XYLT_CAEBR
ID XYLT_CAEBR Reviewed; 803 AA.
AC Q5QQ52; A8XS06; Q60ZC1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Xylosyltransferase sqv-6;
DE EC=2.4.2.26 {ECO:0000250|UniProtKB:Q965Q8};
DE AltName: Full=Peptide O-xylosyltransferase;
DE AltName: Full=Squashed vulva protein 6;
GN Name=sqv-6; Synonyms=xt; ORFNames=CBG17882;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ouzzine M., Fournel-Gigleux S., Mollicone R., Oriol R.;
RT "Phylogeny of animal protein xylosyltransferases.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. {ECO:0000250|UniProtKB:Q965Q8}.
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:0000250|UniProtKB:Q965Q8};
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 -!- 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; AJ866723; CAI28926.1; -; mRNA.
DR EMBL; HE601413; CAP35425.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5QQ52; -.
DR SMR; Q5QQ52; -.
DR STRING; 6238.CBG17882; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR EnsemblMetazoa; CBG17882a.1; CBG17882a.1; WBGene00037395.
DR WormBase; CBG17882a; CBP37604; WBGene00037395; Cbr-sqv-6.
DR eggNOG; KOG0799; Eukaryota.
DR eggNOG; KOG4157; Eukaryota.
DR HOGENOM; CLU_012840_1_0_1; -.
DR InParanoid; Q5QQ52; -.
DR OMA; RMFRIGK; -.
DR OrthoDB; 564384at2759; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000008549; Chromosome V.
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; IBA:GO_Central.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
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 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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..803
FT /note="Xylosyltransferase sqv-6"
FT /id="PRO_0000191412"
FT TOPO_DOM 3..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..803
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 115..209
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT BINDING 265
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 294..296
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 399..400
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 480
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 506..507
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..91
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 107..446
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 465..479
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 467..477
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 769..775
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 803 AA; 92745 MW; EB3D2F7D6BEA6F26 CRC64;
MVVVGGVNTN YRHYALVIVL FFFLNVYLLY SAQNSVQIRK DEGETREKFQ TPKVPLVDPI
STCEIVDELA KSAISRATSP GCKSKLQLEA CQLKNGTFSE SFPQSTCSNH QDALIDQRIG
CFLDKKDARV LKEFEYKFPQ SNSKSTCRKN CYKAGFLYYG LEFGLECFCG NDVANATEID
SGECRNYKCP GAEDEFCGGF NAVEIFRTDK LVMLKPKYLP PAENVSKPPI KILFLLQLNG
RNERQVKRFL KSIYLPNHYY YIHVDKRQNY MYSEMAKIAE KVPNIHITST RYSTIWGGAS
LLQMFQQVIR DSMEIEMFKD WDYIFNFSES DFPILPIQDF ERLITEHQGK SFLASHGYNT
GKFIQKQGFE FVFSECDQRM FRIGKREFPE NLRIDGGSDW VGIHRDLAEY SISNEELPQK
LRKTFESILL PLESFYHTLA FNSKFCDDLM MSNLRLTNWL RKQGCRCASL KQIVDWCGCS
PLVFREDTKI KFEMQKAISK PTYFARKFDS MVDIEAIESA EQQSMSTSKI QMDHPTYHFA
YANIFKFGID EEKIAHRSLA SFALNTIKSH EKMAKIVQID ALRAHHNAQI EIVMKVETQS
GANFEFLIHR KSHVNLSTSG ALEVDGYVLK DVVYGTKFEW KEEICREYMG FVTEKDTLHT
RLEWSPTERV KKNDKTSPEI EFQYRNGPEK IDKSIVKPYD SVFGGQFDSW DVGKRLSNLS
TCPDFFVDVF SPSSSESPLA TLRFSVYTEQ NVDCHVAYLR DFFEIVDFCT SETACGEKIW
SMSYPDPKSD IQVGWDEEAR ILR
