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UniProt functional annotation for Q9Y231 | ||
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| UniProt code: Q9Y231. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth (PubMed:23263199, PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574, PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078, PubMed:16282604). Also fucosylates di-, tri- and tetraantennary N- glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (PubMed:11278338, PubMed:12107078, PubMed:18395013). Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (PubMed:18395013, PubMed:23192350). {ECO:0000269|PubMed:10386598, ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:16282604, ECO:0000269|PubMed:17335083, ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23000574, ECO:0000269|PubMed:23192350, ECO:0000269|PubMed:23263199}. |
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| Catalytic activity: | |
Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L- fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941; EC=2.4.1.152; Evidence={ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23192350, ECO:0000269|PubMed:23263199}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258; Evidence={ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23192350}; |
| Catalytic activity: | |
Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)- N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D- GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:136545, ChEBI:CHEBI:139509; Evidence={ECO:0000269|PubMed:11278338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077; Evidence={ECO:0000269|PubMed:11278338}; |
| Catalytic activity: | |
Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)- N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N- acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D- glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = alpha-N- glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta- D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl- (1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)- beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48388, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90383, ChEBI:CHEBI:90384; Evidence={ECO:0000250|UniProtKB:O88819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48389; Evidence={ECO:0000250|UniProtKB:O88819}; |
| Catalytic activity: | |
Reaction=alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl- beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl- (1<->1')-ceramide + GDP-beta-L-fucose = a neolactoside IV(3)-alpha- Gal,III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48380, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90380, ChEBI:CHEBI:90381; Evidence={ECO:0000250|UniProtKB:O88819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48381; Evidence={ECO:0000250|UniProtKB:O88819}; |
| Catalytic activity: | |
Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48376, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90376, ChEBI:CHEBI:90379; Evidence={ECO:0000250|UniProtKB:O88819}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377; Evidence={ECO:0000250|UniProtKB:O88819}; |
| Activity regulation: | |
Activated by Mn2+. {ECO:0000269|PubMed:18395013}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.61 mM for N-acetyllactosamine {ECO:0000269|PubMed:23263199}; KM=2.6 uM for GDP-fucose {ECO:0000269|PubMed:23263199}; |
| Pathway: | |
Protein modification; protein glycosylation. |
| Subcellular location: | |
Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18395013}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O88819}. |
| Tissue specificity: | |
Strongly expressed in forebrain and stomach, lower expression in spleen and peripheral blood leukocytes, and no expression in small intestine, colon, liver, lung, kidney, adrenal cortex or uterus (PubMed:10386598). Highly expressed in granulocytes. Not expressed in monocytes (PubMed:11278338). {ECO:0000269|PubMed:10386598, ECO:0000269|PubMed:11278338}. |
| Ptm: | |
N-glycosylated with complex-type N-glycans. {ECO:0000269|PubMed:18395013}. |
| Similarity: | |
Belongs to the glycosyltransferase 10 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.