ID   FUT10_CANLF             Reviewed;         478 AA.
AC   Q5F2N4;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Alpha-(1,3)-fucosyltransferase 10;
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:Q5F2L2, ECO:0000250|UniProtKB:Q6P4F1};
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martinez-Duncker I., Oriol R., Mollicone R.;
RT   "Phylogeny of fucosyltransferases.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Predominantly fucosylates the innermost N-acetyl glucosamine
CC       (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to
CC       generate core alpha(1->3)-fucose epitope within the chitobiose unit of
CC       biantennary N-glycans, providing for a recognition signal to reorient
CC       aberrantly folded glycoproteins for degradation (By similarity).
CC       Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that
CC       regulate neuron stem cell self-renewal during brain development (By
CC       similarity). {ECO:0000250|UniProtKB:Q5F2L2,
CC       ECO:0000250|UniProtKB:Q6P4F1}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q6P4F1}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6P4F1}; Single-pass type II membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6P4F1};
CC       Single-pass type II membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ879585; CAI52075.1; -; mRNA.
DR   RefSeq; NP_001012665.1; NM_001012647.1.
DR   AlphaFoldDB; Q5F2N4; -.
DR   STRING; 9615.ENSCAFP00000009503; -.
DR   CAZy; GT10; Glycosyltransferase Family 10.
DR   PaxDb; Q5F2N4; -.
DR   PRIDE; Q5F2N4; -.
DR   GeneID; 503548; -.
DR   KEGG; cfa:503548; -.
DR   CTD; 84750; -.
DR   eggNOG; KOG2619; Eukaryota.
DR   InParanoid; Q5F2N4; -.
DR   OrthoDB; 551308at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0008417; F:fucosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0036071; P:N-glycan fucosylation; ISS:UniProtKB.
DR   GO; GO:0036445; P:neuronal stem cell division; ISS:UniProtKB.
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   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..478
FT                   /note="Alpha-(1,3)-fucosyltransferase 10"
FT                   /id="PRO_0000299001"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..478
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   478 AA;  56055 MW;  CBA12798326D06AA CRC64;
     MVWIQRRRLL ASCLCITATV FLLVTLQVVV ELGKFERKKF KNSDLRAGHA KMEEEPVHLY
     PLPGKEALIL KRKNQLETDS YPIMLWWSPL TGETGRLGQC GADECFFTIN RTYLHHPMTK
     AFLFYGTDFN IDSLPLPRKA HHDWALFHEE SPKNNYKLFH KPVITLFNYT ATFSRHSHLP
     LTTQYLEGVE VLKSLRYLVP LRSKNNLRRR LAPLVYIQSD CDPPSDRDSY VRELMTYIEV
     DSYGECLRNK DLPQQLKNPA SMDADGFYRI IAQYKFILAF ENAVCDDYIT EKFWRPLKLG
     VVPVYYGSPS IADWLPSNRS AILVSEFAHP RELANYIRQL DHDDRMYEAY IEWKLKGEVS
     NQRLLTALRE RKWGVQDVHQ DNYIDAFECM VCTKVWDNIR LQEKGLPPKR WKADVSHLSC
     PEPAVFAFSP LAPRWSSLRE MWIPSFEQSK KEAQALRWLV DRNKNFSAQE FWALVFKD