XYLT2_BOVIN
ID XYLT2_BOVIN Reviewed; 867 AA.
AC Q5QQ49;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Xylosyltransferase 2;
DE EC=2.4.2.26 {ECO:0000250|UniProtKB:Q86Y38};
DE AltName: Full=Peptide O-xylosyltransferase 2;
DE AltName: Full=Xylosyltransferase II;
GN Name=XYLT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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, heparan sulfate and dermatan sulfate proteoglycans, such as
CC DCN (By similarity). Transfers D-xylose from UDP-D-xylose to specific
CC serine residues of the core protein (By similarity).
CC {ECO:0000250|UniProtKB:Q9EPL0, ECO:0000250|UniProtKB:Q9H1B5}.
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 -!- PTM: Contains disulfide bonds. {ECO:0000250|UniProtKB:Q86Y38}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ866726; CAI29053.1; -; mRNA.
DR RefSeq; NP_001008667.1; NM_001008667.1.
DR AlphaFoldDB; Q5QQ49; -.
DR SMR; Q5QQ49; -.
DR STRING; 9913.ENSBTAP00000012247; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PRIDE; Q5QQ49; -.
DR GeneID; 493989; -.
DR KEGG; bta:493989; -.
DR CTD; 64132; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; Q5QQ49; -.
DR OrthoDB; 564384at2759; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000009136; Unplaced.
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:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
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..867
FT /note="Xylosyltransferase 2"
FT /id="PRO_0000191404"
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..867
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 41..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 266
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 295..297
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 399..400
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 480
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT BINDING 503..504
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 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..189
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 205..447
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 580..835
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
FT DISULFID 828..841
FT /evidence="ECO:0000250|UniProtKB:Q86Y38"
SQ SEQUENCE 867 AA; 97189 MW; 6776E6FE5D4B3460 CRC64;
MVASARVQKL VRRYKLAIAT ALAILLLQGL VVWSFSVLED DEPGEKGRQK KSRPLDPSEG
SKDTDSSAGR RGSAGRRHGR WRGRAESPGV PVAKVVRAVT SRHRTGRRIP PTPPPEAPGR
QNLSGAAAEE ALVGAAGFPH GDTGSVEGAP QPTDNSFTPK CEIVGKDALS ALARASSKQC
QQEIANVVCL HQAGSLMPKA VPRHCQRAGK MSPGIPWDEV RAQQPADGPP VRIAYMLVVH
GRAIRQLKRL LKAVYHKQHF FYVHVDERSN YLHREVVELA RQYDNVRVTP WRMVTIWGGA
SLLRMYLRSM QDLLEVPGWA WDFFINLSAT DYPTRTNEEL VAFLSKNRDK NFLKSHGRDN
SRFIKKQGLD RLFHECDSHM WRLGERQIPA GIVVDGGSDW FVLTRSFVEY VVYTDDPLVA
QLRQFYTYTL LPAESFFHTV LEISPACESL VDNNMRVTTW NRKMGSKSQY KHIVDWCGCS
PNDFKPQDFL RLQQTARPTF FARKFEAVVN QEIIGQLDYY LYGNYPAGTP GLRSYWENVY
DEPDGIHSLS DVTLTLYHSF SRLGLRRAEA SLRAPGESSC RFEPRGLPSS VHLYFYDDHF
QGYLVTQAVQ SSAQGPAETL EMWLMPQGSL KLLGHSDQAS RLQSLEVGQV GTEWDPKERL
FRNFGGLLGP LDEPVAMQRW ARGPNLTVTV VWIDPTYVVA TSYDIVVDAE TEVTQYKPPL
SRPLRPGAWT VRLLQFWEPL GETRFLVLPL TFNRKLPLRK GKFSQMIAGP PHNEYMEQSF
QGLSGILNLP QLEPAEEAAR LHAELTGPAL EAWTDGEQSS FWSVAGVCAV GPSACPSLEL
CRLTSWSSLS PDPKSELGPV KADGRLR
