ID A0A091VAE8_NIPNI Unreviewed; 836 AA.
AC A0A091VAE8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=Y956_00477 {ECO:0000313|EMBL:KFQ99759.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ99759.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ99759.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ99759.1};
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; KL410807; KFQ99759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VAE8; -.
DR STRING; 128390.A0A091VAE8; -.
DR eggNOG; KOG0799; Eukaryota.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000053283; 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:UP000053283};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFQ99759.1}.
FT DOMAIN 490..670
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..836
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..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ99759.1"
FT NON_TER 836
FT /evidence="ECO:0000313|EMBL:KFQ99759.1"
SQ SEQUENCE 836 AA; 95990 MW; 38821E810BCA622E CRC64;
DGYFSHRPKE KTRTDSNNEN SVPKDFENID NSNFAPRTQR QKHQSELVKK PLSKQKEHLR
KKLEEEKMKE NLLLGKNSNE VVQFSDHPGK NSSSSNNNNL KEIHRSPRQH HLKKSGNSSP
ELRYDQPPKC EVTGKEAISA MSRSKSKQCR QEIAEVYCQH KHGKLMPEKV TRFCTLEGKA
NNNVQWDEDS VEYMPANPVR IAFVLVVHGR ASRQLQRMFK AIYHKDHFYY IHVDKRSNYL
HRQVLQFASQ YPNVRVTSWR MATIWGGASL LSTYLQTMRD LMEMNDWPWD FFINLSAADY
PIRTNDQLVA FLSRYRDMNF LKSHGRDNAR FIRKQGLDRL FLECDTHMWR LGDRRIPEGI
AVDGGSDWFL LNRKFVEYVT FSNDDLVTKM KRYVAPLASQ ALLPGCSFFH TVLENSPYCD
SMVDNNLRIT NWNRKLGCKC QYKHIVDWCG CSPNDFKPAD FHRFQQTARP TFFARKFEAV
VNQEIIGQLD YYLYGNYPSG TPGLRSYWEN VYDEPDGVHT LSDVALTMYH AFSRLGLRRA
ETSFHAAGDN SCRYYAMGHP VSVHLYFLAD RFQGFLIRHH ATNLAVSKLE TLETWVMPKK
VFKIASPPSD FGRLQFSEIG TEWDAKERLF RNFGGLIGPT DEPVGMQKWG KGPNVTVTVI
WVDPVNVIAA TYDILIESSA EFTHYKPPLN LPLRPGVWTI KILHHWVQVA ETKFLVTPLT
FSNRQPIKQE EAMKYHSGPP KNAYMEQSFQ GLNPVLNIPI SAARVDQAKR NAGLVGARLE
AWVDSLVSTV WSAVDICSTG PTACPVMQAC AQTAWSSLSP DPKSELGPVK PDGRLR
//
