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Protein

Glucoside xylosyltransferase 1

Gene

Gxylt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoside xylosyltransferase 1 (EC:2.4.2.n2)
Alternative name(s):
Glycosyltransferase 8 domain-containing protein 3
S33-D
Gene namesi
Name:Gxylt1
Synonyms:Glt8d3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1563062. Gxylt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 435406LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glucoside xylosyltransferase 1PRO_0000288536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ6GX83.
PRIDEiQ6GX83.

Expressioni

Inductioni

By E2F1.1 Publication

Gene expression databases

ExpressionAtlasiQ6GX83. baseline and differential.
GenevisibleiQ6GX83. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055150.

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.
InParanoidiQ6GX83.
KOiK13676.
OMAiSLCYWNP.
OrthoDBiEOG7W6WMC.
PhylomeDBiQ6GX83.
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.

Q6GX83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRYLRVVGL CLACGFCSLL YAFSQLAVSL EEGAAVGRRP QAAVASWLAD
60 70 80 90 100
GGRGTGRGAG SAGPGRTGRC KEVSLSYWNP YWMLPSDVCG VNCFWEAAFR
110 120 130 140 150
YGLKTRPTEK MHLAVVACGD RLEETVTMLK SALIFSIKPL HVHIFAEDQL
160 170 180 190 200
HDSFKDRLDS WSFLQRFNYS LYPITFPSDS AMEWKKLFKP CASQRLFLPL
210 220 230 240 250
ILKGVDSLLY VDTDVLFLRP VDDIWSLLER FNSTQIAAMA PEHEEPRVGW
260 270 280 290 300
YNRFARHPYY GRTGVNSGVM LMNMTRMRRK YFKNDMTTAR LQWGDILMPL
310 320 330 340 350
LKKYKLNITW GDQDLLNIMF YHNPESLFVF PCQWNYRPDH CIYGSNCREA
360 370 380 390 400
EEEGVFILHG NRGVYHDDKQ PAFRAMYEAL RNCSLEDDSV RSLLKPLELE
410 420 430
LQKTVHTYCG KTYKIFIKQL AKSIRNRYDT PPKER
Length:435
Mass (Da):50,243
Last modified:May 29, 2007 - v2
Checksum:i75A51D4A21074747
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03055509 Genomic DNA. No translation available.
AABR03055661 Genomic DNA. No translation available.
AY623036 mRNA. Translation: AAT46050.1.
RefSeqiNP_001094357.1. NM_001100887.1.
UniGeneiRn.14826.

Genome annotation databases

EnsembliENSRNOT00000058349; ENSRNOP00000055150; ENSRNOG00000005234.
GeneIDi300173.
KEGGirno:300173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03055509 Genomic DNA. No translation available.
AABR03055661 Genomic DNA. No translation available.
AY623036 mRNA. Translation: AAT46050.1.
RefSeqiNP_001094357.1. NM_001100887.1.
UniGeneiRn.14826.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055150.

Proteomic databases

PaxDbiQ6GX83.
PRIDEiQ6GX83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000058349; ENSRNOP00000055150; ENSRNOG00000005234.
GeneIDi300173.
KEGGirno:300173.

Organism-specific databases

CTDi283464.
RGDi1563062. Gxylt1.

Phylogenomic databases

eggNOGiKOG3765. Eukaryota.
ENOG410XRNY. LUCA.
GeneTreeiENSGT00510000046589.
HOGENOMiHOG000264229.
HOVERGENiHBG059879.
InParanoidiQ6GX83.
KOiK13676.
OMAiSLCYWNP.
OrthoDBiEOG7W6WMC.
PhylomeDBiQ6GX83.
TreeFamiTF323210.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi646470.
PROiQ6GX83.

Gene expression databases

ExpressionAtlasiQ6GX83. baseline and differential.
GenevisibleiQ6GX83. RN.

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

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Identification of novel E2F1 target genes regulated in cell cycle-dependent and independent manners."
    Iwanaga R., Komori H., Ishida S., Okamura N., Nakayama K., Nakayama K., Ohtani K.
    Oncogene 25:1786-1798(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-435, INDUCTION.

Entry informationi

Entry nameiGXLT1_RAT
AccessioniPrimary (citable) accession number: Q6GX83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: May 11, 2016
This is version 73 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. 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.