XYLT1_RAT
ID XYLT1_RAT Reviewed; 821 AA.
AC Q9EPI1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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;
DE Flags: Fragment;
GN Name=Xylt1;
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 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; AJ295748; CAC16797.1; -; mRNA.
DR AlphaFoldDB; Q9EPI1; -.
DR SMR; Q9EPI1; -.
DR STRING; 10116.ENSRNOP00000025008; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q9EPI1; 3 sites.
DR PaxDb; Q9EPI1; -.
DR PRIDE; Q9EPI1; -.
DR UCSC; RGD:620093; rat.
DR RGD; 620093; Xylt1.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q9EPI1; -.
DR PhylomeDB; Q9EPI1; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000002494; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030158; F:protein xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISO:RGD.
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:0048681; P:negative regulation of axon regeneration; IMP:RGD.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
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; Transferase.
FT CHAIN <1..821
FT /note="Xylosyltransferase 1"
FT /id="PRO_0000191403"
FT TOPO_DOM <1..821
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 226
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 255..257
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 359..360
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 440
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 463..464
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..150
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 166..407
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 426..439
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 428..437
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 540..789
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 782..795
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT NON_TER 1
SQ SEQUENCE 821 AA; 93859 MW; 75186697AD3428A3 CRC64;
YFSHRPKEKV RTDSNNENSV PKDFENVDNS NFAPRTQKQK HQPELAKKPL SRQKERLQRK
LGAQDKGQGQ SVLGKGPKEV LPPREKAPGN SSQGKDLSRH SHSRKSGGGG SPETKSDQVP
KCDISGKEAI SALTRAKSKH CRQEIAETYC RHKLGLLMPE KVARFCPLEG KANKNVQWDE
DAVEYMPPNP VRIAFVLVVH GRASRQLQRM FKAIYHKDHF YYIHVDKRSN YLHRQVLQFS
RQYDNVRVTS WRMATIWGGA SLLSTYLQSM RDLLEMTDWP WDFFINLSAA DYPIRTNDQL
VAFLSRYRDM NFLKSHGRDN ARFIRKQDLD RLFLECDTHM WRLGDRRIPE GIAVDGGSDW
FLLNRKFVEY VAFSTDDLVT KMKQFYSYTL LPAESFFHTV LENSPHCDTM VDNNLRITNW
NRKLGCKCQY KHIVDWCGCS PNDFKPQDFH RFQQTARPTF FARKFEAIVN QEIIGQLDSY
LYGNYPAGTP GLRSYWENVY DEPDGIQSLS DVALTMYHSF IRLGLRRAES SLHTDGENSC
RYYPMGHPAS VHLYFLADRF QGFLIKHHVT NLAVSKLETL ETWMMPKKVF KVASPPSDFG
RLQFSEVGTD WDAKERLFRN FGGLLGPMDE PVGMQKWGKG PNVTVTVIWV DPVNVIAATY
DILIESTAEF THYKPPLNLP LRPGVWTVKI LHHWVPVAET KFLVAPLTFS NKQPIKPEEA
LKLHNGPPRS AYMEQSFQSL NPVLSLHINP AQVEQARKNA AFTGTALEAW LVGGTWTAMD
VCATGPTACP VMQTCSQTAW SSFSPDPKSE LGAVKPDGRL R
