FUT8_PONAB
ID FUT8_PONAB Reviewed; 574 AA.
AC Q5NVB3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase;
DE EC=2.4.1.68;
DE AltName: Full=Fucosyltransferase 8;
DE AltName: Full=GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase;
DE Short=alpha1-6FucT;
DE AltName: Full=GDP-fucose--glycoprotein fucosyltransferase;
DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase;
GN Name=FUT8;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (DEC-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 -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000250|UniProtKB:Q9BYC5}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00992}.
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DR EMBL; CR926471; CAI30264.1; -; mRNA.
DR AlphaFoldDB; Q5NVB3; -.
DR SMR; Q5NVB3; -.
DR STRING; 9601.ENSPPYP00000006721; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR eggNOG; KOG3705; Eukaryota.
DR InParanoid; Q5NVB3; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Unplaced.
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: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: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 Phosphoprotein; Reference proteome; SH3 domain; SH3-binding; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..574
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000357041"
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..574
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 206..492
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 501..562
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 365..366
FT /note="Important for donor substrate binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT MOTIF 299..305
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTS2"
FT DISULFID 204..266
FT /evidence="ECO:0000250"
FT DISULFID 212..230
FT /evidence="ECO:0000250"
FT DISULFID 218..222
FT /evidence="ECO:0000250"
FT DISULFID 464..471
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 66434 MW; 1554E3D513C9AA6E CRC64;
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDRPDHSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT RKLGFKHPVI
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK
YPNYFISDNS ISWSAGLHNR YTENSLRGVI LDIHFLSQAD FLVCTFSSQV CRVAYEIMQT
LHPDASANFH SLDDIYYFGG QNAHNQIAIY AHQPRTADEI PMEPGDIIGV AGNHWDGYSK
GVNRKLGRTG LYPSYKVREK IETVKYPTYP EAEK
