ID A0A0L7QR74_9HYME Unreviewed; 885 AA.
AC A0A0L7QR74;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=WH47_04394 {ECO:0000313|EMBL:KOC61128.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC61128.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC61128.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC61128.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ414784; KOC61128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7QR74; -.
DR STRING; 597456.A0A0L7QR74; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
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; 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; IPR002889; WSC_carb-bd.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR PANTHER; PTHR46025:SF3; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF01822; WSC; 1.
DR Pfam; PF12529; Xylo_C; 1.
DR SMART; SM00321; WSC; 1.
DR PROSITE; PS51212; WSC; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOC61128.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..234
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT REGION 51..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 101967 MW; E93B9A70BFD673C1 CRC64;
MVITKNHSIS RPSSCLRKYR ILFVFGITVL CVQIYLAHTF FGLEIRNHKS NRLSSGEDSS
QPEEDEGLPT GLRQLKLPPD KHSNSNKILH SQRNRTTRIK LDRKSLNFTP LCEFTGREAG
LLYPERIQSL CPHSPGFIDK PVSLGCFKDD KTLRILSGYY HVFKGNNSPE RCAFLCLQSG
YLYAGTEYSV ECFCGMEKPS QLKRLPDSSC NMKCSGNPKY SCGGYLTINI FWTGIQRFKA
QEARNTSIDI ENEKPARIAY LLTVNGRASR QVKRLISILY HPSHLFYIHV DARQDYLYRD
MLEVEKSCKS NNIKVARGEN LRHASIWGGA SLLTTLLKSA QQMLTHHHHW DFLVNLSESD
FPIKNNAQLT QFLSLNKGMN FVKSHGREVQ RFITKQGLDK TFVECETRMW RTGDRKLPDG
IQIDGGSDWV ALSREFVEYV ANPIPDALVT DLLKVFKYTL LPAESFFHTV LRNSRFCNTY
IDNNLHVTNW KRKLGCKCQY KAVVDWCGCS PNDFKLEDFS RIRNTVDRNL FFARKFESVI
DQRIIDRVEE WLYPEKLNKT VSAKGYDAYW QSLYHTADLS PLTDDAQLTV SNSLARLIFR
KLNIDSKDVH LLETTAYFKQ NQFVGILILA EAIIQQKSIQ QEYMKQVESL IYLRHNFSTS
REWLGKVQSL SVNTDYDQKE KTFRNLMGSI GPYSHPVLSY EFDTGITTPQ NLSILWVDPY
GQLADVNYVQ LEEMTLTGYV KPQFNEHLVV GTWHLLLVAD SLLVAKMNFL VTPLGYWKNK
KMDAAKAKEV NNASGDNYHI TEEMNTKWSH LLSSINFHER TIDITRDDIK INSNLDQWID
KLVHEHYKID KICNADDTIL NLQNCINTYW SSLSPDSKAD INNLC
//
