XYLT1_PANTR
ID XYLT1_PANTR Reviewed; 945 AA.
AC Q5QQ57;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ866718; CAI28922.1; -; mRNA.
DR RefSeq; NP_001032366.1; NM_001037289.1.
DR AlphaFoldDB; Q5QQ57; -.
DR SMR; Q5QQ57; -.
DR STRING; 9598.ENSPTRP00000013343; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PaxDb; Q5QQ57; -.
DR GeneID; 453955; -.
DR KEGG; ptr:453955; -.
DR CTD; 64131; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q5QQ57; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000002277; 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..945
FT /note="Xylosyltransferase 1"
FT /id="PRO_0000191402"
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..945
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 42..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 347
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 376..378
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 BINDING 561
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 584..585
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 243..271
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 287..528
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 547..560
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 549..558
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 661..913
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 906..919
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 945 AA; 106077 MW; 8517B6DF3ED53554 CRC64;
MQAAPCARRL ARRSHSALLA ALTVLLLQTL VVWNFSSLDS GAGERRGGAA VGGGEQPPPA
PRRERRDLPA EPAAARGGGG GGGGCGGGGR GPQARARGGG PGEPRGQQPA SRGALPARAL
DGYFSHRPKE KVRTDSNNEN SVPKDFENVD NSNFAPRTQK QKHQPELAKK PPSRQKELLK
RKLEQQEKGK GHTFPGKGPG EVLPPGDRAA ANSSHGKDVS RPPHARKTGG SSPETKYDQP
PKCDISGKEA ISALSRAKSK HCRQEIGETY CRHKLGLLMP EKVTRFCPLE GKANKNVQWD
EDSVEYMPAN PVRIAFVLVV HGRASRQLQR MFKAIYHKDH FYYIHVDKRS NYLHRQVLQV
SRQYSNVRVT PWRMATIWGG ASLLSTYLQS MRDLLEMTDW PWDFFINLSA ADYPIRTNDQ
LVAFLSRYRD MNFLKSHGRD NARFIRKQGL DRLFLECDAH MWRLGDRRIP EGIAVDGGSD
WFLLNRRFVE YVTFSTDDLV TKMKQFYSYT LLPAESFFHT VLENSPHCDT MVDNNLRITN
WNRKLGCKCQ YKHIVDWCGC SPNDFKPQDF HRFQQTARPT FFARKFEAVV NQEIIGQLDY
YLYGNYPAGT PGLRSYWENV YDEPDGIHSL SDVTLTLYHS FARLGLRRAE TSLHTDGENS
CRYYPMGHPA SVHLYFLADR FQGFLIKHHA TNLAVSKLET LETWVMPKKV FKIASPPSDF
GRLQFSEVGT DWDAKERLFR NFGGLLGPMD EPVGMQKWGK GPNVTVTVIW VDPVNVIAAT
YDILIESTAE FTHYKPPLNL PLRPGVWTVK ILHHWVPVAE TKFLVAPLTF SNRQPIKPEE
ALKLHNGPLR NAYMEQSFQS LNPVLSLPIS PAQVEQARRN AASTGTALEG WLDSLVGGMW
TAMDICATGP TACPVMQTCS QTAWSSFSPD PKSELGAVKP DGRLR
