XYLT_DROPS
ID XYLT_DROPS Reviewed; 880 AA.
AC Q5QQ53; Q2LYT4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Xylosyltransferase oxt;
DE EC=2.4.2.26 {ECO:0000250|UniProtKB:Q7KVA1};
DE AltName: Full=Peptide O-xylosyltransferase;
GN Name=oxt; Synonyms=xt; ORFNames=GA16815;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
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=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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:Q7KVA1}.
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:Q7KVA1};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q7KVA1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q7KVA1};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7KVA1};
CC Note=Divalent metal cations. Calcium or manganese or magnesium.
CC {ECO:0000250|UniProtKB:Q7KVA1};
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 -!- SEQUENCE CAUTION:
CC Sequence=EAL29776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ866722; CAI28925.1; -; mRNA.
DR EMBL; CH379069; EAL29776.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001354039.1; XM_001354003.3.
DR AlphaFoldDB; Q5QQ53; -.
DR SMR; Q5QQ53; -.
DR STRING; 7237.FBpp0274031; -.
DR EnsemblMetazoa; FBtr0275593; FBpp0274031; FBgn0076829.
DR GeneID; 4813803; -.
DR KEGG; dpo:Dpse_GA16815; -.
DR eggNOG; KOG0799; Eukaryota.
DR eggNOG; KOG4157; Eukaryota.
DR HOGENOM; CLU_012840_1_0_1; -.
DR InParanoid; Q5QQ53; -.
DR OMA; QYKGFLV; -.
DR PhylomeDB; Q5QQ53; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR ChiTaRS; oxt; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0076829; Expressed in female reproductive system and 3 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR002889; WSC_carb-bd.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025; PTHR46025; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF01822; WSC; 1.
DR Pfam; PF12529; Xylo_C; 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; Magnesium; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..880
FT /note="Xylosyltransferase oxt"
FT /id="PRO_0000191415"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..880
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 138..232
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT BINDING 287
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 316..318
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 419..420
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 502
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 526..527
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..115
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 131..469
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 488..501
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 490..499
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 846..859
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 880 AA; 99651 MW; 45D87F312B202202 CRC64;
MEQSVSARWL RRYRPVLIIL VLIFGIQLFL AYKSVDIGGG SGSGLDVDAA QRSQRDLASN
PVIAEPPESL PRPARLTANQ LGFQPECDIQ AKEAISALQR AKTKDCRQHI AQIACSIQAG
RFYAIQLKSS CPSGNHTANV SLGCYRDEKD RRLLGGYYTS FKNSNSPNLC LELCLQSGYP
YAGVQYGREC FCGFDTPPKA AKLPDSSCNI KCLGNAREIC GGFYAMNIYE TGIAKFTAQL
AASTPPTGAK RVRIAFLLTI NGRALRQVHR LLKALYAPEH VYYIHVDERQ DYLYRKLLEL
EQKFPNIRLA RKRFSTIWGG ASLLTMLLQC MEDLLKSKWQ WDFVINLSES DFPVKTLDKL
VDFLSANRGR NFVKGHGRET QKFIQKQGLD RTFVECDTHM WRIGDRKLPA GIQVDGGSDW
VALSRPFVAY VTHPKKEDEL LQALLKLFRH TLLPAESFFH TVLRNTHHCH TYVDNNLHVT
NWKRKQGCKC QYKHVVDWCG CSPNDFMPDD WPRLLATEQK SLFFARKFEP IINQAVLLQL
EEWLYGPYTS EYLNLHGYWQ SLYHHEDVHG SADDLVRSVG DSLMRLAGSQ ARVDPLELLE
LTHYLHRDQY KGFLVRFSAR RATGQDVQLE TRVRPVQHGK LARNARFSKR LRNFEVSTDF
DQKEQVARNF GKLLGPQSDL VLSYTYQGST DSGAASHSYN LTLLWIDPLG RLQDFNELHV
EDSSTDLINH SKTLLSHPIT PGVWTAKLIG RSSIYAQLKF LISPMAYGNG EPLETTPEAE
KRNGGLGIAL PDDFELPVEW QQHLHTDDEQ FSLREEALAN GKLTGPPLHR WIDDLVGKFF
QLRESCVVDA GTELSLPLCS DAPWSSLAPD PKSDVDALLK
