FUT8_XENTR
ID FUT8_XENTR Reviewed; 578 AA.
AC Q6NVP8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase;
DE Short=Alpha1-6FucT;
DE EC=2.4.1.68;
DE AltName: Full=GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase;
DE AltName: Full=GDP-fucose--glycoprotein fucosyltransferase;
DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase;
GN Name=fut8;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the
CC first GlcNAc residue, next to the peptide chains in N-glycans.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP +
CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-
CC [alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein];
CC Xref=Rhea:RHEA:12985, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13532,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137207; EC=2.4.1.68;
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 Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00992}.
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DR EMBL; BC067957; AAH67957.1; -; mRNA.
DR RefSeq; NP_001001232.1; NM_001001232.2.
DR RefSeq; XP_012825727.1; XM_012970273.2.
DR AlphaFoldDB; Q6NVP8; -.
DR SMR; Q6NVP8; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR PaxDb; Q6NVP8; -.
DR DNASU; 407913; -.
DR Ensembl; ENSXETT00000016641; ENSXETP00000016641; ENSXETG00000007644.
DR GeneID; 407913; -.
DR KEGG; xtr:407913; -.
DR CTD; 2530; -.
DR Xenbase; XB-GENE-954943; fut8.
DR eggNOG; KOG3705; Eukaryota.
DR HOGENOM; CLU_021940_1_0_1; -.
DR InParanoid; Q6NVP8; -.
DR OMA; TYCAITA; -.
DR OrthoDB; 1290594at2759; -.
DR PhylomeDB; Q6NVP8; -.
DR TreeFam; TF106108; -.
DR Reactome; R-XTR-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007644; Expressed in heart and 12 other tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046921; F:alpha-(1->6)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0046368; P:GDP-L-fucose metabolic process; ISS:UniProtKB.
DR GO; GO:0036071; P:N-glycan fucosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR CDD; cd11792; SH3_Fut8; 1.
DR InterPro; IPR015827; Fut8.
DR InterPro; IPR045573; Fut8_N_cat.
DR InterPro; IPR035653; Fut8_SH3.
DR InterPro; IPR027350; GT23_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF19745; FUT8_N_cat; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000472; Alpha1_6FUT_euk; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51659; GT23; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; SH3 domain; SH3-binding; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000357043"
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..578
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 209..496
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 505..566
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 368..369
FT /note="Important for donor substrate binding"
FT MOTIF 302..308
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT DISULFID 207..269
FT /evidence="ECO:0000250"
FT DISULFID 215..233
FT /evidence="ECO:0000250"
FT DISULFID 221..225
FT /evidence="ECO:0000250"
FT DISULFID 468..475
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 66685 MW; C161502A464C38EE CRC64;
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNENPDHSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGPIEQGAAA GRIRALEEQL LKAKEQIEMY KQQSSNAVSG LGKDHEILRR
AIENGAKEFW YFVQSEVKKL KHLDRNELQR HVDEIIIDMG HQQRSVMTDL YYLSQTDGAG
DWREREAKDL TDLVQRRITY LQNPKDCSKA KKLVCNINKG CGYGCQLHHV VYCFMIAYGT
QRTLILESQS WRYATGGWET VFKPVSETCT DRSGSSTGHW SGEANDKNVQ VVELPIVDSL
HPRPPYLPLG VPEDLADRLI RLHGDPAVWW VSQFVKYLIR PQPWLEKEIE ESTKKLGFKH
PVIGVHVRRT DKVGTEAAFH PIEEYMVHVE EHFQLLARRM QIDKKRVYLA TDDPTLLQEA
KAKYPQYEFI SDNSISWSAG LHNRYTENSL RGVILDIHFL SQADFLVCTF SSQVCRVAYE
IMQTLHPDAS AHFHSLDDIY YFGGQNAHNQ LAIYPHQPRN AEEIPLEPGD IIGVAGNHWD
GYSKGINRKL GRTGLYPSYK VKEKIETVKY PTYQEAEK
