ID F6QQR0_XENTR Unreviewed; 922 AA.
AC F6QQR0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Xylosyltransferase 1 {ECO:0000256|ARBA:ARBA00015604};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE AltName: Full=Peptide O-xylosyltransferase 1 {ECO:0000256|ARBA:ARBA00030536};
DE AltName: Full=Xylosyltransferase I {ECO:0000256|ARBA:ARBA00032285};
GN Name=xylt1 {ECO:0000313|Ensembl:ENSXETP00000042631};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000042631};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000042631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000042631};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000042631}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000256|ARBA:ARBA00010195}.
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DR AlphaFoldDB; F6QQR0; -.
DR Ensembl; ENSXETT00000042631; ENSXETP00000042631; ENSXETG00000019693.
DR AGR; Xenbase:XB-GENE-949399; -.
DR Xenbase; XB-GENE-949399; xylt1.
DR eggNOG; KOG0799; Eukaryota.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; F6QQR0; -.
DR TreeFam; TF315534; -.
DR Reactome; R-XTR-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Bgee; ENSXETG00000019693; Expressed in spleen and 7 other cell types or tissues.
DR ExpressionAtlas; F6QQR0; baseline.
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; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025:SF2; XYLOSYLTRANSFERASE 1; 1.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF12529; Xylo_C; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 576..756
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 39..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 105595 MW; 7059D7A5CB5D35EA CRC64;
MVTASIPRRL ARRSRTAIVA ALTVLLIQTL IVWNFSNLDS GDEQRAGGGG SSSREKRDRG
SDKDDLGLGH EQQEQQHRRE PAPGAQQHSQ AMNGYFSHRP KEKQRTDSNN ENSVPKDFEN
IDNSNFAPRT QRHKYQTELM KKPVSKQKEH IKRKLALEAK VKENSLLGKT SNEVLHYVGN
TSKNTSNSNL KDSYKSSKSH HTKKSGSSSP EIKYELPPKC EITGKEAISA LSRAKSKQCR
QEIAEVYCQH KQGKLMPEKV TRLCPLEGKS SNNVQWDDDS VEYPTVNPVR IAFVLVVHGR
ASRQLQRMFK AIYHKDHYYF IHCDKRSHYL HRQVLQFASQ YPNVRVTSWR MSTIWGGASL
LSTYLQSMRD LLEMSDWSWD FFINLSAADY PVRTNDQLVA FLSRYRNMNF LKSHGRDNAR
FIRKQGLDRL FLECDTHMWR LGDRKIPEGI NVDGGSDWFL LNRKFVEYVT FSNDDLVTKM
KQFYSYTLLP AESFFHTVLE NSPYCDTMVD NNLRITNWNR KLGCKCQYKH IVDWCGCSPN
DFKPSDFHRF QQTSRPTFFA RKFEAVVNQE IIGQLDYYLY GNYPSGTPGL RSYWENLYDE
PDGIHSISDV MLTMFHAFSH MGLKRAESSL HTDGENTCRY YPMGHPVSVH LYFLADRFQG
FLIKHHATNL AVSKLETLET WVMPKKVFKI ANPTSDFGRL QFSEVGTEWD AKERIFRNFG
GLMGPMDEPI AMQKWGKGPN ITITVVWIDP INVIAATYDI LIESTAEYTH YKPPLNLPLR
PGVWTIRILH HWVPVAETKF LITPLTFSNR QPIKQEELAK FHGGPPKNAY MEQSFQGLNP
VLNIPVNTAQ VEEARKNAAL VGAKLENLVD SLTSSMWSAV DICTTGPSSC PVMQSCAQTA
WSSLSPDPKS ELGLVKHDGR LR
//
