XYLT1_MOUSE
ID XYLT1_MOUSE Reviewed; 953 AA.
AC Q811B1; Q9EPL1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Xylosyltransferase 1;
DE EC=2.4.2.26 {ECO:0000269|PubMed:24161523};
DE AltName: Full=Peptide O-xylosyltransferase 1;
DE AltName: Full=Xylosyltransferase I;
GN Name=Xylt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15461586; DOI=10.1042/bj20041206;
RA Mueller S., Schoettler M., Schoen S., Prante C., Brinkmann T., Kuhn J.,
RA Goetting C., Kleesiek K.;
RT "Human xylosyltransferase I: functional and biochemical characterization of
RT cysteine residues required for enzymic activity.";
RL Biochem. J. 386:227-236(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-950.
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17189265; DOI=10.1074/jbc.m611665200;
RA Poenighaus C., Ambrosius M., Casanova J.C., Prante C., Kuhn J., Esko J.D.,
RA Kleesiek K., Goetting C.;
RT "Human xylosyltransferase II is involved in the biosynthesis of the uniform
RT tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate
RT proteoglycans.";
RL J. Biol. Chem. 282:5201-5206(2007).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17517600; DOI=10.1073/pnas.0700908104;
RA Condac E., Silasi-Mansat R., Kosanke S., Schoeb T., Towner R., Lupu F.,
RA Cummings R.D., Hinsdale M.E.;
RT "Polycystic disease caused by deficiency in xylosyltransferase 2, an
RT initiating enzyme of glycosaminoglycan biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9416-9421(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PATHWAY, AND MUTAGENESIS OF TRP-932.
RX PubMed=24161523; DOI=10.1016/j.ydbio.2013.10.014;
RA Mis E.K., Liem K.F. Jr., Kong Y., Schwartz N.B., Domowicz M.,
RA Weatherbee S.D.;
RT "Forward genetics defines Xylt1 as a key, conserved regulator of early
RT chondrocyte maturation and skeletal length.";
RL Dev. Biol. 385:67-82(2014).
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:0000269|PubMed:24161523}.
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:0000269|PubMed:24161523};
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:0000269|PubMed:24161523}.
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:0000269|PubMed:24161523}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain, spleen, kidney and testis, and
CC at low levels in skeletal muscle. {ECO:0000269|PubMed:17189265,
CC ECO:0000269|PubMed:17517600}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic chondrocytes in humerus and
CC ulna during embryonic bone development. Not detected in mature bone.
CC {ECO:0000269|PubMed:24161523}.
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; AJ539164; CAD62249.1; -; mRNA.
DR EMBL; AJ291750; CAC18566.1; -; mRNA.
DR CCDS; CCDS40101.1; -.
DR RefSeq; NP_783576.2; NM_175645.3.
DR AlphaFoldDB; Q811B1; -.
DR SMR; Q811B1; -.
DR BioGRID; 231443; 7.
DR STRING; 10090.ENSMUSP00000032892; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q811B1; 3 sites.
DR iPTMnet; Q811B1; -.
DR PhosphoSitePlus; Q811B1; -.
DR MaxQB; Q811B1; -.
DR PaxDb; Q811B1; -.
DR PRIDE; Q811B1; -.
DR ProteomicsDB; 299802; -.
DR DNASU; 233781; -.
DR GeneID; 233781; -.
DR KEGG; mmu:233781; -.
DR CTD; 64131; -.
DR MGI; MGI:2451073; Xylt1.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q811B1; -.
DR OrthoDB; 564384at2759; -.
DR PhylomeDB; Q811B1; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 233781; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Xylt1; mouse.
DR PRO; PR:Q811B1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q811B1; protein.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA: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; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISO:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP: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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..953
FT /note="Xylosyltransferase 1"
FT /id="PRO_0000191401"
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..953
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 327
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 355
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 384..386
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 488..489
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 569
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 592..593
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..279
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 295..536
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 555..568
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 557..566
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 669..921
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 914..927
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT MUTAGEN 932
FT /note="W->R: In pug; strongly reduced enzyme activity leads
FT to defects in proteoglycan synthesis, abnormal chondrocyte
FT maturation, premature ossification and dwarfism with short
FT limbs and a compressed ribcage, which may be the cause for
FT the increased mortality before weaning."
FT /evidence="ECO:0000269|PubMed:24161523"
FT CONFLICT 162
FT /note="A -> L (in Ref. 2; CAC18566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 107298 MW; 816C2068230B36E0 CRC64;
MVAAPCARRL ARRSHSALLA ALMVLLLHTL VVWNFSSLDS GAGEQRRAGA AAGAAEQQQP
AAPRRERRDL AAHLPAARGG PGGRAGGGGA RGGGPGGARA QQPASRGALA SRARDPQPSP
LITLETQDGY FSHRPKEKVR TDSNNENSVP KDFENVDNSN FAPRTQKQKH QPELAKKPPS
RQKEHLQRKL DALDKRQGQS VLGKGPKEVL PPREKATGNS SQGKDLSRHS HARKSGGGGS
PETKSDQAPK CDISGKEAIS ALTRAKSKHC RQEIAETYCR HKLGLLMPEK VARFCPLKGK
AHKNVQWDED AVEYMPANPV RIAFVLVVHG RAFRQFQRMS KAIYHKDHFY YIHVDKRSNY
LHRQGLQFSR QYENVRVTSW KMATIWGGAS FLSTYLQSMR DLLEMTDWPW DFFINLSAAD
YPIRTNDQLV AFLSRYRDMN FLKSHGRDNA RFIRKQGLDR LFLECDTHMW RLGDRRIPEG
IAVDGGSDWF LLNRKFVEYV AFSTDDLVTK MKQFYSYTLL PAESFFHTVL ENSPHCDTMV
DNNLRITNWN RKLGCKCQYK HIVDWCGCSP NDFKPQDFHR FQQTARPTFF ARKFEAIVNQ
EIIGQLDSYL SGNFPAGTPG LRSYWEKLYD QSAPLRSLSD VALTMYHSFI RLGLRRAESS
LHTDGENSCR YYPMGHPVSV HFYFLADRFQ GFLIKHHVTN LAVSKLETLE TWMMPKEVFK
VASPPSDFGR LQFSEVGTDW DAKERLFRNF GGLLGPMDEP VGMQKWGKGP NVTVTVIWVD
PVNVITATYD ILIESTAEFT HYKPPLNLPL RPGVWTVKIL HHWVPVAETK FLVAPLTFSN
KQPIKPEEAL KLHNGPPRSA YMEQSFQSLN PVLSLHINPA QVEQARKNAA FTGTALEAWL
DSLVGGTWTA MDICTTGPTA CPVMQTCSQT AWSSFSPDPK SELGAVKPDG RLR
