FUT8_RAT
ID FUT8_RAT Reviewed; 575 AA.
AC Q6EV76;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Martinez-Duncker I., Oriol R., Mollicone R.;
RT "Phylogeny of fucosyltransferases.";
RL Submitted (JUL-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; AJ781406; CAH03674.1; -; mRNA.
DR RefSeq; NP_001002289.1; NM_001002289.1.
DR AlphaFoldDB; Q6EV76; -.
DR SMR; Q6EV76; -.
DR STRING; 10116.ENSRNOP00000011220; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR iPTMnet; Q6EV76; -.
DR PhosphoSitePlus; Q6EV76; -.
DR PaxDb; Q6EV76; -.
DR PRIDE; Q6EV76; -.
DR GeneID; 432392; -.
DR KEGG; rno:432392; -.
DR UCSC; RGD:1303096; rat.
DR CTD; 2530; -.
DR RGD; 1303096; Fut8.
DR eggNOG; KOG3705; Eukaryota.
DR InParanoid; Q6EV76; -.
DR OrthoDB; 1290594at2759; -.
DR PhylomeDB; Q6EV76; -.
DR Reactome; R-RNO-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6EV76; -.
DR Proteomes; UP000002494; 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:0046921; F:alpha-(1->6)-fucosyltransferase activity; ISO:RGD.
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:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0046368; P:GDP-L-fucose metabolic process; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0036071; P:N-glycan fucosylation; ISO:RGD.
DR GO; GO:0006491; P:N-glycan processing; ISO:RGD.
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 GO; GO:0043112; P:receptor metabolic process; ISO:RGD.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
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..575
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000357042"
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..575
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 206..493
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 502..563
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 365..366
FT /note="Important for donor substrate binding"
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 465..472
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 66485 MW; 731EFB6D850B76CC CRC64;
MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY KKQARNGLGK DHELLRRRIE
NGAKELWFFL QSELKKLKHL EGNELQRHAD EILLDLGHHE RSIMTDLYYL SQTDGAGDWR
EKEAKDLTEL VQRRITYLQN PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
LILESQNWRY ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PALLKEAKTK
YSNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ
TLHPDASANF HSLDDIYYFG GQNAHNQIAV YPHKPRTDEE IPMEPGDIIG VAGNHWDGYS
KGVNRKLGKT GLYPSYKVRE KIETVKYPTY PEAEK
