FUT8_DROME
ID FUT8_DROME Reviewed; 619 AA.
AC Q9VYV5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase;
DE Short=Alpha1-6FucT;
DE EC=2.4.1.68 {ECO:0000269|PubMed:15604090};
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=FucT6; ORFNames=CG2448;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAK92875.1};
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN63649.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Petit D., Picaud F., Dupuy F., Germot A., Julien R., Maftah A.;
RT "Core a3- and a6-fucosyltransferases in Drosophila: characterization and
RT origin of diversity.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP HOMOLOGY.
RX PubMed=11698403; DOI=10.1074/jbc.m107927200;
RA Roos C., Kolmer M., Mattila P., Renkonen R.;
RT "Composition of Drosophila melanogaster proteome involved in fucosylated
RT glycan metabolism.";
RL J. Biol. Chem. 277:3168-3175(2002).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15604090; DOI=10.1093/glycob/cwi028;
RA Paschinger K., Staudacher E., Stemmer U., Fabini G., Wilson I.B.;
RT "Fucosyltransferase substrate specificity and the order of fucosylation in
RT invertebrates.";
RL Glycobiology 15:463-474(2005).
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. The
CC addition is prevented if the GlcNAc residue is already fucosylated.
CC {ECO:0000269|PubMed:15604090}.
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 Evidence={ECO:0000269|PubMed:15604090};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:G5EFE7};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:G5EFE7};
CC Note=May also use Ca(2+). The enzyme has substantial activity without
CC divalent cations. {ECO:0000250|UniProtKB:G5EFE7};
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; AF441264; AAN63649.1; -; mRNA.
DR EMBL; AE014298; AAF48079.1; -; Genomic_DNA.
DR EMBL; AY051451; AAK92875.1; -; mRNA.
DR RefSeq; NP_572740.1; NM_132512.4.
DR AlphaFoldDB; Q9VYV5; -.
DR SMR; Q9VYV5; -.
DR BioGRID; 58529; 3.
DR DIP; DIP-21409N; -.
DR IntAct; Q9VYV5; 2.
DR STRING; 7227.FBpp0073457; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR PaxDb; Q9VYV5; -.
DR PRIDE; Q9VYV5; -.
DR DNASU; 32122; -.
DR EnsemblMetazoa; FBtr0073620; FBpp0073457; FBgn0030327.
DR GeneID; 32122; -.
DR KEGG; dme:Dmel_CG2448; -.
DR CTD; 32122; -.
DR FlyBase; FBgn0030327; FucT6.
DR VEuPathDB; VectorBase:FBgn0030327; -.
DR eggNOG; KOG3705; Eukaryota.
DR GeneTree; ENSGT00530000063737; -.
DR HOGENOM; CLU_021940_1_0_1; -.
DR InParanoid; Q9VYV5; -.
DR OMA; GGQNPHN; -.
DR OrthoDB; 1290594at2759; -.
DR PhylomeDB; Q9VYV5; -.
DR Reactome; R-DME-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 32122; 0 hits in 1 CRISPR screen.
DR ChiTaRS; FucT6; fly.
DR GenomeRNAi; 32122; -.
DR PRO; PR:Q9VYV5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030327; Expressed in oviduct (Drosophila) and 33 other tissues.
DR Genevisible; Q9VYV5; DM.
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; IDA:FlyBase.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion 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 PIRSF; PIRSF000472; Alpha1_6FUT_euk; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51659; GT23; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycosyltransferase; Golgi apparatus; Magnesium; Manganese;
KW Membrane; Metal-binding; Reference proteome; SH3 domain; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..619
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000080530"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..619
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 255..539
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 548..609
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 411..412
FT /note="Important for donor substrate binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT MOTIF 345..351
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT DISULFID 253..315
FT /evidence="ECO:0000250"
FT DISULFID 261..279
FT /evidence="ECO:0000250"
FT DISULFID 267..271
FT /evidence="ECO:0000250"
FT DISULFID 511..518
FT /evidence="ECO:0000250"
SQ SEQUENCE 619 AA; 70206 MW; 691BFD9B5C6557DE CRC64;
MLLVRQLFGA SANSWARALI IFVLAWIGLV YVFVVKLTNT QGQQAAGESE LNARRISQAL
QMLEHTRQRN EELKQLIDEL MSDQLDKQSA MKLVQRLEND ALNPKLAPEV AGPEPESMFE
SAPADLRGWN NVAEGAPNDL EAGVPDHGEF EPSLEYEFTR RRIQTNIGEI WNFFSSELGK
VRKAVAAGHA SADLEESINQ VLLQGAEHKR SLLSDMERMR QSDGYEAWRH KEARDLSDLV
QRRLHHLQNP SDCQNARKLV CKLNKGCGYG CQLHHVVYCF IVAYATERTL ILKSRGWRYH
KGGWEEVFQP VSNSCHDAGT ANTYNWPGKP NTQVLVLPII DSLMPRPPYL PLAVPEDLAP
RLKRLHGDPI VWWVGQFLKY LLRPQPTTRD FLTSGMRNLG WERPIVGVHV RRTDKVGTEA
ACHSVEEYMT YVEDYYRTLE VNGSTVARRI FLASDDAQVI EEARRKYPQY QIIGDPEVAR
MASVSTRYTD TALNGIILDI HLLSMSDHLV CTFSSQVCRV AYEIMQTMYP DAAHRFKSLD
DIYYYGGQNA HNRRVVIAHK PRTHEDLQLR VGDLVSVAGN HWDGNSKGKN TRTNQGGLFP
SFKVEEKVDT AKLPLYAGI
