ID   A0A0M3LHR2_AMBME        Unreviewed;       253 AA.
AC   A0A0M3LHR2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Fucosyltransferase {ECO:0000256|RuleBase:RU003832};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU003832};
DE   Flags: Fragment;
GN   Name=FUT9 {ECO:0000313|EMBL:AIW47104.1};
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296 {ECO:0000313|EMBL:AIW47104.1};
RN   [1] {ECO:0000313|EMBL:AIW47104.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26385618;
RA   Shen X.X., Liang D., Chen M.Y., Mao R.L., Wake D.B., Zhang P.;
RT   "Enlarged Multilocus Dataset Provides Surprisingly Younger Time of Origin
RT   for the Plethodontidae, the Largest Family of Salamanders.";
RL   Syst. Biol. 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC         derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC         fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC         Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC         EC=2.4.1.152; Evidence={ECO:0000256|ARBA:ARBA00029329};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC         Evidence={ECO:0000256|ARBA:ARBA00029329};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside
CC         III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48376,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:90376, ChEBI:CHEBI:90379;
CC         Evidence={ECO:0000256|ARBA:ARBA00036757};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC         Evidence={ECO:0000256|ARBA:ARBA00036757};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-
CC         beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC         (1<->1')-ceramide + GDP-beta-L-fucose = a neolactoside IV(3)-alpha-
CC         Gal,III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48380,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:90380, ChEBI:CHEBI:90381;
CC         Evidence={ECO:0000256|ARBA:ARBA00036053};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48381;
CC         Evidence={ECO:0000256|ARBA:ARBA00036053};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-
CC         N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-
CC         acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC         glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = alpha-N-
CC         glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-
CC         D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-
CC         (1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-
CC         beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48388,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:90383, ChEBI:CHEBI:90384;
CC         Evidence={ECO:0000256|ARBA:ARBA00036295};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48389;
CC         Evidence={ECO:0000256|ARBA:ARBA00036295};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC         N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC         alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC         GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC         Evidence={ECO:0000256|ARBA:ARBA00036481};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC         Evidence={ECO:0000256|ARBA:ARBA00036481};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc
CC         derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC         (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+);
CC         Xref=Rhea:RHEA:77191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:133510, ChEBI:CHEBI:195560;
CC         Evidence={ECO:0000256|ARBA:ARBA00043838};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77192;
CC         Evidence={ECO:0000256|ARBA:ARBA00043838};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC         beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an
CC         alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-
CC         Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP +
CC         H(+); Xref=Rhea:RHEA:68044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:145343, ChEBI:CHEBI:176900;
CC         Evidence={ECO:0000256|ARBA:ARBA00036234};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045;
CC         Evidence={ECO:0000256|ARBA:ARBA00036234};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc
CC         + GDP-beta-L-fucose = beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC         GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP + H(+);
CC         Xref=Rhea:RHEA:77187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:60239, ChEBI:CHEBI:61352;
CC         Evidence={ECO:0000256|ARBA:ARBA00043828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77188;
CC         Evidence={ECO:0000256|ARBA:ARBA00043828};
CC   -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004394}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|RuleBase:RU003832}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU003832}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000256|ARBA:ARBA00037848}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00037848}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC       {ECO:0000256|ARBA:ARBA00008919, ECO:0000256|RuleBase:RU003832}.
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DR   EMBL; KF912774; AIW47104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3LHR2; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008417; F:fucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11660; Glycosyl transferase family 10, C-terminal domain; 1.
DR   InterPro; IPR031481; Glyco_tran_10_N.
DR   InterPro; IPR001503; Glyco_trans_10.
DR   InterPro; IPR038577; GT10-like_C_sf.
DR   PANTHER; PTHR11929:SF10; 4-GALACTOSYL-N-ACETYLGLUCOSAMINIDE 3-ALPHA-L-FUCOSYLTRANSFERASE 9; 1.
DR   PANTHER; PTHR11929; ALPHA- 1,3 -FUCOSYLTRANSFERASE; 1.
DR   Pfam; PF17039; Glyco_tran_10_N; 1.
DR   Pfam; PF00852; Glyco_transf_10; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU003832};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU003832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003832};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003832};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..88
FT                   /note="Fucosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17039"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AIW47104.1"
FT   NON_TER         253
FT                   /evidence="ECO:0000313|EMBL:AIW47104.1"
SQ   SEQUENCE   253 AA;  29749 MW;  C676542F120182CB CRC64;
     CDSLFNIQGC HLTIDRSLYN RSHAVLIHHR DINWDLTNLP QQARPPFQKW IWMNLESPTH
     TPQKSGIEHL FNLTLTYRRD SDIQVPYGFM IVSTNPLEFD VPSKDKLVCW VVSNWNPDHA
     RVKYYNELSK YIAIQTYGQA FGDYLNDKSL IPTISTCKFY LSFENSIHKD YITEKLYNAL
     LAGSVPVVLG PSRENYENYI PADSFIHVDD FLSPRELADY LLMLNEENEM YISLFNWRKY
     YTVNVSQFWE SHA
//