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Database: UniProt
Entry: K7FK83_PELSI
LinkDB: K7FK83_PELSI
Original site: K7FK83_PELSI 
ID   K7FK83_PELSI            Unreviewed;       818 AA.
AC   K7FK83;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
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:ENSPSIP00000008443.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008443.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000008443.1}
RP   IDENTIFICATION.
RG   Ensembl;
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=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; AGCU01091358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01091367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006123701.1; XM_006123639.2.
DR   AlphaFoldDB; K7FK83; -.
DR   STRING; 13735.ENSPSIP00000008443; -.
DR   Ensembl; ENSPSIT00000008487.1; ENSPSIP00000008443.1; ENSPSIG00000007632.1.
DR   GeneID; 102461402; -.
DR   KEGG; pss:102461402; -.
DR   CTD; 64131; -.
DR   eggNOG; KOG0799; Eukaryota.
DR   GeneTree; ENSGT00940000157381; -.
DR   HOGENOM; CLU_012840_0_0_1; -.
DR   OMA; HWDFVIN; -.
DR   OrthoDB; 4166917at2759; -.
DR   TreeFam; TF315534; -.
DR   UniPathway; UPA00755; -.
DR   UniPathway; UPA00756; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
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; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          472..652
FT                   /note="Xylosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12529"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  94320 MW;  0BD44A4E36DA29D4 CRC64;
     MRTDSNNENS VPKDFENIDN SNFAPRTQRQ KYQPELMKKP LSKQKEHLKK KLEQEEKVKE
     NSLLGKNSNE VLQFSHHAVK NSSSNLKESH RSPRQHHLKK SGNSSPEIRY DQPPKCEISG
     KEAISALSRS KSKHCRREIA EVYCQHKQGK LMPEKVTRFC PLDGKANNNV QWDEDSVEYM
     PANPVRIAFV LVVHGRASRQ LQRMFKAIYH KDHFYYIHVD KRSNYLHRKV LQFASQYPNV
     RITPWRMATI WGGASLLSTY LQSMRDLIEM NDWPWDFFIN LSAADYPIRT NDQLVAFLSR
     YRDMNFLKSH GRDNARFIRK QGLDRLFLEC DTHMWRLGDR KIPEGITLDG GSDWFLLNRK
     FVEYVTFSSD DLVTKMKRFY SYTLLPAKSF FHTVLENSPH CDSMVDNNLR ITNWNRKLGC
     KCQYKHIVDW CGCSPNDFKP ADFHRFQQTT RPTFFARKFE AVVNQEIIGQ LDYYLYGNYP
     SGTPGLRSYW ENIYDEPDGI HSLSDVMLSM FHSFSRLGLR RAETSLHTDG DNSCRYYPMG
     HPVSVQVYFL ADRFQGFLIK HHATNLAVSK LETLETWVMP KKMFKIASPP SDFGRLQFSE
     IGTDWDAKER IFRNFGGLIG PMDEPVGMQK WGKGPNVTVT VIWVDPINVI AATYDILIES
     SAEFTHYKPP LNLPLRPGVW TVKILHHWVP VAETKFLVTP LTFSNKQPIK QEESMKLHSG
     PPKNAYMEQS FQGLNPVLNI PIKAAQVDQA KKNAALIGTK LENWVDTLVS NVWSAVDVCS
     TGPTSCPVMQ ACTQTAWSSL SPDPKSELGP IKPDGRLR
//
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