GXLT1_HUMAN
ID GXLT1_HUMAN Reviewed; 440 AA.
AC Q4G148; B3KWJ2; Q8IXV1; Q96BH4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glucoside xylosyltransferase 1;
DE EC=2.4.2.42 {ECO:0000269|PubMed:19940119};
DE AltName: Full=Glycosyltransferase 8 domain-containing protein 3;
GN Name=GXYLT1; Synonyms=GLT8D3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19940119; DOI=10.1074/jbc.c109.065409;
RA Sethi M.K., Buettner F.F., Krylov V.B., Takeuchi H., Nifantiev N.E.,
RA Haltiwanger R.S., Gerardy-Schahn R., Bakker H.;
RT "Identification of glycosyltransferase 8 family members as
RT xylosyltransferases acting on O-glucosylated notch epidermal growth factor
RT repeats.";
RL J. Biol. Chem. 285:1582-1586(2010).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-237.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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:0000269|PubMed:19940119}.
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:0000269|PubMed:19940119};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4G148-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4G148-2; Sequence=VSP_025709;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AK125141; BAG54154.1; -; mRNA.
DR EMBL; CH471111; EAW57832.1; -; Genomic_DNA.
DR EMBL; BC015597; AAH15597.2; -; mRNA.
DR EMBL; BC030023; AAH30023.1; -; mRNA.
DR EMBL; BC039145; AAH39145.1; -; mRNA.
DR CCDS; CCDS41771.1; -. [Q4G148-2]
DR CCDS; CCDS41772.1; -. [Q4G148-1]
DR RefSeq; NP_001093120.1; NM_001099650.1. [Q4G148-2]
DR RefSeq; NP_775872.1; NM_173601.1. [Q4G148-1]
DR AlphaFoldDB; Q4G148; -.
DR SMR; Q4G148; -.
DR BioGRID; 129573; 104.
DR IntAct; Q4G148; 8.
DR STRING; 9606.ENSP00000381666; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyConnect; 1270; 3 N-Linked glycans (1 site).
DR GlyGen; Q4G148; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q4G148; -.
DR PhosphoSitePlus; Q4G148; -.
DR SwissPalm; Q4G148; -.
DR BioMuta; GXYLT1; -.
DR DMDM; 269849602; -.
DR EPD; Q4G148; -.
DR jPOST; Q4G148; -.
DR MassIVE; Q4G148; -.
DR MaxQB; Q4G148; -.
DR PaxDb; Q4G148; -.
DR PeptideAtlas; Q4G148; -.
DR PRIDE; Q4G148; -.
DR ProteomicsDB; 62154; -. [Q4G148-1]
DR ProteomicsDB; 62155; -. [Q4G148-2]
DR Antibodypedia; 66044; 66 antibodies from 12 providers.
DR DNASU; 283464; -.
DR Ensembl; ENST00000280876.6; ENSP00000280876.6; ENSG00000151233.11. [Q4G148-2]
DR Ensembl; ENST00000398675.8; ENSP00000381666.3; ENSG00000151233.11. [Q4G148-1]
DR GeneID; 283464; -.
DR KEGG; hsa:283464; -.
DR MANE-Select; ENST00000398675.8; ENSP00000381666.3; NM_173601.2; NP_775872.1.
DR UCSC; uc001rms.5; human. [Q4G148-1]
DR CTD; 283464; -.
DR DisGeNET; 283464; -.
DR GeneCards; GXYLT1; -.
DR HGNC; HGNC:27482; GXYLT1.
DR HPA; ENSG00000151233; Low tissue specificity.
DR MIM; 613321; gene.
DR neXtProt; NX_Q4G148; -.
DR OpenTargets; ENSG00000151233; -.
DR PharmGKB; PA165512868; -.
DR VEuPathDB; HostDB:ENSG00000151233; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000156242; -.
DR HOGENOM; CLU_040965_0_0_1; -.
DR InParanoid; Q4G148; -.
DR OMA; IPIHKEY; -.
DR OrthoDB; 978446at2759; -.
DR PhylomeDB; Q4G148; -.
DR TreeFam; TF323210; -.
DR PathwayCommons; Q4G148; -.
DR SignaLink; Q4G148; -.
DR SIGNOR; Q4G148; -.
DR BioGRID-ORCS; 283464; 12 hits in 1085 CRISPR screens.
DR ChiTaRS; GXYLT1; human.
DR GenomeRNAi; 283464; -.
DR Pharos; Q4G148; Tdark.
DR PRO; PR:Q4G148; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q4G148; protein.
DR Bgee; ENSG00000151233; Expressed in pigmented layer of retina and 177 other tissues.
DR Genevisible; Q4G148; HS.
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; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..440
FT /note="Glucoside xylosyltransferase 1"
FT /id="PRO_0000288534"
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..440
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VAR_SEQ 74..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025709"
FT CONFLICT 211
FT /note="D -> N (in Ref. 3; AAH30023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50567 MW; 1A68504D913DBF0E CRC64;
MRRYLRVVVL CVACGFCSLL YAFSQLAVSL EEGTGGGGGK PQAAVASWLA GGGRGAVRGA
GVAGPAAHPG VSDRCKDFSL CYWNPYWMLP SDVCGMNCFW EAAFRYSLKI QPVEKMHLAV
VACGERLEET MTMLKSAIIF SIKPLQFHIF AEDQLHHSFK GRLDNWSFLQ TFNYTLYPIT
FPSENAAEWK KLFKPCASQR LFLPLILKEV DSLLYVDTDI LFLRPVDDIW SLLKKFNSTQ
IAAMAPEHEE PRIGWYNRFA RHPYYGKTGV NSGVMLMNMT RMRRKYFKND MTTVRLQWGD
ILMPLLKKYK LNITWGDQDL LNIVFFHNPE SLFVFPCQWN YRPDHCIYGS NCQEAEEGGI
FILHGNRGVY HDDKQPAFRA VYEALRNCSF EDDNIRSLLK PLELELQKTV HTYCGKIYKI
FIKQLAKSVR DRYARSPKEK
