FUCTC_DROME
ID FUCTC_DROME Reviewed; 425 AA.
AC P83088; Q7PLF1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase C;
DE EC=2.4.1.-;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FucTC; ORFNames=CG40305;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=11382750; DOI=10.1074/jbc.m100573200;
RA Fabini G., Freilinger A., Altmann F., Wilson I.B.H.;
RT "Identification of core alpha1,3-fucosylated glycans and cloning of the
RT requisite fucosyltransferase cDNA from Drosophila melanogaster: Potential
RT basis of the neural anti-horseradish peroxidase epitope.";
RL J. Biol. Chem. 276:28058-28067(2001).
RN [2]
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).
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 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ302047; CAC41643.1; -; mRNA.
DR EMBL; AE014298; EAA46057.5; -; Genomic_DNA.
DR RefSeq; NP_001036320.3; NM_001042855.4.
DR AlphaFoldDB; P83088; -.
DR BioGRID; 78296; 1.
DR IntAct; P83088; 1.
DR STRING; 7227.FBpp0289204; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; P83088; 2 sites.
DR PaxDb; P83088; -.
DR EnsemblMetazoa; FBtr0299926; FBpp0289204; FBgn0044872.
DR GeneID; 3355171; -.
DR KEGG; dme:Dmel_CG40305; -.
DR UCSC; CG40305-RB; d. melanogaster.
DR CTD; 3355171; -.
DR FlyBase; FBgn0044872; FucTC.
DR VEuPathDB; VectorBase:FBgn0044872; -.
DR eggNOG; KOG2619; Eukaryota.
DR HOGENOM; CLU_646520_0_0_1; -.
DR InParanoid; P83088; -.
DR OMA; ACTARSK; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; P83088; -.
DR Reactome; R-DME-9037629; Lewis blood group biosynthesis.
DR Reactome; R-DME-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SignaLink; P83088; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 3355171; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3355171; -.
DR PRO; PR:P83088; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0044872; Expressed in adult midgut (Drosophila) and 6 other tissues.
DR ExpressionAtlas; P83088; baseline and differential.
DR Genevisible; P83088; 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:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:FlyBase.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..425
FT /note="Alpha-(1,3)-fucosyltransferase C"
FT /id="PRO_0000221123"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..425
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 425 AA; 49130 MW; 0E037B103ACF2EC1 CRC64;
MYLGRVHCSF EVPGLLSGRV GHMSMAVRSV RLACGPRGAL LLLLLVLLGV LVVLHKVTQS
PLLNQNKILQ DHLRGQHERY IQSTRTILLW TEFFGDSRWK LSWDTLGPQE LRDELHCPVY
QCEISNQNAF LPAVELYDAI VFHAAEMFPL LRPVPSQRSP HQVYVFALME PPGETKHRLD
DEQGFYNLTM TYRIDSDVFW PYGQLLDITA DAVVAPSVKP PWRKPPVAFN DSLVWDLWSG
KTKTAAWFVS HCETLSKREV LANRLQEFFE VDIYGNCGTL SCTRGDPHCA EMLDTDYFFY
LAFENSLCDD YVTEKLFDAL ERTVIPVVFG GADYSRILPP HSYVDANRFM SVEGLAQYMK
LVVADPDLYV SYFWWRSHYR LTYSSPFCDL CARLHDPSFG HKTQFYHDIQ SWWFNSCRLQ
SRIRL