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Database: UniProt
Entry: A0A091EMJ4_CORBR
LinkDB: A0A091EMJ4_CORBR
Original site: A0A091EMJ4_CORBR 
ID   A0A091EMJ4_CORBR        Unreviewed;       807 AA.
AC   A0A091EMJ4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Xylosyltransferase 1 {ECO:0000256|ARBA:ARBA00015604};
DE            EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE   AltName: Full=Peptide O-xylosyltransferase 1 {ECO:0000256|ARBA:ARBA00030536};
DE   AltName: Full=Xylosyltransferase I {ECO:0000256|ARBA:ARBA00032285};
DE   Flags: Fragment;
GN   ORFNames=N302_11947 {ECO:0000313|EMBL:KFO59123.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO59123.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO59123.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO59123.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001814};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
CC   -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004840}.
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005093}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC       subfamily. {ECO:0000256|ARBA:ARBA00010195}.
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DR   EMBL; KK718885; KFO59123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091EMJ4; -.
DR   STRING; 85066.A0A091EMJ4; -.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000052976; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030158; F:protein xylosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   InterPro; IPR043538; XYLT.
DR   InterPro; IPR024448; XylT_C.
DR   PANTHER; PTHR46025:SF2; XYLOSYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR   Pfam; PF02485; Branch; 1.
DR   Pfam; PF12529; Xylo_C; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO59123.1}.
FT   DOMAIN          482..662
FT                   /note="Xylosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12529"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO59123.1"
FT   NON_TER         807
FT                   /evidence="ECO:0000313|EMBL:KFO59123.1"
SQ   SEQUENCE   807 AA;  92910 MW;  DC077D1E804FFD3C CRC64;
     DGYFSHRPKE KMRTDSNNEN SVPKDFETID NSNFAPRTQR QKHQSELVKK PLSKQKEHLR
     KKLEEEKMKE NLLLGKNSNE AVQVSDHPGK NISVSSNLKD IDRSPKQHLL KKVENSSPEL
     KYDQPARCEV TGKEAVSAMS RAKSKQCRQE IADVYCQHKL GKLMPEQVTR FCALEGKANN
     NVQWDEDSVE YMPANPVRIA FVLVVHGRAS RQLQRMFKAI YHKDHFYYIH VDKRSNYLHR
     QVLQFASQYP NVRVTPWRMA TIWGGASLLT TYLQTMKDLM EMSDWPWDFF INLSAADYPI
     RTNDQLVAFL YRDMNFLKSH GRDNARFIRK QGLDRLFLEC DTHMWRLGDR KIPEGITVDG
     GSDWFLLNRK FVEYVTFSND DLVTKMKRFY SYTLLPAESF FHTVLENSPF CDSMVDNNLR
     ITNWNRKLGC KCQYKHIVDW CGCSPNDFKP ADFHRFQQTA RPTFFARKFE AVVNQEIIGQ
     LDYYLYGNYP SGTPGLRSYW ENVYEEPDGV SALSDVALTM FHSFSRLGLR RAETSFHAAG
     DNSCRYYPMG HPVSIHLYFL ADRFQGFLIR HHATNLAVSK LETLETWVMP KKVFKIASPP
     SDFGRLQFSE IGTEWDAKER LFRNFGGLLG PTDEPVGMQK WGKGPNVTVT VIWVDPINVI
     AATYDILIES SAEFTHYKPP LNLPLRPGVW TIKILHHWVQ VAETKFLVTP LTFSNQQPIK
     QEEAIKLHNG PPKNAYMEQS FQGLNPVLNI PVSAARLDQA KRSAGLVRAR RQASCPVLQG
     CAQTAWSSLS PDPKSELGPV KPDGRLR
//
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