ID R7TR12_CAPTE Unreviewed; 987 AA.
AC R7TR12;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=protein xylosyltransferase {ECO:0000256|ARBA:ARBA00011972};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
GN ORFNames=CAPTEDRAFT_218838 {ECO:0000313|EMBL:ELT93931.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT93931.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELT93931.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT93931.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP218838}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 -!- 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: 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; AMQN01012504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB309561; ELT93931.1; -; Genomic_DNA.
DR AlphaFoldDB; R7TR12; -.
DR STRING; 283909.R7TR12; -.
DR EnsemblMetazoa; CapteT218838; CapteP218838; CapteG218838.
DR HOGENOM; CLU_302326_0_0_1; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000014760; 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; IPR043538; XYLT.
DR PANTHER; PTHR46025:SF5; PROTEIN XYLOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 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 Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..987
FT /note="protein xylosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008787260"
FT TRANSMEM 935..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 987 AA; 113609 MW; CE5C093B75E2616B CRC64;
MDIYLALALL LSMLTSSRGQ TAEQKELHSS RDSYQRISFN LSSPENLPWT NVVCPKGYFI
SSISYAFNRT AIVDKNKSEF LWDPDIAKLL QLDDVLLKYK EDRTIDLPKS SRDEEFLVRL
IETERRQKSN RAKKRQTTKA NTLEHDHIRE SNRQQSTIHS SPGPNIHFVS SKIDKREYFL
SPSKPRQDWE DVLKSARDNY ERRQRNQSLD IQVAESDFGP CPTLLMCLGY QACVFHLSTE
FCRGDPVPLF RKQLDMNVVC EQDAAFPTRH APHGAEKLYE EVVYLKYDSK LEIPLRQYES
TQIHPVVNKE SEIFDVKCPD VSRAFASGYR GNCTATPSNK DNSSNELWFK LAKSFTTAWG
SYDILRAILE GMEWLLRLGH WDHAIVISGS DLPVRTVGDM MLALAPYRGH SFLGFYDINE
EFSKWNYARD NIWLTCEGFT HSLGSRRSPS NLKSYAATSW SIYARNFISA ILERPRDELF
DKMQWFLQTT FIPDEAFLAT LTHINSSLRQ YVHHWKLYWS KPFVGENIDG LCRHTLHADS
CQGPGILYPQ DVTSLKDQSH HTFFSRKFSA DPEDIARKEV LNIILNDEFG AYLREQTPAA
IMELLIKIAL NKMAAKYSME FKMIQMRNFR SLPRLQSADP GCYWLQRANF NRLHEFFYII
EFEVIDAHGQ KLNARALMAP RHPLRHQCFC DGDLRVLYVS STPSNRDLMN FAYSVPHDPY
SDTLHLAIGL DMANTTLSCS GLKSELIPAR LVNQTIGNKV RSLLEFEILL LSPGGIVECR
KTRVVEHTHG KENPVPEHRH IFFHFEIPCS IREVGYWTVS VSEVNRTSAF VYNATFLVVD
TSEPVDIAQM TGILETLKLQ ITIYAFPTPL PDIITDNWKV ENVAVINEKR HESYYSNVER
DGSIPKAEEH VDQPSNKTLK AHSRQPQKKR TATSWIWITL VVIVILDMFW GDIVGLVEKL
KGRIRRKLSF YALLVVCALA LDKLSHV
//
