GXLT1_MOUSE
ID GXLT1_MOUSE Reviewed; 404 AA.
AC Q3UHH8; B7ZWC3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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, Gm87;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UHH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHH8-2; Sequence=VSP_025710;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AK147387; BAE27879.1; -; mRNA.
DR EMBL; AC127360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04286.1; -; Genomic_DNA.
DR EMBL; BC141302; AAI41303.1; -; mRNA.
DR EMBL; BC171972; AAI71972.1; -; mRNA.
DR CCDS; CCDS27764.1; -. [Q3UHH8-2]
DR CCDS; CCDS88828.1; -. [Q3UHH8-1]
DR RefSeq; NP_001028447.1; NM_001033275.4. [Q3UHH8-2]
DR RefSeq; XP_006520912.1; XM_006520849.1.
DR AlphaFoldDB; Q3UHH8; -.
DR SMR; Q3UHH8; -.
DR STRING; 10090.ENSMUSP00000047281; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyConnect; 2338; 2 N-Linked glycans (1 site).
DR GlyGen; Q3UHH8; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q3UHH8; -.
DR PhosphoSitePlus; Q3UHH8; -.
DR SwissPalm; Q3UHH8; -.
DR MaxQB; Q3UHH8; -.
DR PaxDb; Q3UHH8; -.
DR PRIDE; Q3UHH8; -.
DR ProteomicsDB; 271370; -. [Q3UHH8-1]
DR ProteomicsDB; 271371; -. [Q3UHH8-2]
DR Antibodypedia; 66044; 66 antibodies from 12 providers.
DR Ensembl; ENSMUST00000049484; ENSMUSP00000047281; ENSMUSG00000036197. [Q3UHH8-2]
DR Ensembl; ENSMUST00000230063; ENSMUSP00000155854; ENSMUSG00000036197. [Q3UHH8-1]
DR GeneID; 223827; -.
DR KEGG; mmu:223827; -.
DR UCSC; uc007xiq.1; mouse. [Q3UHH8-2]
DR UCSC; uc011zyf.1; mouse. [Q3UHH8-1]
DR CTD; 283464; -.
DR MGI; MGI:2684933; Gxylt1.
DR VEuPathDB; HostDB:ENSMUSG00000036197; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000156242; -.
DR HOGENOM; CLU_040965_0_0_1; -.
DR InParanoid; Q3UHH8; -.
DR PhylomeDB; Q3UHH8; -.
DR TreeFam; TF323210; -.
DR BioGRID-ORCS; 223827; 3 hits in 57 CRISPR screens.
DR PRO; PR:Q3UHH8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UHH8; protein.
DR Bgee; ENSMUSG00000036197; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q3UHH8; baseline and differential.
DR Genevisible; Q3UHH8; 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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="Glucoside xylosyltransferase 1"
FT /id="PRO_0000288535"
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..404
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 353..404
FT /note="SLEDDSVRSLLKPLELELQKTVHTYCGKTYKIFIKQLTKSIRNRYDTPPKER
FT -> WCLTASAVSLRGFRGWSGTD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025710"
SQ SEQUENCE 404 AA; 46491 MW; A0D1C1B9A2B6ADBC CRC64;
MRRYLRVVGL CLACGFCSLL YAFSQLAVSL EEGAAGGRRP QAAVVSWLAD GGRGTGRGAG
SAGPGRTGRY DMKTRPDEKM HLAVVACGER LEETVTMLKS ALIFSIKPLH VHIFAEDQLH
DSFKDRLASW SFLRRFDYSL YPITFPGDSA ADWKKLFKPC ASQRLFLPLI LKEVDSLLYV
DTDILFLRPV DDIWSLLKKF NSTQIAAMAP EHEEPRIGWY NRFARHPYYG RTGVNSGVML
MNMTRMRRKY FKNDMTTARL QWGDILMPLL KKYKLNITWG DQDLLNIVFS HNPESLFVFP
CQWNYRPDHC IYGSNCREAE EEGVFILHGN RGVYHDDKQP AFRAVYEALR NCSLEDDSVR
SLLKPLELEL QKTVHTYCGK TYKIFIKQLT KSIRNRYDTP PKER
