ID   FUT10_XENLA             Reviewed;         469 AA.
AC   Q6NTZ6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Alpha-(1,3)-fucosyltransferase 10;
DE            EC=2.4.1.-;
DE   AltName: Full=Fucosyltransferase X;
DE            Short=Fuc-TX;
DE            Short=FucT-X;
DE   AltName: Full=Galactoside 3-L-fucosyltransferase 10;
DE            Short=Fucosyltransferase 10;
GN   Name=fut10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable fucosyltransferase. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH68806.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC068806; AAH68806.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001084663.1; NM_001091194.1.
DR   AlphaFoldDB; Q6NTZ6; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   PRIDE; Q6NTZ6; -.
DR   DNASU; 414623; -.
DR   GeneID; 414623; -.
DR   CTD; 414623; -.
DR   Xenbase; XB-GENE-976925; fut10.L.
DR   OrthoDB; 551308at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 414623; Expressed in muscle tissue and 18 other tissues.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11660; -; 1.
DR   InterPro; IPR017176; Alpha-1_3-FUT_met.
DR   InterPro; IPR031481; Glyco_tran_10_N.
DR   InterPro; IPR001503; Glyco_trans_10.
DR   InterPro; IPR038577; GT10-like_C_sf.
DR   PANTHER; PTHR11929; PTHR11929; 1.
DR   Pfam; PF17039; Glyco_tran_10_N; 1.
DR   Pfam; PF00852; Glyco_transf_10; 1.
DR   PIRSF; PIRSF037332; Alpha1_3FUT_met; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..469
FT                   /note="Alpha-(1,3)-fucosyltransferase 10"
FT                   /id="PRO_0000299007"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..469
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  55051 MW;  079524AB1E9996AE CRC64;
     MVNRIWEKRF WISCFFIIFL FILVIFQVMV ELGRFEKKET KSSTVINIQK QKKPLLKEQS
     NSRLRHFKDN YPIMLWWSPL TGENGRLGQC GTDTCFFTIN RTYLQDPMTK AILFYGTDFN
     IDSLPLPRKS SHEWALFHEE SPKNNYKLFH EPAITLFNHT ATFSRHSHMP LTSQYLEGLQ
     ALKSTDYLVS VEKKNVLRKR LSPLAYVQSD CDPPSDRDTY VQELMKYIAV DSYGECLHNK
     DLPQQVNNPS FMDDSQFHHI LGQYKFILAF ENAVCEDYIT EKLWRPLKLG AVPVYFGAPN
     VEDWLPSNKS AIIVSRFSHP KDLAAYIKKL DKNDTLYMQF IEWKLHGNIN NKRLVSAITE
     RKWGVQDVTQ DNYIDAFECM VCKRVCENVR LKEQGPSTKL WNADSAHLNC PAPEVFSFLP
     VHSPKSSMRE MWKPSFEQSK KEAKALRTLV ERNRNFTTVE FWNLVFKFW