XYLT2_RAT
ID XYLT2_RAT Reviewed; 864 AA.
AC Q9EPI0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Xylosyltransferase 2;
DE EC=2.4.2.26 {ECO:0000250|UniProtKB:Q86Y38};
DE AltName: Full=Peptide O-xylosyltransferase 2;
DE AltName: Full=Xylosyltransferase II;
GN Name=Xylt2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11099377; DOI=10.1006/jmbi.2000.4261;
RA Goetting C., Kuhn J., Zahn R., Brinkmann T., Kleesiek K.;
RT "Molecular cloning and expression of human UDP-D-xylose:proteoglycan core
RT protein beta-D-xylosyltransferase and its first isoform XT-II.";
RL J. Mol. Biol. 304:517-528(2000).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of chondroitin
CC sulfate, heparan sulfate and dermatan sulfate proteoglycans, such as
CC DCN (By similarity). Transfers D-xylose from UDP-D-xylose to specific
CC serine residues of the core protein (By similarity).
CC {ECO:0000250|UniProtKB:Q9EPL0, ECO:0000250|UniProtKB:Q9H1B5}.
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:Q9H1B5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H1B5};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9H1B5};
CC Note=Active with either Mg(2+) or Mn(2+), but activity is highest when
CC both are present. {ECO:0000250|UniProtKB:Q9H1B5};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q9H1B5}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q9H1B5}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9H1B5}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9H1B5}. Secreted
CC {ECO:0000250|UniProtKB:Q9H1B5}.
CC -!- PTM: Contains disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ295749; CAC16796.2; -; mRNA.
DR AlphaFoldDB; Q9EPI0; -.
DR SMR; Q9EPI0; -.
DR STRING; 10116.ENSRNOP00000052446; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q9EPI0; 3 sites.
DR PaxDb; Q9EPI0; -.
DR RGD; 619765; Xylt2.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q9EPI0; -.
DR PhylomeDB; Q9EPI0; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR PRO; PR:Q9EPI0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
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:0006024; P:glycosaminoglycan biosynthetic process; ISO:RGD.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; ISO:RGD.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISO:RGD.
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; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..864
FT /note="Xylosyltransferase 2"
FT /id="PRO_0000191409"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..864
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 39..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 267
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 296..298
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 400..401
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 481
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 504..505
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 162..190
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 206..448
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 467..480
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 469..478
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 580..832
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 825..838
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 864 AA; 96790 MW; ED6586B9D886D21D CRC64;
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSGLEE DEPGEKGRQR KPRPLDPGEG
SKDTDSSAGR RGSAGRRHGR WRGRAESPGV PVAKVVRAVT SRQRASRRVP PAPPPEAPGR
QNLSGAAAGE ALIGAAGFPQ HGDTGSVEGA PQPTDNSFTP KCEIVGKDAL SALARASTKH
CQQEIANVVC LHQAGNLMPK SVPRHCQLAG KVSPGIQWEE VRAQQPVSGP LVRIAYMLVV
HGRAVRQLKR LLKAVYHEEH FFYIHVDKRS NYLYREVVEL AQHYDNVRVT PWRMVTIWGG
ASLLRMYLRS MKDLLETPGW TWDFFINLSA TDYPTRTNEE LVAFLSKNRD KNFLKSHGRD
NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD WFVLTRSFVE YVVYTEDPLV
AQLRQFYTYT LLPAESFFHT VLENSPACES LVDNNLRVTN WNRKLGCKCQ YKHIVDWCGC
SPNDFKPQDF LRLQQVSRPT FFARKFESTV NQEVLEILDF HLYGSYPPGT PALKAYWENI
YDMADGPSGL SDVLLTAYTA FARISLRHAA TVSPLATAVC RFEPRGLPSS VHLYFYDDHF
QGYLVTQAVQ PSAQGPAETL EMWLMPQRLL KPLGHSDQAS RLQSLEVGTE WDPKERLFRN
FGGLLGPLDE PVAMQRWARG PNLTATVVWI DPTYVVATSY DITVDADTEV TQYKPPLSLP
LRPGAWTVRL LQFWEPLGET RFLVLPLTFN HKLPLRKDDA SWLHAGPPHN EYMEQSFQGL
SGILNLPQPE AVEEAARRHT ELTGPALEAW TDGELSSFWS VAGLCAIGPS SCPSLELCRL
TSWSSLSPDP KSELGPVKAD GRLR
