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Xylosylprotein 4-beta-galactosyltransferase (XGalT-I) (EC 2.4.1.133) (Squashed vulva protein 3) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase sqv-3)

 SQV3_CAEEL              Reviewed;         289 AA.
P34548;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
28-MAR-2018, entry version 123.
RecName: Full=Xylosylprotein 4-beta-galactosyltransferase {ECO:0000305|PubMed:11005858};
Short=XGalT-I {ECO:0000305};
EC=2.4.1.133 {ECO:0000269|PubMed:11005858};
AltName: Full=Squashed vulva protein 3;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase sqv-3 {ECO:0000305};
Name=sqv-3; ORFNames=R10E11.4;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Bristol N2;
PubMed=9927678; DOI=10.1073/pnas.96.3.974;
Herman T., Horvitz H.R.;
"Three proteins involved in Caenorhabditis elegans vulval invagination
are similar to components of a glycosylation pathway.";
Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=7906398; DOI=10.1038/368032a0;
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
Wohldman P.;
"2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
elegans.";
Nature 368:32-38(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
MUTAGENESIS OF GLY-183 AND VAL-275.
PubMed=9927677; DOI=10.1073/pnas.96.3.968;
Herman T., Hartwieg E., Horvitz H.R.;
"sqv mutants of Caenorhabditis elegans are defective in vulval
epithelial invagination.";
Proc. Natl. Acad. Sci. U.S.A. 96:968-973(1999).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
AND SUBCELLULAR LOCATION.
PubMed=11005858; DOI=10.1073/pnas.97.20.10838;
Bulik D.A., Wei G., Toyoda H., Kinoshita-Toyoda A., Waldrip W.R.,
Esko J.D., Robbins P.W., Selleck S.B.;
"sqv-3, -7, and -8, a set of genes affecting morphogenesis in
Caenorhabditis elegans, encode enzymes required for glycosaminoglycan
biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 97:10838-10843(2000).
-!- FUNCTION: Glycosyltransferase required for the biosynthesis of the
tetrasaccharide (GlcA-Gal-Gal-Xyl-)Ser core linker of heparan
sulfate and chondroitin sulfate. Required for embryonic
development (PubMed:11005858). Involved in vulval epithelium
invagination (PubMed:9927677). {ECO:0000269|PubMed:11005858,
ECO:0000269|PubMed:9927677}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + O-beta-D-xylosyl-
[protein] = UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein].
{ECO:0000269|PubMed:11005858}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q9UBV7};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=47 uM for beta-xylose nitrophenyl (at 17 degrees Celsius)
{ECO:0000269|PubMed:11005858};
KM=440 uM for beta-N-acetylglucosamine nitrophenyl (at 17
degrees Celsius) {ECO:0000269|PubMed:11005858};
KM=680 uM for alpha-N-acetylglucosamine nitrophenyl (at 17
degrees Celsius) {ECO:0000269|PubMed:11005858};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:11005858}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11005858};
Single-pass type II membrane protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ005867; CAA06744.1; -; mRNA.
EMBL; Z29095; CAA82350.1; -; Genomic_DNA.
PIR; S40716; S40716.
RefSeq; NP_499164.1; NM_066763.6.
UniGene; Cel.37560; -.
ProteinModelPortal; P34548; -.
SMR; P34548; -.
STRING; 6239.R10E11.4; -.
CAZy; GT7; Glycosyltransferase Family 7.
EPD; P34548; -.
PaxDb; P34548; -.
EnsemblMetazoa; R10E11.4; R10E11.4; WBGene00005021.
GeneID; 176382; -.
KEGG; cel:CELE_R10E11.4; -.
UCSC; R10E11.4; c. elegans.
CTD; 176382; -.
WormBase; R10E11.4; CE00306; WBGene00005021; sqv-3.
eggNOG; KOG3917; Eukaryota.
eggNOG; ENOG410Z0TP; LUCA.
GeneTree; ENSGT00760000119140; -.
HOGENOM; HOG000286021; -.
InParanoid; P34548; -.
KO; K00733; -.
OMA; KAATPWC; -.
OrthoDB; EOG091G0HCH; -.
PhylomeDB; P34548; -.
Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
UniPathway; UPA00378; -.
PRO; PR:P34548; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00005021; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:WormBase.
GO; GO:0008378; F:galactosyltransferase activity; IDA:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046525; F:xylosylprotein 4-beta-galactosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:WormBase.
GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
GO; GO:0018991; P:oviposition; IMP:WormBase.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
GO; GO:0022604; P:regulation of cell morphogenesis; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0040025; P:vulval development; IMP:WormBase.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR003859; Galactosyl_T.
InterPro; IPR027791; Galactosyl_T_C.
InterPro; IPR027995; Galactosyl_T_N.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19300; PTHR19300; 2.
Pfam; PF02709; Glyco_transf_7C; 1.
Pfam; PF13733; Glyco_transf_7N; 1.
PRINTS; PR02050; B14GALTRFASE.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Glycosyltransferase; Magnesium;
Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 289 Xylosylprotein 4-beta-
galactosyltransferase.
/FTId=PRO_0000080552.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 289 Lumenal. {ECO:0000255}.
REGION 58 62 UDP-alpha-D-galactose binding.
{ECO:0000250|UniProtKB:Q9UBV7}.
REGION 97 99 UDP-alpha-D-galactose binding.
{ECO:0000250|UniProtKB:Q9UBV7}.
REGION 123 124 UDP-alpha-D-galactose binding.
{ECO:0000250|UniProtKB:Q9UBV7}.
REGION 186 189 N-acetyl-D-glucosamine binding.
{ECO:0000305}.
REGION 218 220 UDP-alpha-D-galactose binding.
{ECO:0000250|UniProtKB:Q9UBV7}.
METAL 124 124 Manganese.
{ECO:0000250|UniProtKB:Q9UBV7}.
METAL 218 218 Manganese; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9UBV7}.
BINDING 154 154 UDP-alpha-D-galactose.
{ECO:0000250|UniProtKB:Q9UBV7}.
BINDING 184 184 UDP-alpha-D-galactose.
{ECO:0000250|UniProtKB:Q9UBV7}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 183 183 G->E: In n2841; F1 adults accumulate eggs
in the uterus. Embryos are arrested at
the 1-cell embryonic stage. Partial
collapse of vulva invagination.
{ECO:0000269|PubMed:9927677}.
MUTAGEN 275 275 V->F: In n2823; embryos are arrested at
the 1-cell embryonic stage.
{ECO:0000269|PubMed:9927677}.
SEQUENCE 289 AA; 33807 MW; 16C2C1F5AF35DC91 CRC64;
MKLKTRLILS GTILISLAAC YFLVLLVLDL EITRDLMTDY VDPRPLQTSY HKLCVIVPYR
DRLEELREFS PHMSKFLHNQ NVSHHILIIN QTDPLRFNRA SLINVGWNEA DRLGCDYMVM
NDVDLLPVNP EVPYDFPGIG VIRHITSPQY HPKYHYEKFI GGILMLTLKD YKKLNGMSNK
YWGWGLEDDE FYLRIIDSKL NLTRVSGLST DSSNTFRHIH GPKRKRDYTP KKNDKNQWEI
KRKRDHVSGL HDVRYLIDSR QLLDFSGTSV TIINVALHCD LNWTPYCKS


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