ID B3DIV0_DANRE Unreviewed; 867 AA.
AC B3DIV0;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Xylosyltransferase 2 {ECO:0000256|ARBA:ARBA00039683};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE AltName: Full=Xylosyltransferase II {ECO:0000256|ARBA:ARBA00041721};
GN Name=xylt2 {ECO:0000313|RefSeq:NP_001124250.1,
GN ECO:0000313|ZFIN:ZDB-GENE-081022-125};
GN ORFNames=zgc:194562 {ECO:0000313|EMBL:AAI63258.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI63258.1};
RN [1] {ECO:0000313|EMBL:AAI63258.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:NP_001124250.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [4] {ECO:0000313|RefSeq:NP_001124250.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26876635;
RA Gistelinck C., Gioia R., Gagliardi A., Tonelli F., Marchese L., Bianchi L.,
RA Landi C., Bini L., Huysseune A., Witten P.E., Staes A., Gevaert K.,
RA De Rocker N., Menten B., Malfait F., Leikin S., Carra S., Tenni R.,
RA Rossi A., De Paepe A., Coucke P., Willaert A., Forlino A.;
RT "Zebrafish Collagen Type I: Molecular and Biochemical Characterization of
RT the Major Structural Protein in Bone and Skin.";
RL Sci. Rep. 6:21540-21540(2016).
RN [5] {ECO:0000313|RefSeq:NP_001124250.1}
RP IDENTIFICATION.
RG RefSeq;
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000256|ARBA:ARBA00010195}.
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DR EMBL; BC163258; AAI63258.1; -; mRNA.
DR RefSeq; NP_001124250.1; NM_001130778.1.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GeneID; 563446; -.
DR KEGG; dre:563446; -.
DR AGR; ZFIN:ZDB-GENE-081022-125; -.
DR CTD; 64132; -.
DR ZFIN; ZDB-GENE-081022-125; xylt2.
DR OrthoDB; 4166917at2759; -.
DR PhylomeDB; B3DIV0; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000000437; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; 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 InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025:SF1; XYLOSYLTRANSFERASE 2; 1.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF12529; Xylo_C; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B3DIV0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 523..700
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 98652 MW; A4875E6690EC156A CRC64;
MVASTRVQKL LRRYKLVIAA GLTILLVQGL VVWSLRSLEE GEAERKHRRS KLPDHNGQEQ
NLDPAIFDSG ANHGQWRLRQ DQPAVTAIIR RGSRRRNKPP LKDKSFGGPE DGVAVEKVAH
YDPSSSRNFS ETRAGETAKI HLVAPGEPGS VEGAPQVPSS DFVPKCEISG KDALSALHRA
GSRQCRQEIA NIVCQHQAGQ LMPQSLPQFC PQHVISSAVQ HVDFADADLS KVENPVRVVF
VLVVHGRAVR QLKRLLKAIY HKDHFYYIHV DKRSNYMHRE VLKMAELYPN VRATPWRMVT
IWGGASLLKA YLRSMHDLLS MLDWKWDFFI NLSATDFPTR TNDELVAFLS QNRDKNFLKS
HGRENARFIK KQGLDRLFHE CDNHMWRLGE RTIPEGLEVS GGSDWFSLTR KFVEYVVNSQ
DELVTGLKQF YTYALLPAES FFHTVLGNSH MCDTLVDNNL RVTNWNRKLG CKCQYKHIVD
WCGCSPNDFK PSDLIRIQQL TRPTFFARKF ESTVNQEAIE ILDNHLYGQY PPGTVALKAY
WESLFEQADG VSSLNDVALT AYSSFFRLGL HRQETSQSSS EACRFEPIGY PMSVHLYFYD
DRFQGYLVRQ EVQNMVTRSR EMLEVWAVPQ ATLQLEHNLH EFERLKHLEV GTEWDPKERI
FRNFGGVMGP LDEPVAVQKW ARGPNLTATI VWIDPAHIVA ASYDISIDVE AEYTQYKPPL
QRPLRPGLWT VRVLRLWERV AEARFLVMPL AFKGREPLRT EDHGWVHAGP PGNVYLEQSF
QQLAHVLKLP PSEPALQEAQ KKTSLVGKPL EAWVDSSVGA FWVTGDTCSE RTSSCPTIGL
CSKTSWSSLS PDPKSELAPV KANGRIR
//
