ID M3VVC0_FELCA Unreviewed; 952 AA.
AC M3VVC0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 60.
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:ENSFCAP00000000694.5,
GN ECO:0000313|VGNC:VGNC:67125};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000000694.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000000694.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000000694.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000000694.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000000694.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000000694.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000000694.5};
RG Ensembl;
RL Submitted (SEP-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=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 EMBL; AANG04001668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VVC0; -.
DR STRING; 9685.ENSFCAP00000000694; -.
DR PaxDb; 9685-ENSFCAP00000000694; -.
DR Ensembl; ENSFCAT00000000748.5; ENSFCAP00000000694.5; ENSFCAG00000000748.5.
DR VGNC; VGNC:67125; XYLT1.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000157381; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; M3VVC0; -.
DR OMA; HWDFVIN; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000000748; Expressed in brain and 9 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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: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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 607..785
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 41..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 106910 MW; 0A3D71AC0F5BA754 CRC64;
MVAAPCARRL ARRSHSALLA ALTVLLLQTL VVWNFSSLDS GAGERRGGAA AGGAEQAAPR
RERRDLPAGP AAARGGGGGG GGGGGRGPPA RARGGGPGEP RAQQPASRGA LPARALDPHP
SPPITLETQD GYFSHRPKEK VRTDSNNENS VPKDFENVDN SNFAPRTQKQ KHQPELAKKA
PSRQKELLKR KLEEEKGKGH PFPGKGTNEV LPPGEKAAVN GSRGKDVPRQ PHSRKSGGSS
PEIKYDQPPK CDISGKEAIS ALSRAKSKHC RQEIGETYCR HKLGLLMPKK VTRFCPLEGK
ANKNVQWDED SVEYMLANPV RIAFVLVVHG RASRQLQRMF KAIYHKDHFY YIHVDKRSNY
LHRQVLQFAR QYDNVRVTPW RMATIWGGAS LLSTYLQGMR DLLEMTDWPW DFFINLSAAD
YPIRTNDQLV AFLSRYRDMN FLKSHGRDNA RFIRKQGLDR LFLECDAHMW RLGDRRIPEG
IAVDGGSDWF LLNRKFVEYV TFSTDDLVTK MKQFYSYTLL PAESFFHTVL ENSPHCDTMV
DNNLRITNWN RKLGCKCQYK HIVDWCGCSP NDFKPQDFHR FQQTARPTFF ARKFEAVVNQ
EIIGQLDYYL YNYPAGTPGL RSYWENVYDE PDGTHSLSDV ALTLYHSFAR LGLRRAESSL
HVEGENSCRY YPMGHPASVH LYFLADRFQG FLIKHHATNL AVSKLETLET WVMPKKVFKI
ASPPSDFGRL QFSEVGTDWD AKERLFRNFG GLLGPMDEPV GMQKWGKGPN VTVTVIWVDP
VNIIAATYDI LIESTAEFTH YKPPLNLPLR PGVWTVKILH HWVPVAETKF LVAPLTFSNR
QPIKPEEALR LHNGPLRSAY MEQSFQSLNP VLSLPISPAQ VEQARRNAAT AGAGLERWLD
SLVGGMWAAM DICTTGPTAC PVMQTCSQTA WSSFSPDPKS ELGAVKPDGR LR
//
