FUT8_PIG
ID FUT8_PIG Reviewed; 575 AA.
AC P79282;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase;
DE Short=Alpha1-6FucT;
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 AltName: Full=GDP-fucose--glycoprotein fucosyltransferase;
DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase;
GN Name=FUT8;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-130; 333-344; 402-415
RP AND 566-575, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=8910378; DOI=10.1074/jbc.271.44.27810;
RA Uozumi N., Yanagidani S., Miyoshi E., Ihara Y., Sakuma T., Gao C.-X.,
RA Teshima T., Fujii S., Shiba T., Taniguchi N.;
RT "Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-beta-D-
RT glucosaminide alpha1-->6fucosyltransferase.";
RL J. Biol. Chem. 271:27810-27817(1996).
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:0000269|PubMed:8910378}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.;
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 -!- TISSUE SPECIFICITY: Highest expression in brain.
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; D86723; BAA13157.1; -; mRNA.
DR RefSeq; NP_999064.1; NM_213899.1.
DR AlphaFoldDB; P79282; -.
DR SMR; P79282; -.
DR STRING; 9823.ENSSSCP00000002478; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR PaxDb; P79282; -.
DR PRIDE; P79282; -.
DR GeneID; 396933; -.
DR KEGG; ssc:396933; -.
DR CTD; 2530; -.
DR eggNOG; KOG3705; Eukaryota.
DR InParanoid; P79282; -.
DR BRENDA; 2.4.1.68; 6170.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; IBA:GO_Central.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:MGI.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycosyltransferase;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW SH3-binding; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..575
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000080529"
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 /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 465..472
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 66229 MW; 0F199D0BC2018F7B CRC64;
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHSDHSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGPIDQGPAS GRVRALEEQF MKAKEQIENY KKQTKNGPGK DHEILRRRIE
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLSDLGHHE RSIMTDLYYL SQTDGAGDWR
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
LALESHNWRY ATGGWETVFR PVSETCTDRS GSSTGHWSGE VKDKNVQVVE LPIVDSVHPR
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI
GVHVRRTDKV GAEAAFHPIE EYTVHVEEDF QLLARRMQVD KKRVYLATDD PALLKEAKTK
YPSYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ
ALHPDASANF RSLDDIYYFG GPNAHNQIAI YPHQPRTEGE IPMEPGDIIG VAGNHWDGYP
KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEADK
