SQV3_CAEEL
ID SQV3_CAEEL Reviewed; 289 AA.
AC P34548;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Xylosylprotein 4-beta-galactosyltransferase {ECO:0000305|PubMed:11005858};
DE Short=XGalT-I {ECO:0000305};
DE EC=2.4.1.133 {ECO:0000269|PubMed:11005858};
DE AltName: Full=Squashed vulva protein 3;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase sqv-3 {ECO:0000305};
GN Name=sqv-3; ORFNames=R10E11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9927678; DOI=10.1073/pnas.96.3.974;
RA Herman T., Horvitz H.R.;
RT "Three proteins involved in Caenorhabditis elegans vulval invagination are
RT similar to components of a glycosylation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP MUTAGENESIS OF GLY-183 AND VAL-275.
RX PubMed=9927677; DOI=10.1073/pnas.96.3.968;
RA Herman T., Hartwieg E., Horvitz H.R.;
RT "sqv mutants of Caenorhabditis elegans are defective in vulval epithelial
RT invagination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:968-973(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11005858; DOI=10.1073/pnas.97.20.10838;
RA Bulik D.A., Wei G., Toyoda H., Kinoshita-Toyoda A., Waldrip W.R.,
RA Esko J.D., Robbins P.W., Selleck S.B.;
RT "sqv-3, -7, and -8, a set of genes affecting morphogenesis in
RT Caenorhabditis elegans, encode enzymes required for glycosaminoglycan
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10838-10843(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 184-TRP--SER-289.
RX PubMed=31371405; DOI=10.1534/genetics.119.302492;
RA Shimizu T., Kato Y., Sakai Y., Hisamoto N., Matsumoto K.;
RT "N-Glycosylation of the Discoidin Domain Receptor Is Required for Axon
RT Regeneration in Caenorhabditis elegans.";
RL Genetics 213:491-500(2019).
CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of the
CC tetrasaccharide (GlcA-Gal-Gal-Xyl-)Ser core linker of heparan sulfate
CC and chondroitin sulfate. Required for embryonic development
CC (PubMed:11005858). Involved in vulval epithelium invagination
CC (PubMed:9927677). Required for axon regeneration after injury
CC (PubMed:31371405). {ECO:0000269|PubMed:11005858,
CC ECO:0000269|PubMed:31371405, ECO:0000269|PubMed:9927677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose
CC = 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:15297, Rhea:RHEA-COMP:12567, Rhea:RHEA-
CC COMP:12570, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132085, ChEBI:CHEBI:132088; EC=2.4.1.133;
CC Evidence={ECO:0000269|PubMed:11005858};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UBV7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for beta-xylose nitrophenyl (at 17 degrees Celsius)
CC {ECO:0000269|PubMed:11005858};
CC KM=440 uM for beta-N-acetylglucosamine nitrophenyl (at 17 degrees
CC Celsius) {ECO:0000269|PubMed:11005858};
CC KM=680 uM for alpha-N-acetylglucosamine nitrophenyl (at 17 degrees
CC Celsius) {ECO:0000269|PubMed:11005858};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11005858}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11005858}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR EMBL; AJ005867; CAA06744.1; -; mRNA.
DR EMBL; Z29095; CAA82350.1; -; Genomic_DNA.
DR PIR; S40716; S40716.
DR RefSeq; NP_499164.1; NM_066763.6.
DR AlphaFoldDB; P34548; -.
DR SMR; P34548; -.
DR STRING; 6239.R10E11.4; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR EPD; P34548; -.
DR PaxDb; P34548; -.
DR EnsemblMetazoa; R10E11.4.1; R10E11.4.1; WBGene00005021.
DR GeneID; 176382; -.
DR KEGG; cel:CELE_R10E11.4; -.
DR UCSC; R10E11.4; c. elegans.
DR CTD; 176382; -.
DR WormBase; R10E11.4; CE00306; WBGene00005021; sqv-3.
DR eggNOG; KOG3917; Eukaryota.
DR GeneTree; ENSGT00940000157712; -.
DR HOGENOM; CLU_044391_5_0_1; -.
DR InParanoid; P34548; -.
DR OMA; QMNGMSN; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; P34548; -.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:P34548; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00005021; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046525; F:xylosylprotein 4-beta-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Xylosylprotein 4-beta-galactosyltransferase"
FT /id="PRO_0000080552"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..289
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 214..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..62
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 97..99
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 123..124
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 154
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 184
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 186..189
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000305"
FT BINDING 218..220
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 183
FT /note="G->E: In n2841; F1 adults accumulate eggs in the
FT uterus. Embryos are arrested at the 1-cell embryonic stage.
FT Partial collapse of vulva invagination."
FT /evidence="ECO:0000269|PubMed:9927677"
FT MUTAGEN 184..289
FT /note="Missing: In n2842; reduces axon regeneration after
FT injury."
FT /evidence="ECO:0000269|PubMed:31371405"
FT MUTAGEN 275
FT /note="V->F: In n2823; embryos are arrested at the 1-cell
FT embryonic stage."
FT /evidence="ECO:0000269|PubMed:9927677"
SQ 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
