GXLT2_MOUSE
ID GXLT2_MOUSE Reviewed; 444 AA.
AC Q810K9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC049816; AAH49816.1; -; mRNA.
DR CCDS; CCDS20390.1; -.
DR RefSeq; NP_941014.1; NM_198612.2.
DR AlphaFoldDB; Q810K9; -.
DR STRING; 10090.ENSMUSP00000032157; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; Q810K9; 1 site.
DR iPTMnet; Q810K9; -.
DR PhosphoSitePlus; Q810K9; -.
DR MaxQB; Q810K9; -.
DR PaxDb; Q810K9; -.
DR PeptideAtlas; Q810K9; -.
DR PRIDE; Q810K9; -.
DR ProteomicsDB; 270906; -.
DR Antibodypedia; 66937; 65 antibodies from 16 providers.
DR DNASU; 232313; -.
DR Ensembl; ENSMUST00000032157; ENSMUSP00000032157; ENSMUSG00000030074.
DR GeneID; 232313; -.
DR KEGG; mmu:232313; -.
DR UCSC; uc009dca.1; mouse.
DR CTD; 727936; -.
DR MGI; MGI:2682940; Gxylt2.
DR VEuPathDB; HostDB:ENSMUSG00000030074; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000158065; -.
DR HOGENOM; CLU_040965_0_0_1; -.
DR InParanoid; Q810K9; -.
DR OMA; RFHIFTE; -.
DR OrthoDB; 978446at2759; -.
DR PhylomeDB; Q810K9; -.
DR TreeFam; TF323210; -.
DR BioGRID-ORCS; 232313; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gxylt2; mouse.
DR PRO; PR:Q810K9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q810K9; protein.
DR Bgee; ENSMUSG00000030074; Expressed in vault of skull and 148 other tissues.
DR Genevisible; Q810K9; MM.
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..444
FT /note="Glucoside xylosyltransferase 2"
FT /id="PRO_0000288540"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..444
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 31..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 51479 MW; 6417FCF53DBFA002 CRC64;
MKLRSKAAAL LLLALAVLLL ALLSLRARRD PEPPGFPARP EAAPQRRHAP VPTLPPEPRA
FPGAAGRRSP RRQPPRLRPR AGRPRAASRE KLARRPGETR SLHSVPPELW IHLAVVACGN
RLEETLVMLK SAVLFSHRKM RFHIFTEDAL KPEFDKQLRQ WPDSYTKKFE HRLYPITFSV
GNPQEWKKLF KPCAAQRLFL PAILKDVDSL LYVDTDVLFL RPVDDIWKLL RQFNSTQLAA
MAPEHEIPKI GWYSRFARHP FYGSAGVNSG VMLMNLTRIR NTQFKNSLIP AGLAWEEMLL
PLYQKYKSAI TWGDQDLLNI IFYYNPECLY VFPCQWNYRP DHCMYGSNCK EAEREGVSVL
HGNRGVYHDD KQPTFRALYE AIRDFPFQDN LFQSMYYPLQ LKFLETVHTL CGRIPQVFLK
QIEKTMRRAY EKHVIIHMGP NPMS