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Database: UniProt
Entry: F0ZAC6_DICPU
LinkDB: F0ZAC6_DICPU
Original site: F0ZAC6_DICPU 
ID   F0ZAC6_DICPU            Unreviewed;       473 AA.
AC   F0ZAC6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
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   ORFNames=DICPUDRAFT_93669 {ECO:0000313|EMBL:EGC39100.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC39100.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
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}. 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; GL870963; EGC39100.1; -; Genomic_DNA.
DR   RefSeq; XP_003284352.1; XM_003284304.1.
DR   AlphaFoldDB; F0ZAC6; -.
DR   STRING; 5786.F0ZAC6; -.
DR   EnsemblProtists; EGC39100; EGC39100; DICPUDRAFT_93669.
DR   GeneID; 10510258; -.
DR   KEGG; dpp:DICPUDRAFT_93669; -.
DR   eggNOG; KOG0799; Eukaryota.
DR   InParanoid; F0ZAC6; -.
DR   OMA; SAPSICC; -.
DR   OrthoDB; 5390370at2759; -.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030158; F:protein xylosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   InterPro; IPR043538; XYLT.
DR   PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR   PANTHER; PTHR46025:SF3; XYLOSYLTRANSFERASE OXT; 1.
DR   Pfam; PF02485; Branch; 1.
DR   PROSITE; PS00022; EGF_1; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          17..28
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS00022"
SQ   SEQUENCE   473 AA;  56076 MW;  16493C9AFF65CD02 CRC64;
     MMGKECSNGG IGFQNECICP YSFSGSMCEN RDEKEQCNSL NLETSMFNLY PEFIFGDNDE
     IDKQYSSSVC CWHKYRVNQN YTEKYINEVL VEPTVDNIKE QSKYIKKLLE TYGPWDRNDK
     LLFNYLLTSA NKKGKEDYYL KYADPKYSPP VLEPFKITSS NLAFFLLVSD IKMEEIKTLF
     TYLYRPKHYY VIHVDNNFND TKKIEELELY LDNLFKKSYE IDHYLTDNYP KNYRVMKDRF
     SGSWGSISLV YPEIAAYSIL FDMVEERSAI SRKNETWTHV INLSANDFPV KTVSELEFFL
     RLPTNINRNF LETGPNKESE RYTETFLRTK LGNTIAVKYK DSNVCGSPNN NNPMITNTFY
     KGKSNEGSQW HFLTYKFAHY IISDFNSIRR LLSLKFAMIP DEFFYQQVRN ESPFYPNEAI
     WDTYNYRFIP WDSSKLAVTK EHIEKGFPYV TYFTRKVYKQ DVKDLIIKKL LHQ
//
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