XYLT1_CANLF
ID XYLT1_CANLF Reviewed; 950 AA.
AC Q5QQ56;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Xylosyltransferase 1;
DE EC=2.4.2.26 {ECO:0000250|UniProtKB:Q86Y38};
DE AltName: Full=Peptide O-xylosyltransferase 1;
DE AltName: Full=Xylosyltransferase I;
GN Name=XYLT1;
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 and dermatan sulfate proteoglycans, such as DCN. Transfers D-
CC xylose from UDP-D-xylose to specific serine residues of the core
CC protein. Required for normal maturation of chondrocytes during bone
CC development, normal onset of ossification and normal embryonic and
CC postnatal skeleton development, especially of the long bones.
CC {ECO:0000250|UniProtKB:Q811B1}.
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:Q86Y38};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q86Y38};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q86Y38}; Single-pass type II membrane protein
CC {ECO:0000250}.
CC -!- PTM: Contains 7 disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ866719; CAI28923.1; -; mRNA.
DR RefSeq; NP_001008718.1; NM_001008718.1.
DR AlphaFoldDB; Q5QQ56; -.
DR SMR; Q5QQ56; -.
DR STRING; 9612.ENSCAFP00000026851; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PaxDb; Q5QQ56; -.
DR PRIDE; Q5QQ56; -.
DR GeneID; 494008; -.
DR KEGG; cfa:494008; -.
DR CTD; 64131; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q5QQ56; -.
DR OrthoDB; 564384at2759; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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; 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:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR039864; Xylosyltrans.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025; PTHR46025; 1.
DR PANTHER; PTHR46025:SF2; PTHR46025:SF2; 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 Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..950
FT /note="Xylosyltransferase 1"
FT /id="PRO_0000191399"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..950
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 42..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 350
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 379..381
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 483..484
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 564
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 587..588
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..274
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 290..531
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 550..563
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 552..561
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 664..918
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 911..924
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 950 AA; 106968 MW; BA21154442399321 CRC64;
MVAAPSARRL VRRSHSALLA ALTVLLLQTL VGWNFSSLHS GAGERRGGAA AGCTEQPAPP
PAPAPRRERR DLPPGPAAPL GACCGGGGRG PPARARARAL AGCPEEPRPQ QPAGQGALPT
RALDGYFSHR PKEKVRTDSN NENSVPKDFE NVDNSNFAPR TQKQKHQPEL AKKPPSRQKE
LLKRRLEQEE KGKGQSFPGK GTHEALPPGG RAAVNGSHGK DAPRQPHTRK SGGGSPELRY
DQPPKCDISG KEAISALSRA KSKHCRQEIG DTYCRHKLGM LMPKKVTRFC SLEGKANKNV
QWDEDSVEYM LANPVRIAFV LVVHGRASRQ LQRMFKAIYH KDHFYYIHVD KRSNYLHRQV
LQFARQYGNV RVTPWRMATI WGGASLLSTY LQSMRDLLEM TDWPWDFFIN LSAADYPIRT
NDQLVAFLSR YRDMNFLKSH GRDNARFIRK QGLDRLFLEC DAHMWRLGDR RIPEGIAVDG
GSDWFLLNRK FVEYVTFSTD DLVTKMKQFY SYTLLPAESF FHTVLENSPH CDTMVDNNLR
ITNWNRKLGC KCQYKHIVDW CGCSPNDFKP QDFHRFQQTA RPTFFARKFE AVVNQEIIGQ
LDYYLYGNYP AGTPGLRSYW ENVYDEPDGI HSLSDVALTL YHSFARLGLR RAESSLHVET
GNSCRYYPMG HPASVHLYFL ADRFQGFLIK HHATNLAVSK LETLETWVMP KKVFKIASPP
SDFGRLQFSE VRVGTDWDAK ERLFRNFGGL LGPMDEPVGM QKWGKGPNVT VTVIWVDPVN
IIAATYDILI ESTAEFTHYK PPLNLPLRPG VWTVKILHHW VPVAETKFLV APLTFSNRQP
IKPEEVLKLH NGPLRSAYME QSFQSLNPVL SLPISPAQVE QARRNAGSTG ATLEHWLDSL
VGGTWTAMDI CATGPTACPV MQTCTHTAWS SFSPDPKSEL GAVKPDGRLR
