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Protein

Xyloside xylosyltransferase 1

Gene

Xxylt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Alpha-1,3-xylosyltransferase, which elongates the O-linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of target proteins by catalyzing the addition of the second xylose. Known targets include Notch proteins and coagulation factors, such as F9.1 Publication

Caution

It is uncertain whether Met-1 or Met-14 is the initiator.Curated

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+1 PublicationNote: Has the highest in vitro activity with 20 mM Mn2+, a concentration entirely out of the physiological range. Can also utilize Mg2+, suggesting this may be the physiological cofactor.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi225ManganeseCombined sources1 Publication1
Binding sitei226UDP-alpha-D-xylose; via amide nitrogenCombined sources1 Publication1
Metal bindingi227ManganeseCombined sources1 Publication1
Binding sitei289UDP-alpha-D-xyloseCombined sources1 Publication1
Binding sitei327UDP-alpha-D-xylose; via carbonyl oxygenCombined sources1 Publication1
Binding sitei330Substrate glycopeptideCombined sources1 Publication1
Binding sitei330UDP-alpha-D-xyloseCombined sources1 Publication1
Binding sitei359Substrate glycopeptideCombined sources1 Publication1
Metal bindingi382ManganeseCombined sources1 Publication1
Binding sitei384Substrate glycopeptideCombined sources1 Publication1

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • UDP-xylosyltransferase activity Source: UniProtKB

GO - Biological processi

  • O-glycan processing Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandMagnesium, Manganese, Metal-binding

Protein family/group databases

CAZyiGT8 Glycosyltransferase Family 8

Names & Taxonomyi

Protein namesi
Recommended name:
Xyloside xylosyltransferase 1 (EC:2.4.2.n31 Publication)
Alternative name(s):
UDP-xylose:alpha-xyloside alpha-1,3-xylosyltransferase
Gene namesi
Name:Xxylt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:2146443 Xxylt1

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 19Cytoplasmic1 PublicationAdd BLAST19
Transmembranei20 – 42Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini43 – 392Lumenal1 PublicationAdd BLAST350

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi225D → N: No effect on enzyme activity. 1 Publication1
Mutagenesisi255E → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi257Q → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi262H → A: Reduces enzyme activity. 1 Publication1
Mutagenesisi265W → A: Slighly reduces enzyme activity. 1 Publication1
Mutagenesisi266Q → K: No effect on enzyme activity. 1 Publication1
Mutagenesisi289S → A: Slighly reduces enzyme activity. 1 Publication1
Mutagenesisi319D → N: No significant effect on enzyme activity. 1 Publication1
Mutagenesisi324R → S: Reduces enzyme activity. 1 Publication1
Mutagenesisi325G → S: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi326H → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi329D → A: Increases enzyme activity. 1 Publication1
Mutagenesisi330Q → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi358W → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi359W → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi384N → A: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002344281 – 392Xyloside xylosyltransferase 1Add BLAST392

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi349 ↔ 374Combined sources
Disulfide bondi356 ↔ 385Combined sources

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ3U4G3
MaxQBiQ3U4G3
PaxDbiQ3U4G3
PeptideAtlasiQ3U4G3
PRIDEiQ3U4G3

PTM databases

iPTMnetiQ3U4G3
PhosphoSitePlusiQ3U4G3

Expressioni

Gene expression databases

BgeeiENSMUSG00000047434
CleanExiMM_AI480653
GenevisibleiQ3U4G3 MM

Interactioni

Subunit structurei

Homodimer (PubMed:26414444). Dimer formation may be essential for the retention in endoplasmic reticulum (Probable).Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
F9P007403EBI-16178491,EBI-9640450From Homo sapiens.

Protein-protein interaction databases

DIPiDIP-61862N
IntActiQ3U4G3, 1 interactor

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi96 – 103Combined sources8
Helixi111 – 127Combined sources17
Beta strandi134 – 142Combined sources9
Helixi144 – 155Combined sources12
Beta strandi165 – 172Combined sources8
Helixi173 – 191Combined sources19
Beta strandi192 – 196Combined sources5
Helixi199 – 202Combined sources4
Helixi203 – 209Combined sources7
Helixi210 – 213Combined sources4
Beta strandi220 – 224Combined sources5
Beta strandi226 – 230Combined sources5
Helixi235 – 238Combined sources4
Helixi239 – 243Combined sources5
Beta strandi250 – 254Combined sources5
Helixi259 – 263Combined sources5
Helixi265 – 270Combined sources6
Turni280 – 282Combined sources3
Beta strandi287 – 295Combined sources9
Helixi296 – 301Combined sources6
Helixi303 – 308Combined sources6
Helixi311 – 321Combined sources11
Helixi329 – 339Combined sources11
Helixi341 – 343Combined sources3
Beta strandi344 – 347Combined sources4
Helixi349 – 351Combined sources3
Beta strandi352 – 354Combined sources3
Helixi358 – 362Combined sources5
Turni365 – 367Combined sources3
Helixi368 – 372Combined sources5
Beta strandi379 – 382Combined sources4
Turni384 – 386Combined sources3

3D structure databases

ProteinModelPortaliQ3U4G3
SMRiQ3U4G3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 105UDP-alpha-D-xylose bindingCombined sources1 Publication3
Regioni262 – 265Interaction with target proteins1 Publication4

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3765 Eukaryota
ENOG410XRNY LUCA
GeneTreeiENSGT00530000063165
HOGENOMiHOG000007690
HOVERGENiHBG061240
InParanoidiQ3U4G3
OMAiCKVIFHD
OrthoDBiEOG091G0GY6
TreeFamiTF323210

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR002495 Glyco_trans_8
IPR029044 Nucleotide-diphossugar_trans
PfamiView protein in Pfam
PF01501 Glyco_transf_8, 1 hit
SUPFAMiSSF53448 SSF53448, 1 hit

Sequencei

Sequence statusi: Complete.

Q3U4G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLRGGAAC ARAMARLGAL RSHYCALLLA AALAVCAFYY LGSGRETFSS
60 70 80 90 100
ATKRLKEARA GAAAPTPPAP ELARGSAAPA SGAKAKSLEG GVVVPVDYHL
110 120 130 140 150
LMMFTKAEHN APLQAKARVA LSSLLRLAKF EAHEVLNLHF VSEEASREVA
160 170 180 190 200
KALLRELLPP AAGFKCKVIF HDVAVLTDKL FPVVEAMQKY FSAGSGTYYS
210 220 230 240 250
DSIFFLSVAM HQIMPKEIPR IIQLDLDLKY KTNIRELFEE FDNFLPGAVI
260 270 280 290 300
GIAREMQPVY RHTFWQFRHE NPKTRVGDPP PEGLPGFNSG VMLLNLEAMR
310 320 330 340 350
QSPLYSHLLE PSWVQQLADK YHFRGHLGDQ DFFTMIGMEH PELFHVLDCT
360 370 380 390
WNRQLCTWWR DHGYSDVFQA YFRCEGHVKI YHGNCNTPIP ED
Length:392
Mass (Da):43,839
Last modified:July 27, 2011 - v2
Checksum:i0916EB1D7E27F08E
GO

Sequence cautioni

The sequence AAH31419 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46 – 47ET → LP in AAH31419 (PubMed:15489334).Curated2
Sequence conflicti80 – 81AS → GF in BAE32468 (PubMed:16141072).Curated2
Sequence conflicti80 – 81AS → GF in AAH31419 (PubMed:15489334).Curated2
Sequence conflicti100L → Q in BAE38667 (PubMed:16141072).Curated1
Sequence conflicti110N → D in BAE38667 (PubMed:16141072).Curated1
Sequence conflicti312S → A in BAE38667 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154256 mRNA Translation: BAE32468.1
AK166259 mRNA Translation: BAE38667.1
AC090430 Genomic DNA No translation available.
AC126280 Genomic DNA No translation available.
BC031419 mRNA Translation: AAH31419.1 Different initiation.
CCDSiCCDS49822.1
RefSeqiNP_941028.2, NM_198626.2
UniGeneiMm.286693

Genome annotation databases

EnsembliENSMUST00000055389; ENSMUSP00000050246; ENSMUSG00000047434
GeneIDi268880
KEGGimmu:268880
UCSCiuc007yxa.2 mouse

Similar proteinsi

Entry informationi

Entry nameiXXLT1_MOUSE
AccessioniPrimary (citable) accession number: Q3U4G3
Secondary accession number(s): E9QL73, Q3TLX5, Q8K2I0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: July 27, 2011
Last modified: October 25, 2017
This is version 87 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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