XYLT_CIOIN
ID XYLT_CIOIN Reviewed; 848 AA.
AC Q5QQ55;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Xylosyltransferase;
DE EC=2.4.2.26;
DE AltName: Full=Peptide O-xylosyltransferase;
GN Name=xt;
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719;
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; AJ866720; CAI28924.1; -; mRNA.
DR RefSeq; NP_001029012.1; NM_001033840.1.
DR AlphaFoldDB; Q5QQ55; -.
DR SMR; Q5QQ55; -.
DR STRING; 7719.NP_001029012.1; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PRIDE; Q5QQ55; -.
DR Ensembl; ENSCINT00000009027; ENSCINP00000009027; ENSCING00000004363.
DR GeneID; 619275; -.
DR KEGG; cin:619275; -.
DR CTD; 619275; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000169133; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; Q5QQ55; -.
DR OMA; EASEWAN; -.
DR TreeFam; TF315534; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000008144; 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; 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; 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..848
FT /note="Xylosyltransferase"
FT /id="PRO_0000191410"
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 824..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 247
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 276..278
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 379..380
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 460
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 482..483
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..173
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 189..427
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 446..459
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 448..457
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 529..811
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 794..822
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 848 AA; 98092 MW; 96BA85C4B70C0F00 CRC64;
MSLHRTLRRF LRKWKALVYA VSFILLIQAF FTFQSSPNLM EEEHLRRLKE LQIKKHQELA
NSMLQGERAL VHGRDKLVLN PRDPGFREEF FKHSNNEINI LEDHNIGQVD KMEKPVLKPN
ENKFEEIHFA TEKVPEIIVK YQPKCDITIK DSISALSRAT TDRCKQQIAD AACKMQDGTL
FPKSMPRTCK HESKFTFDAP MPTSFDPDIR PVRICYMLVV HGRAIRQLRR LLKVIYHRDH
YYYIHVDKRS DYLLREVLKE TEQYPNIKVA PWRMATIWGG SSLLQTLLRA ISDVLRIWKD
WDFFINLSAL DFPIEKDEKL VQYLSKYRDK NFMKSHGRED EKFIRKQGLN RVFVECDQHM
WRLGERQLPE GITVNGGSDW VALNRRLCDF AVNGNDQLLT QLKHWYEYTL LPAESFFHTL
VQNSDLCETF VDNNIRVTNW NRARGCKCQY KHIVDWCGCS PNDFYPSDLV RLRTSRPVFF
ARKFEESINQ EVVNHLDFKL YGDYPPGTPA LHSLWENALR VNSKMPSDCN LSVVSMLQVE
MHKKDEEFVG YVVTFDAGWV GRRGAGDDPA TSEDGSRVQL QAFLSPQPSL RILDRSSNLA
KRLETASVGT NWDVKELVIR DWGGLVGPNS DVHLVARWSR SEDDFVVTVV VIDPLNVVAD
YNDFRTPSKA AGVTETPLSL KKPLRPGRWL VRFYVQRQFT NICAELDFYV TPQEFKGGIE
GDSVLREINR GVVDDAQVNA ANRNLYSIRT TLNLARNNQA ETELASESNH VAGLKLRNWV
DFVVSSGWKA KDACLVAQSP ETWREAQPRR CFMPRQGTPN LCENTNWSSL SPDPKTELIS
VKPDGRIR
