XYLT_DROME
ID XYLT_DROME Reviewed; 876 AA.
AC Q7KVA1; Q24116; Q9W034; Q9W035;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Xylosyltransferase oxt;
DE EC=2.4.2.26 {ECO:0000269|PubMed:11929872};
DE AltName: Full=Imaginal disk type I;
DE AltName: Full=Peptide O-xylosyltransferase;
GN Name=oxt; ORFNames=CG17771, CG32300;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, AND COFACTOR.
RX PubMed=11929872; DOI=10.1074/jbc.m201634200;
RA Wilson I.B.H.;
RT "Functional expression of Drosophila melanogaster peptide O-
RT xylosyltransferase, the key enzyme for proteoglycan chain initiation and
RT member of the core 2/I N-acetylglucosaminyltransferase family.";
RL J. Biol. Chem. 277:21207-21212(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 322-876.
RC TISSUE=Imaginal disk;
RA Bessarab D.A., Sun H.Y.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:11929872}.
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:11929872};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11929872};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11929872};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11929872};
CC Note=Divalent metal cations. Calcium or manganese or magnesium.
CC {ECO:0000269|PubMed:11929872};
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=AAA75448.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ430595; CAD23246.1; -; mRNA.
DR EMBL; AE014296; AAF47625.1; -; Genomic_DNA.
DR EMBL; AY069660; AAL39805.1; -; mRNA.
DR EMBL; U32626; AAA75448.1; ALT_FRAME; mRNA.
DR RefSeq; NP_647705.1; NM_139448.4.
DR AlphaFoldDB; Q7KVA1; -.
DR SMR; Q7KVA1; -.
DR BioGRID; 63804; 1.
DR IntAct; Q7KVA1; 27.
DR STRING; 7227.FBpp0072782; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q7KVA1; 5 sites.
DR PaxDb; Q7KVA1; -.
DR PRIDE; Q7KVA1; -.
DR DNASU; 38288; -.
DR EnsemblMetazoa; FBtr0072904; FBpp0072782; FBgn0015360.
DR GeneID; 38288; -.
DR KEGG; dme:Dmel_CG32300; -.
DR CTD; 5020; -.
DR FlyBase; FBgn0015360; oxt.
DR VEuPathDB; VectorBase:FBgn0015360; -.
DR eggNOG; KOG0799; Eukaryota.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000169133; -.
DR HOGENOM; CLU_012840_1_0_1; -.
DR InParanoid; Q7KVA1; -.
DR OMA; QYKGFLV; -.
DR OrthoDB; 564384at2759; -.
DR PhylomeDB; Q7KVA1; -.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 38288; 0 hits in 3 CRISPR screens.
DR ChiTaRS; oxt; fly.
DR GenomeRNAi; 38288; -.
DR PRO; PR:Q7KVA1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0015360; Expressed in egg cell and 24 other tissues.
DR Genevisible; Q7KVA1; DM.
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; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030158; F:protein xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IMP:FlyBase.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IDA:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IMP:FlyBase.
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..876
FT /note="Xylosyltransferase oxt"
FT /id="PRO_0000191414"
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..876
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 134..228
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 312..314
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 415..416
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 498
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 522..523
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..111
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 127..465
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 484..497
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 486..495
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 842..855
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CONFLICT 590
FT /note="Y -> D (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 876 AA; 99098 MW; A034F7584E59DB98 CRC64;
MEQSVSARWL KRYRAFFLIL LLIVAIQLFL AYKSLDIVGG GSGSGFDAAE APASPPPPHA
QARVQPPART KLTAQQLGFQ PECDILAREA ISALQRAKTK DCREHIAQIA CAIQAGRFYA
PQLRSSCPAG NHTANVSLGC FKDEKDRRLL AGYYSSSKTS NSPAKCVELC LQSGYPYAGV
QYGRECFCGY DPPPKASKLP DSSCNTKCLG NAKEICGGFY AMNIYETGIA KFTAQLAATT
PSEETKRVRI AFLLTLNGRA LRQVHRLLKA LYAPEHVYYI HVDERQDYLY RKLLELESKF
PNIRLARKRF STIWGGASLL TMLLQCMEDL LQSNWHWDFV INLSESDFPV KTLDKLVDFL
SANPGRNFVK GHGRETQKFI QKQGLDKTFV ECDTHMWRIG DRKLPAGIQV DGGSDWVALS
RPFVGYVTHP REDDELLQAL LKLFRHTLLP AESFFHTVLR NTKHCTSYVD NNLHVTNWKR
KQGCKCQYKH VVDWCGCSPN DFKPEDWPRL QATEQKSLFF ARKFEPVINQ AVLLQLEEWL
YGPYTSEYAN LHGYWQSLYH HEDVHGSGDD LARSIGDSVM RLSARQAKLY PLELIELTHY
LHRDQYKGFL VRYRARGSTG KPLHLETRVR PTQQGKLARN ARFSKRLRNF EVSTDFDQKE
QIARNFGKLL GPQSDLLLSY TLQANADSGA ASHSYNLTLL WIDPLGRLQD FNELHVEDST
SDVINHSKTL LKHPITPGIW TAKLIGRNSI YAQLKFLIAP LAYYKGYPLA KSSDAEALNA
GLTVALPEDF EMPVEWQQHL QTDDEQFTMR EESLAKGKML GQELHSWIDG LVGQFFQLRE
SCVVEADSEV SLPLCSDAPW SSLAPDPKSD VDALLK
