UDP + alpha-D-xylose-(1->3)-beta-D-glucosyl-R.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-DRE-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoside xylosyltransferase 1 (EC:2.4.2.n2)
Alternative name(s):
Glycosyltransferase 8 domain-containing protein 3
Gene namesi
Name:gxylt1
Synonyms:glt8d3
ORF Names:si:ch211-155a11.6
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 4

Organism-specific databases

ZFINiZDB-GENE-041210-116. gxylt1b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22CytoplasmicSequence analysis
Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini24 – 405382LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405Glucoside xylosyltransferase 1PRO_0000288538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ5SP46.

Expressioni

Gene expression databases

BgeeiQ5SP46.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000030796.

Structurei

3D structure databases

ProteinModelPortaliQ5SP46.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00510000046589.
HOGENOMiHOG000264229.
HOVERGENiHBG059879.
InParanoidiQ5SP46.
KOiK13676.
OMAiHEHHEEW.
OrthoDBiEOG7W6WMC.
PhylomeDBiQ5SP46.
TreeFamiTF323210.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SP46-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIYLRTFGL CIVVALLSLV FLFSKHDEGS FSAGFKQVRA PLQQKSFNGA
60 70 80 90 100
KAKQRPTATT SHRDVVQNPN SPVQEEVLMH LAAVACGERH GEVVNMLKTA
110 120 130 140 150
VTLSQRALRF HIFAEQQLQT SIKADLDSWP AFIQGKFSYV LHPISFPHEH
160 170 180 190 200
HEEWSQLFKP CASQRLFLPM ILRELDSLLY VDTDVLFLQP VELIWDMLML
210 220 230 240 250
FNSTQLIAMA PEHEEPRIAW YSRFSWHPYY GKMGINSGVM LMNLTRMRIT
260 270 280 290 300
QFKNDMTPVG LHWDELLMPL LQKYKLNITW GDQDLINIIF HYNPEMVYTL
310 320 330 340 350
PCHWNYRPDH CIYGSNCAPA EDEGVFVLHG NRGVFHSDKQ PAFRAVYEAF
360 370 380 390 400
EQYTFGEDLR QSLLSRLEVA LNETTHTYCG KASHFFTTGL QKSVRRLQRA

TPPGD
Length:405
Mass (Da):46,741
Last modified:December 21, 2004 - v1
Checksum:i465414BAC482621B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL929504 Genomic DNA. Translation: CAI11646.1.
RefSeqiNP_001025270.1. NM_001030099.1.
UniGeneiDr.85405.

Genome annotation databases

EnsembliENSDART00000032805; ENSDARP00000030796; ENSDARG00000022550.
GeneIDi556315.
KEGGidre:556315.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL929504 Genomic DNA. Translation: CAI11646.1.
RefSeqiNP_001025270.1. NM_001030099.1.
UniGeneiDr.85405.

3D structure databases

ProteinModelPortaliQ5SP46.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000030796.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Proteomic databases

PaxDbiQ5SP46.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000032805; ENSDARP00000030796; ENSDARG00000022550.
GeneIDi556315.
KEGGidre:556315.

Organism-specific databases

CTDi556315.
ZFINiZDB-GENE-041210-116. gxylt1b.

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00510000046589.
HOGENOMiHOG000264229.
HOVERGENiHBG059879.
InParanoidiQ5SP46.
KOiK13676.
OMAiHEHHEEW.
OrthoDBiEOG7W6WMC.
PhylomeDBiQ5SP46.
TreeFamiTF323210.

Enzyme and pathway databases

ReactomeiR-DRE-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.

Miscellaneous databases

PROiQ5SP46.

Gene expression databases

BgeeiQ5SP46.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.

Entry informationi

Entry nameiGXLT1_DANRE
AccessioniPrimary (citable) accession number: Q5SP46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 65 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.