GXLT1_RAT
ID GXLT1_RAT Reviewed; 435 AA.
AC Q6GX83;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
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;
DE AltName: Full=S33-D;
GN Name=Gxylt1; Synonyms=Glt8d3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-435, AND INDUCTION.
RX PubMed=16288221; DOI=10.1038/sj.onc.1209210;
RA Iwanaga R., Komori H., Ishida S., Okamura N., Nakayama K., Nakayama K.,
RA Ohtani K.;
RT "Identification of novel E2F1 target genes regulated in cell cycle-
RT dependent and independent manners.";
RL Oncogene 25:1786-1798(2006).
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 -!- INDUCTION: By E2F1. {ECO:0000269|PubMed:16288221}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AABR03055509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03055661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY623036; AAT46050.1; -; mRNA.
DR RefSeq; NP_001094357.1; NM_001100887.1.
DR AlphaFoldDB; Q6GX83; -.
DR SMR; Q6GX83; -.
DR STRING; 10116.ENSRNOP00000055150; -.
DR GlyGen; Q6GX83; 2 sites.
DR PaxDb; Q6GX83; -.
DR Ensembl; ENSRNOT00000058349; ENSRNOP00000055150; ENSRNOG00000005234.
DR GeneID; 300173; -.
DR KEGG; rno:300173; -.
DR CTD; 283464; -.
DR RGD; 1563062; Gxylt1.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000156242; -.
DR InParanoid; Q6GX83; -.
DR OMA; IPIHKEY; -.
DR OrthoDB; 978446at2759; -.
DR PhylomeDB; Q6GX83; -.
DR TreeFam; TF323210; -.
DR PRO; PR:Q6GX83; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005234; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q6GX83; baseline and differential.
DR Genevisible; Q6GX83; RN.
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..435
FT /note="Glucoside xylosyltransferase 1"
FT /id="PRO_0000288536"
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..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 435 AA; 50243 MW; 75A51D4A21074747 CRC64;
MRRYLRVVGL CLACGFCSLL YAFSQLAVSL EEGAAVGRRP QAAVASWLAD GGRGTGRGAG
SAGPGRTGRC KEVSLSYWNP YWMLPSDVCG VNCFWEAAFR YGLKTRPTEK MHLAVVACGD
RLEETVTMLK SALIFSIKPL HVHIFAEDQL HDSFKDRLDS WSFLQRFNYS LYPITFPSDS
AMEWKKLFKP CASQRLFLPL ILKGVDSLLY VDTDVLFLRP VDDIWSLLER FNSTQIAAMA
PEHEEPRVGW YNRFARHPYY GRTGVNSGVM LMNMTRMRRK YFKNDMTTAR LQWGDILMPL
LKKYKLNITW GDQDLLNIMF YHNPESLFVF PCQWNYRPDH CIYGSNCREA EEEGVFILHG
NRGVYHDDKQ PAFRAMYEAL RNCSLEDDSV RSLLKPLELE LQKTVHTYCG KTYKIFIKQL
AKSIRNRYDT PPKER
