XYLT2_MOUSE
ID XYLT2_MOUSE Reviewed; 865 AA.
AC Q9EPL0; Q5SUY1; Q8K060;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Xylosyltransferase 2;
DE EC=2.4.2.26;
DE AltName: Full=Peptide O-xylosyltransferase 2;
DE AltName: Full=Xylosyltransferase II;
GN Name=Xylt2;
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].
RA Goetting C.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-865.
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of chondroitin
CC sulfate, heparan sulfate and dermatan sulfate proteoglycans, such as
CC DCN (PubMed:17517600). Transfers D-xylose from UDP-D-xylose to specific
CC serine residues of the core protein (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1B5, ECO:0000269|PubMed:17517600}.
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 -!- TISSUE SPECIFICITY: Detected in brain, liver, lung, kidney, heart,
CC spleen and testis, and at lower levels in skeletal muscle.
CC {ECO:0000269|PubMed:17189265}.
CC -!- PTM: Contains disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate. Their livers display strongly reduced levels of heparan sulfate
CC proteoglycan. DCN glycosylation is altered and lacks chondroitin
CC sulfate groups. After 3 to 5 months, all mutant mice display increased
CC liver weight. At an age of 4 to 5 months, about half of them delevop
CC liver cysts, due to biliary epithelial cell hyperplasia. At an age of 3
CC and 10 months, mutant mice also display increased kidney weight due to
CC hydronephrosis and impaired renal function, but they do not develop
CC cysts. {ECO:0000269|PubMed:17517600}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ291751; CAC18567.2; -; mRNA.
DR EMBL; AL645764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034082; AAH34082.1; ALT_INIT; mRNA.
DR CCDS; CCDS48888.1; -.
DR RefSeq; NP_665827.2; NM_145828.3.
DR AlphaFoldDB; Q9EPL0; -.
DR SMR; Q9EPL0; -.
DR BioGRID; 229845; 2.
DR IntAct; Q9EPL0; 1.
DR STRING; 10090.ENSMUSP00000112052; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q9EPL0; 3 sites.
DR iPTMnet; Q9EPL0; -.
DR PhosphoSitePlus; Q9EPL0; -.
DR MaxQB; Q9EPL0; -.
DR PaxDb; Q9EPL0; -.
DR PRIDE; Q9EPL0; -.
DR ProteomicsDB; 299803; -.
DR Antibodypedia; 2239; 99 antibodies from 15 providers.
DR DNASU; 217119; -.
DR Ensembl; ENSMUST00000116349; ENSMUSP00000112052; ENSMUSG00000020868.
DR GeneID; 217119; -.
DR KEGG; mmu:217119; -.
DR UCSC; uc007kzi.2; mouse.
DR CTD; 64132; -.
DR MGI; MGI:2444797; Xylt2.
DR VEuPathDB; HostDB:ENSMUSG00000020868; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000158326; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; Q9EPL0; -.
DR OMA; AVYHERH; -.
DR OrthoDB; 564384at2759; -.
DR PhylomeDB; Q9EPL0; -.
DR TreeFam; TF315534; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR BioGRID-ORCS; 217119; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Xylt2; mouse.
DR PRO; PR:Q9EPL0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9EPL0; protein.
DR Bgee; ENSMUSG00000020868; Expressed in ectoplacental cone and 91 other tissues.
DR ExpressionAtlas; Q9EPL0; baseline and differential.
DR Genevisible; Q9EPL0; MM.
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:0006024; P:glycosaminoglycan biosynthetic process; IMP:MGI.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; IMP:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:MGI.
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_0000191407"
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..155
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"
FT CONFLICT 94
FT /note="K -> N (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="N -> K (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="GC -> AG (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="C -> S (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="N -> K (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="P -> R (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..506
FT /note="RKF -> GKL (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="L -> V (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="L -> V (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="P -> A (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 675..676
FT /note="MQ -> LR (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="T -> R (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 768..770
FT /note="PPH -> QPQ (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="G -> V (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="P -> S (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="R -> Q (in Ref. 1; CAC18567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 865 AA; 96811 MW; DA30B77B9807A797 CRC64;
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSGLEE DEPGEKGRQR KPRPLDPGEG
SKDTDSSAGR RGSAGRRHGR WRGRAESPGV PVAKVVRAVT SRQRASRRVP PAPPPEAPGR
QNLSGAAAGE ALIGAPGFPQ HGDTGSVEGA PQPTDNTFTP KCEIVGKDAL SALARASTKQ
CQQEIANVVC LHQAGNLMPK SVPRHCQLAG KMSPGVQWEE IRAQQPVGGP PVRIAYMLVV
HGRAIRQLKR LLKAVYHEQH FFYIHVDKRS NYLYREVVEL AQHYENVRVT PWRMVTIWGG
ASLLRMYLRS MKDLLEIPGW TWDFFINLSA TDYPTRTNEE LVAFLSKNRD KNFLKSHGRD
NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD WFVLTRSFVE YVVYTDDPLV
AQLRQFYTYT LLPAESFFHT VLENSPACAS LVDNNLRVTN WNRKLGCKCQ YKHIVDWCGC
SPNDFKPQDF LRLQQVSRPT FFARKFESTV NQEVLEILDF HLYGSYPPST PALKAYWENI
YDVADGPGGL SDVLLTAYTA FARLSLRHAA TAVSPLATAV CRFEPRGLPS SVHLYFYDDH
FQGYLVTQAV QPSAQGPAET LEMWLMPQRS LKLLGHSDQA SRLQSLEVGT EWDPKERLFR
NFGGLLGPLD EPVAMQRWAR GPNLTATVVW IDPTYVVATS YDITVDADTE VTQYKPPLSL
PLRPGAWTVR LLQFWEPLGE TRFLVLPLTF NRKLPLRKDD ASWLHAGPPH NEYMEQSFQG
LSGILNLPQA EALEEAARRH TELTGSALEA WTDGELSNFW SVAGLCAIGP SACPSLELCR
LTSWSSLSPD PKSELGPVKA DGRLR
