XYLT2_CANLF
ID XYLT2_CANLF Reviewed; 865 AA.
AC Q5QQ50;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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 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; AJ866725; CAI29052.1; -; mRNA.
DR RefSeq; NP_001008714.1; NM_001008714.1.
DR AlphaFoldDB; Q5QQ50; -.
DR SMR; Q5QQ50; -.
DR STRING; 9615.ENSCAFP00000025069; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PaxDb; Q5QQ50; -.
DR Ensembl; ENSCAFT00845022508; ENSCAFP00845017674; ENSCAFG00845012646.
DR GeneID; 493990; -.
DR KEGG; cfa:493990; -.
DR CTD; 64132; -.
DR VEuPathDB; HostDB:ENSCAFG00845012646; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000158326; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; Q5QQ50; -.
DR OMA; AVYHERH; -.
DR OrthoDB; 564384at2759; -.
DR TreeFam; TF315534; -.
DR Reactome; R-CFA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000017026; Expressed in stomach and 49 other tissues.
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:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:Ensembl.
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..865
FT /note="Xylosyltransferase 2"
FT /id="PRO_0000191405"
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..865
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 39..157
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 683
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 581..833
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 826..839
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 865 AA; 96741 MW; AAD79A7F92E6D7C6 CRC64;
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSGLEE DEPGEKGRQR KPRPLDPGEG
SKDTDSSAGR RGSAGRRHGR WRGRAESPGM PVAKVVRAVT SRHRASRRVP PAPPPEAPGR
QNLSGAAAGE ALVGAAGFPP HGDTGSVEGA PQPTDNGFTP KCEIVGKDAL SALARASSKQ
CQQEIANVVC LHQAGNLMPK AVPRHCQLAG KMNPGIQWDE VRAQQPVDGP PVRIAYMLVV
HGRAIRQLKR LLKAVYHEQH FFYIHVDKRS NYLHREVVEL ARQYDNVRVT PWRMVTIWGG
ASLLRMYLRS MQDLLEVPGW AWDFFINLSA TDYPTRTNEE LVAFLSKNRD KNFLKSHGRD
NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD WFVLTRSFVE YVVYTDDPLV
AQLRQFYTYT LLPAESFFHT VLENSPACES LVDNNLRVTN WNRRLGCKCQ YKHIVDWCGC
SPNDFKPQDF LRLQQVSRPT FFARKFESTV NQEVLEILDF HLYGSYPPGT PALKAYWENT
YDAADGPGGL SDVMLTAYTA FARLSLRHAA TAIPPLATPL CRFEPRGLPS SVHLYFYDDH
FQGYLVTQAV QPSAQGPAET LEMWLMPQGS LKLLGRSDQA SRLQSLEVGT EWDPKERLFR
NFGGLLGPLD EPVAMQRWAR GPNLTATVVW IDPTYVVATS YDIAVDADTE VTQYKPPLSR
PLRPGAWTVR LLQFWEPLGE TRFLVLPLTF NRKLPLRKDD ASWLHAGPPH NEYMEQSFQG
LSGILNLPQP EPAEEAARRH AELTGPALEA WTDGELSGFW SVAGLCAMGP SACPSLELCR
LTSWSSVFPD PKSELGPVKA DGRLR
