XYLT_CIOSA
ID XYLT_CIOSA Reviewed; 843 AA.
AC Q5QQ54;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Xylosyltransferase;
DE EC=2.4.2.26;
DE AltName: Full=Peptide O-xylosyltransferase;
GN Name=xt;
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511;
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.
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.
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 -!- 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}.
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DR EMBL; AJ866721; CAI29051.1; -; mRNA.
DR AlphaFoldDB; Q5QQ54; -.
DR SMR; Q5QQ54; -.
DR STRING; 51511.ENSCSAVP00000018421; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PRIDE; Q5QQ54; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q5QQ54; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000007875; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025; PTHR46025; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF12529; Xylo_C; 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..843
FT /note="Xylosyltransferase"
FT /id="PRO_0000191411"
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..843
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 823..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 245
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 274..276
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 377..378
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 458
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 480..481
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..171
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 187..425
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 444..457
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 446..455
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 527..806
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 789..817
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 843 AA; 97474 MW; 422230AF8E9363DF CRC64;
MGFRRNFRRV LRKWKVIVYA VSFILLLQAF FTFQSSPNLI EEEHLKRIKE LQIRKHQELA
QKMLQGERSL VDGKIFLNPH DPGFREQFFK HANDSINILE DHDVGKVAKM EKLPSKLKPH
NFEEIQFEAE TKIPSIVKYQ PKCEITLKDS LSALSRATSD ACKQQIADTA CKMQDNTLFP
ESMPRTCPHE NKFKFDAPMP ATFDPDLRPV RICYMLVVHG RAVRQLRRLL KVIYHRNHYY
YIHVDKRSDY LLREIIKETE QYPNIKVAPW RMATIWGGSS LLRTLLRAIS DVLKIWKDWD
FFINLSALDF PIEKDEKLVQ YLTKYRDKNF MKSHGREDDK FIRKQGLNRV FVECDTHMWR
LGERTLPKGI IVNGGSDWVA LNRRLCDYAV FGNDQLLVQL KHWYEYTLLP AESFFHTLVQ
NSDMCESFVD NNLRVTNWNR ARGCKCQYKH IVDWCGCSPN DFYPADLVRL HTSRPVFFAR
KFEESINQEV VNHLDFKLHG EYPPGTPGLH SLWENALRVN EKIPPNCDLH VASVLQVEMY
KKDEEFSGYV VTFDAGWLKA GESEEVIDGS ARVQLQALLS HQPTLRMLDR TSALSKRLES
ASVGTNWDIK ELVLRDWGGL IGPNSDLHLV ARWSRSDDDF VVTVVVIDPV NVVADYNDFR
TPSKAAGVTE TPLSLKKPLR PGRWVVRFYV QRQFTNICAE LDFYVTPLEF KDGAEGDSQL
REINRGVVDD AQLNAASRNL YSIRTTLNLP HNNLAATELA NQAVHVDGAK LRRWVDAVAS
GAYKAKDACL VAQATETWRE AQPRRCYTPR QITPNLCENL NWSSMSPDPK SEMIPVKPDG
RIR
