ID   GXLT2_XENLA             Reviewed;         423 AA.
AC   Q6DE37;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Glucoside xylosyltransferase 2;
DE            EC=2.4.2.42 {ECO:0000250|UniProtKB:Q4G148};
DE   AltName: Full=Glycosyltransferase 8 domain-containing protein 4;
GN   Name=gxylt2; Synonyms=glt8d4;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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:A0PJZ3}.
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; BC077307; AAH77307.1; -; mRNA.
DR   RefSeq; NP_001086684.1; NM_001093215.1.
DR   AlphaFoldDB; Q6DE37; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   GeneID; 446519; -.
DR   KEGG; xla:446519; -.
DR   CTD; 446519; -.
DR   Xenbase; XB-GENE-5889631; gxylt2.S.
DR   OrthoDB; 978446at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 446519; Expressed in neurula embryo and 19 other tissues.
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..423
FT                   /note="Glucoside xylosyltransferase 2"
FT                   /id="PRO_0000288541"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..423
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          60..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  49593 MW;  29012C08EBDD4FA4 CRC64;
     MRFRWKFFGS LLCVTGLLLV LYRQLGNVPQ PPPGPASAQG SPSLTATSGY FRALEDHVPR
     RDARQGGKKK TNWNNVRAPE QKPNPPMPEE WMHLAVVACG DRLEETVTML KSAVLFSFKK
     IKFHIFAEDS LKSDFQMKLE IWPQQISRKI EYKIYPITFP GGNTQEWKKL FKPCAAQRLF
     LPMLLQDVDS LLYVDTDVLF LRPLDHVWAF LRRFNDTQLA AMAPEHEISK IGWYSRFARH
     PFYGTTGVNS GVMLMNLTRI RNQHFKNNMI PAGLTWEEML HPLYQKYKNY ITWGDQDLLN
     IIFYFNPEML YVFPCHWNYR PDHCMYGSNC KAAEEEGVSI LHGNRGVYHD EKQPAFKAFY
     EVIRDYTFDD NLFQSMYFPL QSKFLESVHT LCGRIPQVFL KQIEKTMKMM YERRVVVHIR
     SDV