ID   GXLT1_CHICK             Reviewed;         433 AA.
AC   Q5ZKI6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=RCJMB04_10i5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720098; CAG31757.1; -; mRNA.
DR   RefSeq; NP_001025907.1; NM_001030736.1.
DR   AlphaFoldDB; Q5ZKI6; -.
DR   STRING; 9031.ENSGALP00000015499; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q5ZKI6; -.
DR   GeneID; 417789; -.
DR   KEGG; gga:417789; -.
DR   CTD; 283464; -.
DR   VEuPathDB; HostDB:geneid_417789; -.
DR   eggNOG; KOG3765; Eukaryota.
DR   InParanoid; Q5ZKI6; -.
DR   OrthoDB; 978446at2759; -.
DR   PhylomeDB; Q5ZKI6; -.
DR   PRO; PR:Q5ZKI6; -.
DR   Proteomes; UP000000539; Unplaced.
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   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..433
FT                   /note="Glucoside xylosyltransferase 1"
FT                   /id="PRO_0000288537"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..433
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  49982 MW;  842D58B300B3C6D0 CRC64;
     MRRFARVALL FLGCGVCSLL YGVSQLALSL EQEAGGARQR QARESAAPGG GRQAGSADGG
     EEGAGRCKNL SVSFWNSYWM LPSDVCGVNC FWEAAFRYTY METQPSETMH LAVVACGERL
     EETITMLRSA IIFSIKPLHF HIFAEDQLHE SFKDILDDFP YEGKVNYTLY PITFPSEGAK
     EWKKLFKPCA SQRLFLPLIL KDVDSLLYVD TDILFLRPVD DIWSFLRKFD STQIAAMAPE
     HEEPRIGWYN RFARHPYYGV TGINSGVMLM NMTRIRRKYF KNDMTSVRLR WAEILMPLLK
     KYKLNITWGD QDLLNIMFFH NPESLYVFPC QWNYRPDHCI YGSNCKEAEE EGIFILHGNR
     GVYHDDKQPT FRAVYEAIKN YSFGDDLVRS LLQPLELELQ KTVHTYCGRV YEVFIKQLKK
     SIKDLSVRRS KGS