ID Q4S7R2_TETNG Unreviewed; 907 AA.
AC Q4S7R2;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 62.
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};
GN ORFNames=GSTENG00022671001 {ECO:0000313|EMBL:CAG03320.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG03320.1};
RN [1] {ECO:0000313|EMBL:CAG03320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG03320.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG03320.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAAE01014712; CAG03320.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4S7R2; -.
DR KEGG; tng:GSTEN00022671G001; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 559..741
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAG03320.1"
SQ SEQUENCE 907 AA; 102397 MW; 8D93A03FCDAA4E5A CRC64;
MAPKPPDGLS SELDAQSSED GYYSHRPKEK NKVDSNNENS VPKDFENIDN SNFGARSQPR
RQSVGAGSSK QQREQLQEKA HSRQAWRDSS PGRERSSNEV LPLGQQPLAF GNNGSHLDSP
RQQDHVSRAQ QTQPQHRHQH PHRRQATAAL LEVSYDQPPK CEISGKEAIS ALARAKSKEC
RQQIAEVYCR HKEGQLMPER VTRYCPLEGK ANANVQWDED SAESFPLKPV RIAFVLAVHG
RASRQFQRLF KAIYHTSHYY YIHVDQRSNY LHRQVQALAA LYPNVRVTPW RMATIWGGAS
LLTMYLRSMA DLLAMRDWSW DFFINLSAAD YPIRTNNQLV AFLSRYRNMN FIKSHGRDNA
RFIRKQGLDR LFYECDTHMW RLGDRKIPEG VSVDGGSDWF LLNRLFVEYV INSQDDLVAN
MKRFYAYTLL PAESFFHTVL ENSAHCESMV DNNLRITNWN RKLGCKCQYK HIVDWCGCSP
NDFKPADFHR FQSHPPRDSP GPSGFSPGPA SLGRSSLAPR SCAPASHPGL RLDSKRCGPP
SSPGSSEASV NQEVVNQLDS YLFGPFPQGT KGLSSYWENV YDEPDGVASL SDTRLTYYHS
FSRLGLARAA ASLQGNPKDH SCRYFPMGHP VSVHLYFHSD QFQGYLVKHH ATNLATSKLE
TLETWVSPKN NFKLTGAPGS TFSRLQFAEI GAEWDAKERM FRNFGGLLGP TDETVGMQRW
SKGANVTVTV VWIDPTNVIA ATYDILIDAN AEFTHYRPPL NQPLRPGVWS VRILYHWSPV
AEMRFLVAPL TYSKHQPIRQ DDALKLHNGP AKNSYMEQSF HGLNPVLNIP VSLGYVEQAK
RNAALTGQQL EHWVDGLVGE LWEAADICAV GPTACPVMQA CPKNPWSSMS PDPKSHLGPP
RADGRIR
//
