ID C3YJA0_BRAFL Unreviewed; 851 AA.
AC C3YJA0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=BRAFLDRAFT_93129 {ECO:0000313|EMBL:EEN59598.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN59598.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN59598.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN59598.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; GG666519; EEN59598.1; -; Genomic_DNA.
DR RefSeq; XP_002603587.1; XM_002603541.1.
DR AlphaFoldDB; C3YJA0; -.
DR STRING; 7739.C3YJA0; -.
DR eggNOG; KOG0799; Eukaryota.
DR InParanoid; C3YJA0; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
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; 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 CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR018711; NAGPA.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR043538; XYLT.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR PANTHER; PTHR46025:SF3; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 2.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF09992; NAGPA; 1.
DR SMART; SM00042; CUB; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 790..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..607
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 615..733
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 739..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 95383 MW; 83BE4128FDB5C476 CRC64;
MEEDYFLHGR TPVRIAFVMV VHGRAIRQVK RLLKAIYHQD HYYLIHVDKR SHYLHRELQE
AFRPYHNIRF TTWRMSTIWG GASLLQMLLR CMNDLRAMYD WKWDFFINLS GTDYPTKFIK
KQGLDRVFYE CDTHMWRLGD RKIPEGILID GGSDWVALNR AFCDYVTSSD DELVTSLKHF
YKYTLLPAES FFHTVLENSA MCLSMVDNNL RITNWNRKLG CKCQYKHIVD WCGCSPNDFK
PDDFHKLQCY RSLDDDLLLP FPSFEEWPRH SHRHVRDCQP NIFGNATHET FPAHSSLHTT
ATSTTRYFVT KVVDSLENVK NGYGHYTVIN NPLRTFSVVE PGGSNGCMEP RRRTVTQTSQ
TRTCHVALNA GFFDTRTGAC LGNVVTDGQR VQDSGGIQNA NFGIRKDGTI VVGYLSEQDV
LREDNPFVQL VSGVIWLVRN ATVYVNESRT TECADIQETG TLDRFVNVVS ARTAVGHDEE
GRVVLVHIEG QTGDRGTQSR STIETDDHPA PYPLEPCTWT LEVRQSSVVL LTFNTFDVWP
WTTRGCTGDS VTIIDGASNG TKLGTCEFCG QVLPPAFVST GNTMTVIMKV GNYRNSFTGF
SATFRPAQPD LDSGCNDLSS WTESSRGAIA SMFYGTENYV NDAYCRWTIT VVTGKSIRLT
FPRSFEVDVA LGCSGADNLK VSANGVEIGT YCGSSKANTG PADILSCFHE MTVEFSTDSA
GTSPGFIAEF FEIADASRRM STASTRREPT TASPTTTSMA PTTIPVSTST VTTSAGRNPI
PHPKPSVQSW IVPTVVGGVL LAVILIITCC CIQYCGEDDC EDESRVYEQS ETVNQRQNSN
EIQIIMISNI R
//