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Database: UniProt
Entry: H3D3E5_TETNG
LinkDB: H3D3E5_TETNG
Original site: H3D3E5_TETNG 
ID   H3D3E5_TETNG            Unreviewed;       815 AA.
AC   H3D3E5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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};
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|Ensembl:ENSTNIP00000015033.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
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|Ensembl:ENSTNIP00000015033.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; H3D3E5; -.
DR   STRING; 99883.ENSTNIP00000015033; -.
DR   Ensembl; ENSTNIT00000015235.1; ENSTNIP00000015033.1; ENSTNIG00000012071.1.
DR   GeneTree; ENSGT00940000157381; -.
DR   HOGENOM; CLU_012840_0_0_1; -.
DR   InParanoid; H3D3E5; -.
DR   OMA; HWDFVIN; -.
DR   TreeFam; TF315534; -.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000007303; 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:UP000007303};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          467..649
FT                   /note="Xylosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12529"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..815
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..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  93031 MW;  39A2409DD8C43F48 CRC64;
     DGYYSHRPKE KNKVDSNNEN SVPKDFENID NSNFGARSQP RRQSVGAGSS KQQREQLQEK
     AHSRQAWRDS SPGRERSSNE VLPLGQQPLA FGNNGSHLDS PRQQDYDQPP KCEISGKEAI
     SALARAKSKE CRQQIAEVYC RHKEGQLMPE RVTRYCPLEG KANANVQWDE DSAESFPLKP
     VRIAFVLAVH GRASRQFQRL FKAIYHTSHY YYIHVDQRSN YLHRQVQALA ALYPNVRVTP
     WRMATIWGGA SLLTMYLRSM ADLLAMRDWS WDFFINLSAA DYPIRTNNQL VAFLSRYRNM
     NFIKSHGRDN ARFIRKQGLD RLFYECDTHM WRLGDRKIPE GVSVDGGSDW FLLNRLFVEY
     VINSQDDLVA NMKRFYAYTL LPAESFFHTV LENSAHCESM VDNNLRITNW NRKLGCKCQY
     KHIVDWCGCS PNDFKPADFH RFQQTVRPTF FARKFASVNQ EVVNQLDSYL FGPFPQGTKG
     LSSYWENVYD EPDGVASLSD TRLTYYHSFS RLGLARAAAS LQGNPKDHSC RYFPMGHPVS
     VHLYFHSDQF QGYLVKHHAT NLATSKLETL ETWVSPKNNF KLTGAPGSTF SRLQFAEIGA
     EWDAKERMFR NFGGLLGPTD ETVGMQRWSK GANVTVTVVW IDPTNVIAAT YDILIDANAE
     FTHYRPPLNQ PLRPGVWSVR ILYHWSPVAE MRFLVAPLTY SKHQPIRQDD ALKLHNGPAK
     NSYMEQSFHG LNPVLNIPVS LGYVEQAKRN AALTGQQLEH WVDGLVGELW EAADICAVGP
     TACPVMQACP KNPWSSMSPD PKSHLGPPRA DGRIR
//
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