ID A0A0K0E9U8_STRER Unreviewed; 787 AA.
AC A0A0K0E9U8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein xylosyltransferase {ECO:0000256|ARBA:ARBA00011972};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE AltName: Full=Peptide O-xylosyltransferase {ECO:0000256|ARBA:ARBA00042865};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000628000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000628000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004840}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. 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; A0A0K0E9U8; -.
DR STRING; 6248.A0A0K0E9U8; -.
DR WBParaSite; SSTP_0000628000.1; SSTP_0000628000.1; SSTP_0000628000.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IPR002889; WSC_carb-bd.
DR InterPro; IPR043538; XYLT.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR PANTHER; PTHR46025:SF3; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF01822; WSC; 1.
DR SMART; SM00321; WSC; 1.
DR PROSITE; PS51212; WSC; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..190
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
SQ SEQUENCE 787 AA; 92440 MW; 8FD871D4FAEF96E7 CRC64;
MGLKFFKYGL ISITFCFIFN LIFIYIIESP HLVKKNLKNG WCSKLNNSLA KSTFERLKTE
KCKEKVFDFV CQQKMPLIIN NSCPFFDEKL KGSYIGCYKD SHNNRILSSY NIIFPKINSP
KKCINTCIQG GYIYAGVEYT KECFCGEKID FNNSLVVKID DSNCQKYKCP PPNDNFYCGG
YEAIAIYSTG IKEYKRPYPE YIEVTSKNKN NEVKILFLLQ LNGRNDRQVK RMLKSIYHPK
HFYIIHVDKR QKYMYEKMKN LEKILPNFVV SNKRWSTIWG GASLLTMYLK LVESQLDKEW
DFVINMSESD FLVIPLDELE IQLSLNKGIN FISSHGSNSG KFIKKQGFYF KFMECEERMW
RIEERDTFPE NMYIDGGSDW IIIHRSLIIY ALSNESLPID LRNIFKTILL PLESFFHTLG
YNSKFCDKIK ARNLRLTYWK RKQGCRCAKL KKTVDWCGCS PLVFRNSDTN YIQLSVVKQK
ATYFARKFDD FVDIRAIHFA EKQALKNRQN INDIILQNHP SYNSSWVNLY NINCDGNNEL
INNWSKILLE YQNDCQFINI TDINTFKDNS FSETKFVLTI NGKCSNRISK IEFLVDYVQH
KSLIKNFTID NFILLDVKFG LNLDLKEEIF RDPTNLLSKT KTAYILFSWK DLIKNPSVNE
RKTSPPLYLE WYDGNESLVL IQNVSSYDSI FYNQYSLLEL DTLPNVKPGS WKLLIKDSIN
GKLAGTIYFP VFDFSENTNN YFLIEKFYKI IDNCFDDECK NFSWSTIFPN PKSDIIVGYD
KKLNWIV
//