GXLT1_DANRE
ID GXLT1_DANRE Reviewed; 405 AA.
AC Q5SP46;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glucoside xylosyltransferase 1;
DE EC=2.4.2.42 {ECO:0000250|UniProtKB:Q4G148};
DE AltName: Full=Glycosyltransferase 8 domain-containing protein 3;
GN Name=gxylt1; Synonyms=glt8d3; ORFNames=si:ch211-155a11.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Glycosyltransferase which elongates the O-linked glucose
CC attached to EGF-like repeats in the extracellular domain of Notch
CC proteins by catalyzing the addition of xylose.
CC {ECO:0000250|UniProtKB:Q4G148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + UDP-
CC alpha-D-xylose = 3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-
CC seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:56064,
CC Rhea:RHEA-COMP:14610, Rhea:RHEA-COMP:14611, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:140575,
CC ChEBI:CHEBI:140576; EC=2.4.2.42;
CC Evidence={ECO:0000250|UniProtKB:Q4G148};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AL929504; CAI11646.1; -; Genomic_DNA.
DR RefSeq; NP_001025270.1; NM_001030099.1.
DR AlphaFoldDB; Q5SP46; -.
DR STRING; 7955.ENSDARP00000030796; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q5SP46; -.
DR Ensembl; ENSDART00000032805; ENSDARP00000030796; ENSDARG00000022550.
DR GeneID; 556315; -.
DR KEGG; dre:556315; -.
DR CTD; 556315; -.
DR ZFIN; ZDB-GENE-041210-116; gxylt1b.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000156242; -.
DR HOGENOM; CLU_040965_0_0_1; -.
DR InParanoid; Q5SP46; -.
DR OMA; NMTRMRS; -.
DR OrthoDB; 978446at2759; -.
DR PhylomeDB; Q5SP46; -.
DR TreeFam; TF323210; -.
DR PRO; PR:Q5SP46; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000022550; Expressed in camera-type eye and 15 other tissues.
DR ExpressionAtlas; Q5SP46; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140563; F:UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..405
FT /note="Glucoside xylosyltransferase 1"
FT /id="PRO_0000288538"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..405
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 46741 MW; 465414BAC482621B CRC64;
MRIYLRTFGL CIVVALLSLV FLFSKHDEGS FSAGFKQVRA PLQQKSFNGA KAKQRPTATT
SHRDVVQNPN SPVQEEVLMH LAAVACGERH GEVVNMLKTA VTLSQRALRF HIFAEQQLQT
SIKADLDSWP AFIQGKFSYV LHPISFPHEH HEEWSQLFKP CASQRLFLPM ILRELDSLLY
VDTDVLFLQP VELIWDMLML FNSTQLIAMA PEHEEPRIAW YSRFSWHPYY GKMGINSGVM
LMNLTRMRIT QFKNDMTPVG LHWDELLMPL LQKYKLNITW GDQDLINIIF HYNPEMVYTL
PCHWNYRPDH CIYGSNCAPA EDEGVFVLHG NRGVFHSDKQ PAFRAVYEAF EQYTFGEDLR
QSLLSRLEVA LNETTHTYCG KASHFFTTGL QKSVRRLQRA TPPGD
