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Database: UniProt
Entry: A0A016SDT7_9BILA
LinkDB: A0A016SDT7_9BILA
Original site: A0A016SDT7_9BILA 
ID   A0A016SDT7_9BILA        Unreviewed;       897 AA.
AC   A0A016SDT7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
GN   Name=Acey_s0240.g3345 {ECO:0000313|EMBL:EYB88863.1};
GN   Synonyms=Acey-sqv-6 {ECO:0000313|EMBL:EYB88863.1};
GN   ORFNames=Y032_0240g3345 {ECO:0000313|EMBL:EYB88863.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB88863.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
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:EYB88863.1}.
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DR   EMBL; JARK01001576; EYB88863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SDT7; -.
DR   STRING; 53326.A0A016SDT7; -.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000024635; 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:UP000024635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          201..294
FT                   /note="WSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51212"
SQ   SEQUENCE   897 AA;  102875 MW;  E645401497612896 CRC64;
     MRKRSTPALR TAAPAAIAPH RIPVLRTMYI VAATLLFFFL NLYFIYVYVQ NYSKDELVRS
     FEKSHLSQSK EDSQHIRSTP GINFHSCDIS DQLALSALSR AKTESCRRKL QHEGFGRCRP
     HITQLLVLFR SMIVPRVYVN CPSSRIDQRN EYRPAVKWQL LVCTVHWNRE EISDAACKLK
     NGLFHDSFPE SQCVNHDRLL INFRVGCFED SKSNRALNGF AYEFKSDNSM EKCRATCYRA
     GFIYYGLEFG RECFCGDSLA KQSIDEARCT EYRCTGNSSQ YCGGFNAVEI FRTGLKEPHL
     MPKAKYVETA DADVNTKRPR ILFLLQLNGR NERQVKRLLK ALYSPHHYYY IHVDQRQLYM
     LTEVKAVAAK LSNVYVAPDP HSTIWGGASL LTMVQDAIRR SIAMPSLSDW DYLINLSESD
     FPVLTLNELE TQLRMNPGQS YMSSHGYNTA RFIQKQGFDF VFIECENRMW RIGKRDEFPR
     NLRIDGGSDW IILHREFAEY SISDDELPRK MRALFGSIIL PVESFFHTLS YNSHFCNSIL
     GSNLRLTNWN RKQGCRCESL KKVVDWCGCS PLVFKKEHTH KFAIKNAQAK PFYIARKFES
     LIDIDAIALA EKQAMRDRPH LLHTDDVMFN VTFVNHYKAD IDGYSLPFSM MAESLLSMYD
     KDAEFVSLLR IDAVKVHSSA PHQIIFTMQI RQSDVPLQLL VQRRLVSHIV SPAIVDGFKL
     ESVMAGTEID HKEEIFRGFT AYADVTSSPV VLLRWSRVTG MATTVNETKT SPPIRYLWRG
     PKEKLVATQK LRSYDSMYGG QFAALQLKNL NTSNLEAGMW SVVIQTDRGE SPETIATVWL
     PIYSTDDKPL FQSLVGNFFI IQDSCSKTCF STTWSTFHPD PKSDILVGYD KTVEALV
//
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