XYLT_CAEEL
ID XYLT_CAEEL Reviewed; 806 AA.
AC Q965Q8; Q867S3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Xylosyltransferase sqv-6;
DE EC=2.4.2.26 {ECO:0000269|PubMed:12584198};
DE AltName: Full=Peptide O-xylosyltransferase;
DE AltName: Full=Squashed vulva protein 6;
GN Name=sqv-6; ORFNames=Y50D4C.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], FUNCTION, ENZYME ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12584198; DOI=10.1074/jbc.c200518200;
RA Hwang H.-Y., Olson S.K., Brown J.R., Esko J.D., Horvitz H.R.;
RT "The Caenorhabditis elegans genes sqv-2 and sqv-6, which are required for
RT vulval morphogenesis, encode glycosaminoglycan galactosyltransferase II and
RT xylosyltransferase.";
RL J. Biol. Chem. 278:11735-11738(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wilson I.B.H.;
RT "Cloning of Caenorhabditis elegans xylosyltransferase cDNA.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614 AND ASN-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Catalyzes the first step in biosynthesis of
CC glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific
CC serine residues of the core protein. Initial enzyme in the biosynthesis
CC of chondroitin sulfate and dermatan sulfate proteoglycans in
CC fibroblasts and chondrocytes. Required for vulval morphogenesis and
CC zygotic cytokinesis, suggesting that glycosaminoglycans play a central
CC role in vulval morphogenesis. {ECO:0000269|PubMed:12584198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-
CC L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:50192, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:12567, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132085; EC=2.4.2.26;
CC Evidence={ECO:0000269|PubMed:12584198};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms are infertile because of the failure of the
CC progeny of homozygous mutants to initiate cytokinesis and because of
CC the failure to form an extracellular space between the egg and the
CC eggshell. {ECO:0000269|PubMed:12584198}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY241928; AAO85277.1; -; mRNA.
DR EMBL; AJ496235; CAD42732.1; -; mRNA.
DR EMBL; FO081564; CCD72442.1; -; Genomic_DNA.
DR RefSeq; NP_503359.2; NM_070958.3.
DR AlphaFoldDB; Q965Q8; -.
DR SMR; Q965Q8; -.
DR BioGRID; 54695; 2.
DR STRING; 6239.Y50D4C.4; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR iPTMnet; Q965Q8; -.
DR EPD; Q965Q8; -.
DR PaxDb; Q965Q8; -.
DR PeptideAtlas; Q965Q8; -.
DR EnsemblMetazoa; Y50D4C.4a.1; Y50D4C.4a.1; WBGene00005024.
DR GeneID; 190099; -.
DR KEGG; cel:CELE_Y50D4C.4; -.
DR UCSC; Y50D4C.4; c. elegans.
DR CTD; 190099; -.
DR WormBase; Y50D4C.4a; CE35919; WBGene00005024; sqv-6.
DR eggNOG; KOG0799; Eukaryota.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000169133; -.
DR HOGENOM; CLU_012840_1_0_1; -.
DR InParanoid; Q965Q8; -.
DR OMA; RMFRIGK; -.
DR OrthoDB; 564384at2759; -.
DR PhylomeDB; Q965Q8; -.
DR BRENDA; 2.4.2.26; 1045.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR PRO; PR:Q965Q8; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00005024; Expressed in adult organism and 3 other tissues.
DR ExpressionAtlas; Q965Q8; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030158; F:protein xylosyltransferase activity; IDA:WormBase.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IGI:WormBase.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0030210; P:heparin biosynthetic process; IGI:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0033319; P:UDP-D-xylose metabolic process; IDA:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR002889; WSC_carb-bd.
DR InterPro; IPR043538; XYLT.
DR PANTHER; PTHR46025; PTHR46025; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF01822; WSC; 1.
DR SMART; SM00321; WSC; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..806
FT /note="Xylosyltransferase sqv-6"
FT /id="PRO_0000191413"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..806
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 109..205
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT BINDING 264
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 293..295
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 398..399
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 479
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 505..506
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..85
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 101..445
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 464..478
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 466..476
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 772..778
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 806 AA; 93115 MW; 6EF779BEA4B570CB CRC64;
MLFNGTTKYR DYAIVISLFF LLNVYLLYNT AQHTQVGNSK HISSDSGEKT SNPLPSCEIT
DDLAKSAISR AITPSCKAKL QLEACQLKNG TFTINFPENQ CPNHDSRLID QRIGCFLDKK
EARVLTEFEY KLPKSNGKAT CRKHCYKAGF LYFGLEFGHE CFCGNDVSNA TAVDDVECRA
YKCPGNENSE EFCGGFNAVE IFRTGFRSKV NHRKPTYLPP SSDSIKNPVK ILFLLQLNGR
NERQVKRFLK SIYLPHHYYY IHVDARQNYM FSEMQKVADF LDNIHITERR FSTIWGGASL
LQMFLQVIRD SMKIEKFKDW DYIINFSESD FPILPISDFE RLITVNNGKS FLASHGYNTG
KFIQKQGFEY VFSECDNRMF RIGKREFPQN LRIDGGSDWV GIHRNLAEFS ISDEELPRKL
RKTYESILLP LESFYHTLAF NSEFCDDLLM SNLRLTNWYR KQGCRCASLK PIVDWCGCSP
LVFREETMKK FELQKAISKP TYFARKFDSM VDIDSIEAAE MQSISPEKLQ LNHPTYHFAF
ANIFKTGIDE QKLHFESLAN FALKSTETRA KFRKVLRIDA LRAHHNALIE IVMKIETTDG
ATFEFLIHRL SHVNLTENEE KLVEHGYLLR AVSFGTKFEW KEELCREYMG FVTDNDTLHT
RLQWHPTEHV KKVGDKTSPE MIFKYRKGDE LIEQTVVKPY DSVFGGQFDS WNVGKKLSNL
TTCSNFFVDI ISPSSPDDAP PLATLHFPVY TDQNAHCHVD YLRQFFKIAD FCTSGDACKE
KIWSTSYPDP KSDIFVGYDE DTQTLI
