ID   Q8AXS7_XENLA            Unreviewed;       578 AA.
AC   Q8AXS7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Alpha-(1,6)-fucosyltransferase {ECO:0000256|ARBA:ARBA00018201, ECO:0000256|PIRNR:PIRNR000472};
DE            EC=2.4.1.68 {ECO:0000256|ARBA:ARBA00012660, ECO:0000256|PIRNR:PIRNR000472};
GN   Name=fut8.L {ECO:0000313|Xenbase:XB-GENE-6254427};
GN   Synonyms=fut8 {ECO:0000313|EMBL:CAD55853.1};
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 {ECO:0000313|EMBL:CAD55853.1};
RN   [1] {ECO:0000313|EMBL:CAD55853.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Oriol R.;
RL   Submitted (OCT-2002) 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:0000256|PIRNR:PIRNR000472}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=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-GlcNAc-(1->4)-
CC         beta-D-GlcNAc}-L-asparaginyl-[protein] + GDP-beta-L-fucose = an
CC         N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-
CC         Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein] + GDP + H(+);
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         Evidence={ECO:0000256|PIRNR:PIRNR000472};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|PIRNR:PIRNR000472}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004447}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC       {ECO:0000256|ARBA:ARBA00096265, ECO:0000256|PIRNR:PIRNR000472,
CC       ECO:0000256|PROSITE-ProRule:PRU00992}.
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DR   EMBL; AJ514872; CAD55853.1; -; mRNA.
DR   RefSeq; NP_001081102.1; NM_001087633.1.
DR   AlphaFoldDB; Q8AXS7; -.
DR   GeneID; 394383; -.
DR   KEGG; xla:394383; -.
DR   AGR; Xenbase:XB-GENE-6254427; -.
DR   CTD; 394383; -.
DR   Xenbase; XB-GENE-6254427; fut8.L.
DR   OrthoDB; 2014825at2759; -.
DR   UniPathway; UPA00378; -.
DR   Bgee; 394383; Expressed in kidney and 19 other cell types or tissues.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046921; F:alpha-(1->6)-fucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd11300; Fut8_like; 1.
DR   CDD; cd11792; SH3_Fut8; 1.
DR   FunFam; 1.10.287.1060:FF:000003; Alpha-(1,6)-fucosyltransferase; 1.
DR   FunFam; 2.30.30.40:FF:000070; Alpha-(1,6)-fucosyltransferase; 1.
DR   FunFam; 3.40.50.11350:FF:000001; Alpha-(1,6)-fucosyltransferase; 1.
DR   Gene3D; 3.40.50.11350; -; 1.
DR   Gene3D; 1.10.287.1060; ESAT-6-like; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR13132; ALPHA- 1,6 -FUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR13132:SF29; ALPHA-(1,6)-FUCOSYLTRANSFERASE; 1.
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; SH3-domain; 1.
DR   PROSITE; PS51659; GT23; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000472-52};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|PIRNR:PIRNR000472};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR000472};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000472};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000472};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          209..496
FT                   /note="GT23"
FT                   /evidence="ECO:0000259|PROSITE:PS51659"
FT   DOMAIN          505..566
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          368..369
FT                   /note="Important for donor substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-50,
FT                   ECO:0000256|PROSITE-ProRule:PRU00992"
FT   COILED          43..103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           302..308
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-51"
FT   DISULFID        207..269
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT   DISULFID        215..233
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT   DISULFID        221..225
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
FT   DISULFID        468..475
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000472-52"
SQ   SEQUENCE   578 AA;  66579 MW;  2741A03BDB3C5265 CRC64;
     MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNENPDHSS RELSKILAKL ERLKQQNEDL
     RRMAESLRIP EGPIEQGAAA GRIRALEEQL LKAKEQIEMY KQQSSNAVSG LGKDHEILRR
     AIENGAKEFW YLVQSEVKKL KHLDRNELQR HVDEILIDMG HQQRSVMTDL YYLSQTDGAG
     DWREREAKDL TDLVQRRITY LQNPKDCSKA KKLVCNINKG CGYGCQLHHV VYCFMIAYGT
     QRTLILESQS WRYATGGWET VFKPVSETCT DRSGSSTGHW AGEANDKNVQ VVELPIVDSL
     HPRPPYLPLG VPEDLADQLI RLHGDPAVWW VSQFVKYLIR PQPWLEKEIE EATKKLAFKH
     PVIGVHVRRT DKVGTEAAFH PIEEYMVHVE EHFQLLARRM QIDKKRVYLA TDDPTLLQEA
     KAKYPQYEFI SDNSISWSAG LHNRYTENSL RGVILDIHFL SQANFLVCTF SSQVCRVAYE
     IMQTLHPDAS AYFHSLDDIY YFGGQNANNQ VAIYPHQPRN ADEIPLEPGD IIGVAGNHWD
     GYSKGINRKL GRTGLYPSYK VKEKIETVKY PTYQEAEK
//